메뉴 건너뛰기




Volumn 15, Issue 1, 1981, Pages 49-127

Polyphenol Oxidase and Peroxidase in Fruits and Vegetables

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOL OXIDASE; ISOENZYME; PEROXIDASE;

EID: 0019741905     PISSN: 00990248     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408398109527312     Document Type: Article
Times cited : (931)

References (498)
  • 1
    • 84952432206 scopus 로고
    • Anon. Enzyme Nomenclature
    • Elsevier, Amsterdam
    • Anon. Enzyme Nomenclature, Elsevier, Amsterdam, 1973.
    • (1973)
  • 2
    • 0017441029 scopus 로고
    • Metabolism of phenolic compounds in plants, Russ., Biokhimiya
    • Zaprometov, N.N. Metabolism of phenolic compounds in plants, (Russ.), Biokhimiya, 42, 3, 1977.
    • (1977) , vol.42 , Issue.3
    • Zaprometov, N.N.1
  • 3
    • 0003514946 scopus 로고
    • Principles of Enzymology for the Food Sciences
    • Marcel Dekker, New York, chaps. 22 and 24.
    • Whitaker, J.R. Principles of Enzymology for the Food Sciences, Marcel Dekker, New York, 1972, chaps. 22 and 24.
    • (1972)
    • Whitaker, J.R.1
  • 4
    • 84952432207 scopus 로고
    • aoeber Oxydationsfermente und phenolische Substrate im Gemase and Obst. III.
    • Catechine, Oxyzimtsauren und o-Polyphenoloxidase im Obst. Z. Lebensm. Unters. Forsch. 108, 152
    • Herrmann, K. aoeber Oxydationsfermente und phenolische Substrate im Gemase and Obst. III. Catechine, Oxyzimtsauren und o-Polyphenoloxidase im Obst. Z. Lebensm. Unters. Forsch. 108, 152, 1958.
    • (1958)
    • Herrmann, K.1
  • 5
    • 0016580526 scopus 로고
    • Enzymic browning in food. A review.
    • Enzyme Technol. Dig. 4(3), 89
    • Walker, J.R.L. Enzymic browning in food. A review. Enzyme Technol. Dig. 4(3), 89, 1975.
    • (1975)
    • Walker, J.R.L.1
  • 6
    • 84952432209 scopus 로고
    • Laccase-like enzyme in peaches, Photochemistry
    • Mayer, A.M. and Harel, E. Laccase-like enzyme in peaches, Photochemistry, 5, 783, 1968.
    • (1968) , vol.5 , Issue.783
    • Mayer, A.M.1    Harel, E.2
  • 7
    • 0000963199 scopus 로고
    • Biochemical aspects of oxidative coupling of phenols
    • in Oxidative Coupling of Phenols, Taylor, A.R. Eds. Marcel Dekker, New York, chap.
    • Brown, B.R. Biochemical aspects of oxidative coupling of phenols, in Oxidative Coupling of Phenols, Taylor, W.I. and Battersby, A.R. Eds. Marcel Dekker, New York, 1967, chap. 4.
    • (1967) , pp. 4
    • Brown, B.R.1    Battersby, W.I.2
  • 8
    • 0016685820 scopus 로고
    • Production of ethylene and other volatiles and changes in cellulase and laccase activities during the life cycle of the cultivated mushroom Agaricus bisporus, J. Gen. Microbiol
    • D.J. and
    • Turner, E.M. Wright, M. Ward, T. Osborne, D.J. and Self, R. Production of ethylene and other volatiles and changes in cellulase and laccase activities during the life cycle of the cultivated mushroom Agaricus bisporus, J. Gen. Microbiol. 91, 167, 1975.
    • (1975) , vol.91 , Issue.167
    • Turner, E.M.1    Wright, M.2    Osborne, T.3    Self, R.4
  • 9
    • 0006985938 scopus 로고
    • Enzyme induction in higher plants, Science
    • Ph. Wray, J.L. and
    • Filner, Ph. Wray, J.L. and Varner, J.E. Enzyme induction in higher plants, Science, 165, 358, 1969.
    • (1969) Filner , vol.165 , Issue.358
    • Varner, J.E.1
  • 10
    • 84952419575 scopus 로고
    • Ricerche suite fenolossidasi e sul contenuto in o-difenoli delle olive, Ann. Chim
    • Ragazzi, E. and Veronese, G. Ricerche suite fenolossidasi e sul contenuto in o-difenoli delle olive, Ann. Chim. 57, 1476, 1967.
    • (1967) , vol.57
    • Ragazzi, E.1    Veronese, G.2
  • 11
    • 84952421293 scopus 로고
    • Activation of polyphenol oxidase of chloroplasts, Plant Physiol
    • Tolbert, N.E. Activation of polyphenol oxidase of chloroplasts, Plant Physiol, 51, 234, 1973.
    • (1973) , vol.51 , Issue.234
    • Tolbert, N.E.1
  • 12
    • 6544263251 scopus 로고
    • Localization and activity of phenolase in the potato tuber, Am. Potato J
    • Craft, C.C. Localization and activity of phenolase in the potato tuber, Am. Potato J. 43, 112, 1966.
    • (1966) , vol.43 , Issue.112
    • Craft, C.C.1
  • 13
    • 0016315259 scopus 로고
    • Release of enzymes from cell walls by an endopectate-trans-eliminase, Nature
    • Stephens, G.J. and Wood, R.K.S. Release of enzymes from cell walls by an endopectate-trans-eliminase, Nature, 251, 358, 1974.
    • (1974) , vol.251 , Issue.358
    • Stephens, G.J.1    Wood, R.K.S.2
  • 14
    • 84952432211 scopus 로고
    • The intracellular location of phenol oxidases and peroxidase in stems of spinach beet Beta vulgaris L., Z. Pflanzenphysiol
    • Parish, R.W. The intracellular location of phenol oxidases and peroxidase in stems of spinach beet (Beta vulgaris L.), Z. Pflanzenphysiol, 66, 176, 1972.
    • (1972) , vol.66 , Issue.176
    • Parish, R.W.1
  • 15
    • 84982374825 scopus 로고
    • Catechol oxidases from apples, their properties, subcellular location and inhibition, Physiol Plant
    • Harel, E. Mayer, A.M. and Shain, Y. Catechol oxidases from apples, their properties, subcellular location and inhibition, Physiol Plant. 17, 921, 1964.
    • (1964) , vol.17 , Issue.921
    • Harel, E.1    Mayer, A.M.2    Shain, Y.3
  • 16
    • 0014081737 scopus 로고
    • aoeber aktiv und latent gebundene Phenoloxidase und ihre AblAsung von pflanzlichen Zellstrukturen, Naturwissenschaften
    • Drawert, F. and Gebblng, H. aoeber aktiv und latent gebundene Phenoloxidase und ihre AblAsung von pflanzlichen Zellstrukturen, Naturwissenschaften, 54, 226, 1967.
    • (1967) , vol.54 , Issue.226
    • Drawert, F.1    Gebblng, H.2
  • 17
    • 0001617027 scopus 로고
    • Latent phenolase in extracts of broad bean Vicia faba L. leaves, 1. Activation by acid and alkali, Biochem. J
    • Kenten, R.H. Latent phenolase in extracts of broad bean (Vicia faba L.) leaves, 1. Activation by acid and alkali, Biochem. J. 67, 300, 1957.
    • (1957) , vol.67 , Issue.300
    • Kenten, R.H.1
  • 18
    • 84952432213 scopus 로고
    • Activity of polyphenol oxidase during the ripening of Cherven muscat, dimyat, riesling and aligote grapes, Lozar. Vinar
    • Ivanov, T.P. Activity of polyphenol oxidase during the ripening of Cherven muscat, dimyat, riesling and aligote grapes, Lozar. Vinar. 15, 24, 1966.
    • (1966) , vol.15 , Issue.24
    • Ivanov, T.P.1
  • 19
    • 84952432214 scopus 로고
    • Localization and solubility of polyphenoloxidase in stone fruits, Nauchni Tr. Vissh. Inst. Khranit. Vkusova Promst
    • Dang, F. Localization and solubility of polyphenoloxidase in stone fruits, Nauchni Tr. Vissh. Inst. Khranit. Vkusova Promst. 18, 241, 1971.
    • (1971) , vol.18 , Issue.241
    • Dang, F.1
  • 20
    • 0012328974 scopus 로고
    • Oxydation in Obst und Obstsaften, Mitt. Geb. Lebensmittelunters. Hyg
    • Biedermann, W. Oxydation in Obst und Obstsaften, Mitt. Geb. Lebensmittelunters. Hyg. 47, 86, 1956.
    • (1956) , vol.47 , Issue.86
    • Biedermann, W.1
  • 21
    • 84952382594 scopus 로고
    • Zur Bestimmung der Polyphenoloxidaseaktivitat. II. Orientierende Versuche zur Anwendbarkeit der Methode mit Besthorns Reagens in a.pfeln, Z. Lebensm. Unters. Forsch
    • Voigt, J. and Noske, R. Zur Bestimmung der Polyphenoloxidaseaktivitat. II. Orientierende Versuche zur Anwendbarkeit der Methode mit Besthorns Reagens in a.pfeln, Z. Lebensm. Unters. Forsch. 130, 9, 1966.
    • (1966) , vol.130 , Issue.9
    • Voigt, J.1    Noske, R.2
  • 22
    • 84952432216 scopus 로고
    • Activity of oxidases in sweet cherries during growth and maturation, Stud. Cercet.
    • Biochim. 12, 47
    • Iliescu-Moruju, E. Activity of oxidases in sweet cherries during growth and maturation, Stud. Cercet. Biochim. 12, 47, 1969.
    • (1969)
    • Iliescu-Moruju, E.1
  • 23
    • 0017497719 scopus 로고
    • Olive catechol oxidase-changes during fruit development, J. Sei. Food Agrie
    • E. and
    • Ben-Shalom, N. Kahn, V. Harel, E. and Mayer, N. Olive catechol oxidase-changes during fruit development, J. Sei. Food Agrie. 28, 545, 1977.
    • (1977) , vol.28 , Issue.545
    • Ben-Shalom, N.1    Harel, V.2    Mayer, N.3
  • 24
    • 84952384898 scopus 로고
    • Banana polyphenoloxidase. Preparation and properties, Plant Physiol
    • Palmer, J.K. Banana polyphenoloxidase. Preparation and properties, Plant Physiol, 38, 508, 1963.
    • (1963) , vol.38 , Issue.508
    • Palmer, J.K.1
  • 25
    • 0000703969 scopus 로고
    • of o-diphenol: 02 oxidoreductase from Musa cavendishii, Phytochemistry
    • Padran, M.P. Lozano, J.A. and Gonzailes, A.G. Properties of o-diphenol: 02 oxidoreductase from Musa cavendishii, Phytochemistry, 14, 1959, 1975.
    • (1975) , vol.14 , pp. 1959
    • Padran, M.P.1    Lozano, J.A.2
  • 29
    • 84952432220 scopus 로고
    • Influence of Alar, Ethrel and gibberellic acid on browning of peaches, HortScience
    • Buchanan, D.W. Hall, C.B. Biggs, R.H. and Knapp, F.W. Influence of Alar, Ethrel and gibberellic acid on browning of peaches, HortScience, 4, 302, 1969.
    • (1969) , vol.4 , Issue.302
    • Buchanan, D.W.1    Hall, C.B.2    Biggs, R.H.3    Knapp, F.W.4
  • 30
    • 84952432221 scopus 로고
    • The effect of Ethrel on the biochemical processes in fruit ripening, Prikt. Biokhim. Mikrobiol
    • A.A. and
    • Sal'kova, E.G. Zvyagintseva, Yu.V. Kuliev, A.A. and Akhundov, R.M. The effect of Ethrel on the biochemical processes in fruit ripening, Prikt. Biokhim. Mikrobiol. 13, 97, 1977.
    • (1977) Yu.V. Kuliev , vol.13 , Issue.97
    • Akhundov, R.M.1
  • 31
    • 84952393702 scopus 로고
    • Soluble oxidases and their functions, Annu. Rev. Plant Physiol
    • Bonner, W.D. Soluble oxidases and their functions, Annu. Rev. Plant Physiol. 8, 427, 1957.
    • (1957) , vol.8 , Issue.427
    • Bonner, W.D.1
  • 32
    • 77049203277 scopus 로고
    • Comparative biochemistry of the phenolase complex, Adv. Enzymol. Ret. Subj. Biochem
    • Mason, H.S. Comparative biochemistry of the phenolase complex, Adv. Enzymol. Ret. Subj. Biochem. 16, 105, 1955.
    • (1955) , vol.16 , Issue.105
    • Mason, H.S.1
  • 33
    • 0013670921 scopus 로고
    • Chlorogenic acids and related depsides, Bot. Rev
    • Sondheimer, E. Chlorogenic acids and related depsides, Bot. Rev. 30, 667, 1964.
    • (1964) , vol.30 , Issue.667
    • Sondheimer, E.1
  • 34
    • 84952432222 scopus 로고
    • and Kiraily, Z. Role of phenolic compounds in the physiology of plant disease resistance, Phytopathol. Z
    • Farkas, G.L. and Kiraily, Z. Role of phenolic compounds in the physiology of plant disease resistance, Phytopathol. Z. 44, 106, 1962.
    • (1962) , vol.44 , Issue.106
    • Farkas, G.L.1
  • 35
    • 84952432223 scopus 로고
    • Biokhimiya ifisiologiya immuniteta rastenii. Izd.
    • Akad. Nauk SSSR, Moscow
    • Rubin, V.A. and Artsikovskaya, E.V. Biokhimiya ifisiologiya immuniteta rastenii. Izd. Akad. Nauk SSSR, Moscow, 1960.
    • (1960)
    • Rubin, V.A.1    Artsikovskaya, E.V.2
  • 36
    • 84985052448 scopus 로고
    • Effect of potato virus X on enzymatic darkening and lipid content of potatoes, J. Food Sei
    • Mondy, N.I. and Koch, R.L. Effect of potato virus X on enzymatic darkening and lipid content of potatoes, J. Food Sei. 43, 703, 1978.
    • (1978) , vol.43 , Issue.703
    • Mondy, N.I.1    Koch, R.L.2
  • 37
    • 0141810428 scopus 로고
    • Ceratocystis infection in sweet potato: its effect on proteins, isozymes and acquired immunity, Science
    • Weber, D.J. and Stahmann, M.A. Ceratocystis infection in sweet potato: its effect on proteins, isozymes and acquired immunity, Science, 146, 929, 1964.
    • (1964) , vol.146 , Issue.929
    • Weber, D.J.1    Stahmann, M.A.2
  • 38
    • 0013074823 scopus 로고
    • Increased disease resistance and enzyme activity induced by ethylene and ethylene production by black rot infected sweet potato tissue, Plant Physiol
    • Stahmann, M.A. Clare, B.G. and Woodbury, W. Increased disease resistance and enzyme activity induced by ethylene and ethylene production by black rot infected sweet potato tissue, Plant Physiol. 41, 1505, 1966.
    • (1966) , vol.41
    • Stahmann, M.A.1    Clare, B.G.2    Woodbury, W.3
  • 39
    • 84916692763 scopus 로고    scopus 로고
    • The inhibitory effect of some antibiotics on increase in o-diphenol oxidase activity during incubation of sliced sweet potato tissue, Agrie. Biol. Chem
    • 1066.
    • Hyodo, H. and Uritani, I. The inhibitory effect of some antibiotics on increase in o-diphenol oxidase activity during incubation of sliced sweet potato tissue, Agrie. Biol. Chem. 30, 1083, 1066.
    • , vol.30
    • Hyodo, H.1    Uritani, I.2
  • 40
    • 84952432225 scopus 로고
    • Peroxidase, polyphenol oxidase and endopolygalacturonate trans-eliminase activity in different tissues of sugar beet infected with Phoma betae. Can.
    • J. Bot. 53, 1347
    • Bugbee, M. Peroxidase, polyphenol oxidase and endopolygalacturonate trans-eliminase activity in different tissues of sugar beet infected with Phoma betae. Can. J. Bot. 53, 1347, 1975.
    • (1975)
    • Bugbee, M.1
  • 41
    • 0039833442 scopus 로고
    • Inhibition of the apple phenolase system through infection by Pacnicillium expansum, Phytochemistry
    • Walker, J.R.L. Inhibition of the apple phenolase system through infection by Pacnicillium expansum, Phytochemistry, 8, 561, 1969.
    • (1969) , vol.8 , Issue.561
    • Walker, J.R.L.1
  • 42
    • 0014954189 scopus 로고
    • Phenolase inhibitor from cultures of Pencillium expansum which may play a part in fruit rotting, Nature
    • Walker, J.R.L. Phenolase inhibitor from cultures of Pencillium expansum which may play a part in fruit rotting, Nature. 227, 298, 1970.
    • (1970) , vol.227 , Issue.298
    • Walker, J.R.L.1
  • 43
    • 84952390271 scopus 로고
    • Relations of phenolic inhibitors to resistance of immature apple fruits to rot, J. Hortic. Sei
    • Ndubizu, T.O.C. Relations of phenolic inhibitors to resistance of immature apple fruits to rot, J. Hortic. Sei. 51, 311, 1976.
    • (1976) , vol.51 , Issue.311
    • Ndubizu, T.O.C.1
  • 44
    • 0342835626 scopus 로고
    • Substrates and inhibitors of potato tuber phenolase, Phytochemistry
    • Macrae, A.R. and Duggleby, R.G. Substrates and inhibitors of potato tuber phenolase, Phytochemistry. 7, 855, 1968.
    • (1968) , vol.7 , Issue.855
    • Macrae, A.R.1    Duggleby, R.G.2
  • 45
    • 0013879268 scopus 로고
    • S-, The enzymic oxidation of chlorogenic acid and some reactions of the quinone produced, Biochem. J
    • Pierpoint, W. S-, The enzymic oxidation of chlorogenic acid and some reactions of the quinone produced, Biochem. J. 98, 567, 1966.
    • (1966) , vol.98 , Issue.567
    • Pierpoint, W.1
  • 46
    • 84952432226 scopus 로고
    • Ya. Certain physiological-biological indicators in the leaves of various frost resistant varieties of plums, Agrobiologya
    • Khrushcheva, E.P. and Krehin, N. Ya. Certain physiological-biological indicators in the leaves of various frost resistant varieties of plums, Agrobiologya, 6, 921, 1965.
    • (1965) , vol.6 , Issue.921
    • Khrushcheva, E.P.1    Krehin, N.2
  • 47
    • 84952432227 scopus 로고
    • Ya. The role of oxidases in the resistance of grapevines to unfavorable conditions of wintering, Vinodel.
    • Vinograd. SSSR, 26(1), 21
    • Molchanova, Z. Ya. The role of oxidases in the resistance of grapevines to unfavorable conditions of wintering, Vinodel. Vinograd. SSSR, 26(1), 21, 1966.
    • (1966)
    • Molchanova, Z.1
  • 48
    • 84952379956 scopus 로고
    • Formation of auxin from tryptophan through action of polyphenols. Plant Physiol
    • Gordon, S.A. and Paleg, L.G. Formation of auxin from tryptophan through action of polyphenols. Plant Physiol. 36, 838, 1961.
    • (1961) , vol.36 , Issue.838
    • Gordon, S.A.1    Paleg, L.G.2
  • 49
    • 84952432228 scopus 로고
    • Zur Frage der Braunungsreaktion in Lebensmitteln, Dtsch. Lebensm. Rundsch
    • Heintze, K. Zur Frage der Braunungsreaktion in Lebensmitteln, Dtsch. Lebensm. Rundsch. 51, 69, 1955.
    • (1955) , vol.51 , Issue.69
    • Heintze, K.1
  • 50
    • 0000082764 scopus 로고
    • Interaction of polyphenols with proteins in plants and plant products, Qual. Plant. Plant Foods Hum. Nutr
    • Synge, R.L.M. Interaction of polyphenols with proteins in plants and plant products, Qual. Plant. Plant Foods Hum. Nutr. 24, 337, 1975.
    • (1975) , vol.24 , Issue.337
    • Synge, R.L.M.1
  • 51
    • 0014404984 scopus 로고
    • Fungal degradation of lignin. II. Degradation of the lignin model compound syringyl-glycol /3-guaiacyl ether by Polyporus versicolor and Stereum frustula-tum, Biochim. Biophys. Acta
    • Kent, K.T. Harkin, J.N. and Cowling, E.B. Fungal degradation of lignin. II. Degradation of the lignin model compound syringyl-glycol /3-guaiacyl ether by Polyporus versicolor and Stereum frustula-tum, Biochim. Biophys. Acta, 165, 145, 1968.
    • (1968) , vol.165 , Issue.145
    • Kent, K.T.1    Harkin, J.N.2    Cowling, E.B.3
  • 52
    • 77956995750 scopus 로고
    • Food browning as a polyphenol reaction, Adv. Food Res
    • Mathew, A.G. and Parpia, H.A.B. Food browning as a polyphenol reaction, Adv. Food Res. 19, 75, 1971.
    • (1971) , vol.19 , Issue.75
    • Mathew, A.G.1    Parpia, H.A.B.2
  • 53
    • 85007928162 scopus 로고
    • Tea leaf polyphenol oxidase. Part III. Studies on the changes of polyphenol oxidase activity during black tea manufacture. Agrie. Biol. Chem
    • Takeo, T. Tea leaf polyphenol oxidase. Part III. Studies on the changes of polyphenol oxidase activity during black tea manufacture. Agrie. Biol. Chem. 30, 529, 1966.
    • (1966) , vol.30 , Issue.529
    • Takeo, T.1
  • 54
    • 84985304736 scopus 로고
    • Browning of sultana grape berries during drying, J. Sei. Food Agrie
    • Grncarevic, M. and Hawker, J.S. Browning of sultana grape berries during drying, J. Sei. Food Agrie. 22, 270, 1971.
    • (1971) , vol.22 , Issue.270
    • Grncarevic, M.1    Hawker, J.S.2
  • 55
    • 84952421114 scopus 로고
    • La polyphacnoloxidase de la prune d'Ente. Modification de son ! activitac au cours de l'aclaboration du pruneau d'Agen, Ann. Technol. Agrie
    • Moutounet, M. and Mondies, H. La polyphacnoloxidase de la prune d'Ente. Modification de son ! activitac au cours de l'aclaboration du pruneau d'Agen, Ann. Technol. Agrie. 25, 343, 1976.
    • (1976) , vol.25 , Issue.343
    • Moutounet, M.1    Mondies, H.2
  • 56
    • 0014432115 scopus 로고
    • Relationship between the polyphenol oxidase activity of coffee beans and the quality of the beverage, Nature
    • De Amorim, H.V. and Silva, D.M. Relationship between the polyphenol oxidase activity of coffee beans and the quality of the beverage, Nature, 219, 381, 1968.
    • (1968) , vol.219 , Issue.381
    • De, H.V.1    Silva, D.M.2
  • 57
    • 84952432231 scopus 로고
    • Les composacs phacnoliques du raisin et du vin. Leurs transformations au cours de l'aclaboration des vins et leurs effets sur la qualitac vins rouges, Bull. OtV
    • Bourzeix, M. Les composacs phacnoliques du raisin et du vin. Leurs transformations au cours de l'aclaboration des vins et leurs effets sur la qualitac (vins rouges), Bull. OtV, 49, 988, 1976.
    • (1976) , vol.49 , Issue.988
    • Bourzeix, M.1
  • 58
    • 84952432232 scopus 로고
    • Study of the color of the crumb of bread from flour of high browning capacity, Khlebopek. Konditer.
    • Promsl. 13(9), 14
    • Lukach, E.N. and Skvarkina, T.I. Study of the color of the crumb of bread from flour of high browning capacity, Khlebopek. Konditer. Promsl. 13(9), 14, 1969.
    • (1969)
    • Lukach, E.N.1    Skvarkina, T.I.2
  • 59
    • 84952432233 scopus 로고
    • Role of biochemical factors in the darkening of pasta products, Khlebopek. Konditer.
    • Promst. 20(10), 34
    • Nazarov, N.I. and Mazanashvili, G.G. Role of biochemical factors in the darkening of pasta products, Khlebopek. Konditer. Promst. 20(10), 34, 1976.
    • (1976)
    • Nazarov, N.I.1    Mazanashvili, G.G.2
  • 60
    • 0000259876 scopus 로고
    • Biological value of proteins allowed to react with phenolic compounds in the presence of o-diphenol oxidase, Agrie. Biol. Chem
    • Horigome, T. and Kandatsu, N. Biological value of proteins allowed to react with phenolic compounds in the presence of o-diphenol oxidase, Agrie. Biol. Chem. 52, 1093, 1968.
    • (1968) , vol.52
    • Horigome, T.1    Kandatsu, N.2
  • 61
    • 84952432235 scopus 로고
    • Effect of polyphenols on digestion of proteins, Proc. 19th Hung.
    • Annu. Meet. Biochem. 223.
    • Szaba, M.T. Effect of polyphenols on digestion of proteins, Proc. 19th Hung. Annu. Meet. Biochem. 1979, 223.
    • (1979)
    • Szaba, M.T.1
  • 62
    • 84952432236 scopus 로고
    • Enzymic colour formation in beet and cane juices. Paper presented at the 15th General Assembly of
    • Gross, D. and Coombs, J. Enzymic colour formation in beet and cane juices. Paper presented at the 15th General Assembly of C.I. T.S. Vienna, 1975.
    • (1975)
    • Gross, D.1    Coombs, J.2
  • 63
    • 84952432237 scopus 로고
    • uber die phenolischen Inhaltsstoffe des Obstes, Erwerbsobstbau
    • Herrmann, K. uber die phenolischen Inhaltsstoffe des Obstes, Erwerbsobstbau, 16, 1, 1974.
    • (1974) , vol.16 , Issue.1
    • Herrmann, K.1
  • 64
    • 85008039143 scopus 로고
    • Anthocyanase and anthrocyanin occurring in the eggplant Solanum melongena. III. Oxidative decolorization of the anthocyanin by polyphenol oxidase, Agrie. Biol. Chem
    • Sakamura, S. Watanabe, S. and Obata, Y. Anthocyanase and anthrocyanin occurring in the eggplant (Solanum melongena). III. Oxidative decolorization of the anthocyanin by polyphenol oxidase, Agrie. Biol. Chem. 29, 181, 1965.
    • (1965) , vol.29 , Issue.181
    • Sakamura, S.1    Watanabe, S.2    Obata, Y.3
  • 65
    • 84981869328 scopus 로고
    • Separation of a polyphenol oxidase for anthocyanin degradation in eggplant, J. Food Sei
    • Sakamura, S. Shibusa, S. and Obata, Y. Separation of a polyphenol oxidase for anthocyanin degradation in eggplant, J. Food Sei. 31, 317, 1966.
    • (1966) , vol.31 , Issue.317
    • Sakamura, S.1    Shibusa, S.2    Obata, Y.3
  • 66
    • 0343440423 scopus 로고
    • An anthocyanin-decolorizing system in sour cherries, Nature
    • Van Buren, P.G. Scheiner, D.M. and Wagenknecht, A.G. An anthocyanin-decolorizing system in sour cherries, Nature. 185, 165, 1960.
    • (1960) , vol.185 , Issue.165
    • Van, P.G.1    Scheiner, D.M.2    Wagenknecht, A.G.3
  • 67
    • 84987278698 scopus 로고
    • Enzymatic degradation of anthocyanins: the role of sweet cherry polyphenol oxidase, J. Food Sei
    • Pifferi, P.G. and Cultrera, R. Enzymatic degradation of anthocyanins: the role of sweet cherry polyphenol oxidase, J. Food Sei. 39, 786, 1974.
    • (1974) , vol.39 , Issue.786
    • Pifferi, P.G.1    Cultrera, R.2
  • 68
    • 84952432238 scopus 로고
    • Academic Press
    • Aspects of tyrosinase chemistry, in The Biochemistry of Copper, Peisach, W.E. Eds New York, 343.
    • Brooks, D.W. and Dawson, Ch. R. Aspects of tyrosinase chemistry, in The Biochemistry of Copper, Peisach, J. Aisen, P. and Blumberg, W.E. Eds. Academic Press, New York, 1966, 343.
    • (1966) Dawson, Ch. R.
    • Brooks, D.W.1    Aisen, J.2    Blumberg, P.3
  • 69
    • 0002218318 scopus 로고
    • Structures and functions of the phenolase complex, Nature
    • Mason, H.S. Structures and functions of the phenolase complex, Nature, 177, 79, 1956.
    • (1956) , vol.177 , Issue.79
    • Mason, H.S.1
  • 70
    • 0346061083 scopus 로고
    • Alterations in Solanum tuberosum polyphenol oxidase activity induced by gamma irradiation, Phytochemistry
    • Pendharkar, M.B. and Nair, P.M. Alterations in Solanum tuberosum polyphenol oxidase activity induced by gamma irradiation, Phytochemistry. 13, 1373, 1964.
    • (1964) , vol.13
    • Pendharkar, M.B.1    Nair, P.M.2
  • 71
    • 0010504985 scopus 로고
    • Chlorogenic acid oxidase from potato tuber slices: partial purification and properties, Phytochemistry
    • Alberghina, F.A.M. Chlorogenic acid oxidase from potato tuber slices: partial purification and properties, Phytochemistry, 3, 65, 1964.
    • (1964) , vol.3 , Issue.65
    • Alberghina, F.A.M.1
  • 73
    • 84979316182 scopus 로고
    • The preparation and properties of o-diphenol: oxygen oxidoreductase from potato tubers, New Phytol
    • Abukharma, B.A. and Woolhouse, H.W. The preparation and properties of o-diphenol: oxygen oxidoreductase from potato tubers, New Phytol. 65, 477, 1966.
    • (1966) , vol.65 , Issue.477
    • Abukharma, B.A.1    Woolhouse, H.W.2
  • 74
    • 0002957367 scopus 로고
    • Localization and nature of phenolase in sugar-beet leaves, J. Exp. Bot
    • Mayer, A.M. and Fried, J. Localization and nature of phenolase in sugar-beet leaves, J. Exp. Bot. 11, 141, 1960.
    • (1960) , vol.11 , Issue.141
    • Mayer, A.M.1    Fried, J.2
  • 75
    • 0041085943 scopus 로고
    • Substrates and inhibitors of the activated tyrosinase of broad bean, Phytochemistry
    • Robb, D.A. Swain, T. and Mapson, L.W. Substrates and inhibitors of the activated tyrosinase of broad bean, Phytochemistry, 5, 665, 1966.
    • (1966) , vol.5 , Issue.665
    • Robb, D.A.1    Swain, T.2    Mapson, L.W.3
  • 76
    • 84952432241 scopus 로고
    • Pergamon Press
    • in Enzyme Chemistry of Phenolic Compounds, Pridham, J.B. Ed Oxford, 7.
    • Bendall, D.S. and Gregory, R.P.F. Purification of phenol oxidases, in Enzyme Chemistry of Phenolic Compounds, Pridham, J.B. Ed. Pergamon Press, Oxford, 1966, 7.
    • (1966) Purification of phenol oxidases
    • Bendall, D.S.1    Gregory, R.P.F.2
  • 77
    • 84952420257 scopus 로고
    • The purification and some properties of the polyphenol oxidase from tea Camellia sinensis L., Biochem. J
    • Gregory, R.P.F. and Bendall, D.S. The purification and some properties of the polyphenol oxidase from tea (Camellia sinensis L.), Biochem. J. 101, 569, 1966.
    • (1966) , vol.101 , Issue.569
    • Gregory, R.P.F.1    Bendall, D.S.2
  • 78
    • 84952409336 scopus 로고
    • Polyphenolases of a local variety of mango, J. Food Sei. Technol. India
    • Joshi, P.R. and Shiralkar, N.D. Polyphenolases of a local variety of mango, J. Food Sei. Technol. India, 14, 77, 1977.
    • (1977) , vol.14 , Issue.77
    • Joshi, P.R.1    Shiralkar, N.D.2
  • 79
    • 84952420053 scopus 로고
    • Purification and some properties of two polyphenol oxidases from Bartlett pears, Plant Physiol
    • Rivas, N.J. and Whitaker, J.R. Purification and some properties of two polyphenol oxidases from Bartlett pears, Plant Physiol, 52, 501, 1973.
    • (1973) , vol.52 , Issue.501
    • Rivas, N.J.1    Whitaker, J.R.2
  • 80
    • 0002380324 scopus 로고
    • Specificity of an o-diphenol oxidase from Prunus avium fruits, Phytochemistry
    • Lanzarini, G. Pifferi, P.G. and Zamorani, A. Specificity of an o-diphenol oxidase from Prunus avium fruits, Phytochemistry. 11, 89, 1972.
    • (1972) , vol.11 , Issue.89
    • Lanzarini, G.1    Pifferi, P.G.2    Zamorani, A.3
  • 81
    • 0017780424 scopus 로고
    • on enzymic browning of potatoes Solanum tuberosum. III.
    • Kinetics of potato phenoloxidase E.C. 1.14.18.1 monophenol, dihydroxyphenylalanine:oxygen-oxidoreductase Z. Lebensm. Unters. Forsch. 163, 191
    • Matheis, G. and Belitz, H.-D. Studies on enzymic browning of potatoes (Solanum tuberosum). III. Kinetics of potato phenoloxidase (E.C. 1.14.18.1 monophenol, dihydroxyphenylalanine:oxygen-oxidoreductase Z. Lebensm. Unters. Forsch. 163, 191, 1977.
    • (1977)
    • Matheis, G.1    Belitz, H.-D.2
  • 82
    • 49849127092 scopus 로고
    • Hydroxylation of flavonoids by a phenolase preparation from leaves of spinach beet, Phytochemistry
    • Vaughan, P.F.T. Butt, V.S. Grisebach, H. and Schill, L. Hydroxylation of flavonoids by a phenolase preparation from leaves of spinach beet, Phytochemistry, 8, 1373, 1969.
    • (1969) , vol.8
    • Vaughan, P.F.T.1    Butt, V.S.2    Grisebach, H.3    Schill, L.4
  • 83
    • 84952432243 scopus 로고
    • des Systems Sauerstoff-Phenolase-Brenzcatechin-Hydrochinon, Z. Lebensm. Unters. Forsch
    • I. Untersuchung
    • Heimann, W. and Andler, St. uber die hydroxylierende Wirkung der Phenoloxidase. I. Untersuchung des Systems Sauerstoff-Phenolase-Brenzcatechin-Hydrochinon, Z. Lebensm. Unters. Forsch. 118, 1, 1962.
    • (1962) Andler, St. uber die hydroxylierende Wirkung der Phenoloxidase. , vol.118 , Issue.1
    • Heimann, W.1
  • 84
    • 0011275617 scopus 로고
    • On the heterogeneity of the tyrosinase of broad bean Vicia faba, Phytochemistry
    • Robb, D.A. Mapson, L.W. and Swain, T. On the heterogeneity of the tyrosinase of broad bean (Vicia faba), Phytochemistry, 4, 731, 1965.
    • (1965) , vol.4 , Issue.731
    • Robb, D.A.1    Mapson, L.W.2    Swain, T.3
  • 85
    • 0013808876 scopus 로고
    • Purification and Properties of o-diphenol oxidases in sweet potato, J. Biochem
    • Hyodo, H. and Uritani, I. Purification and Properties of o-diphenol oxidases in sweet potato, J. Biochem. 58, 388, 1965.
    • (1965) , vol.58 , Issue.388
    • Hyodo, H.1    Uritani, I.2
  • 86
    • 0018463333 scopus 로고
    • The mechanism of catalysis by o-diphenoloxidase, Biokhimiya
    • Bresler, S.E. Kazbekov, E.N. Sukhodolova, A.T. and Shadrin, V.N. The mechanism of catalysis by o-diphenoloxidase, Biokhimiya, 44, 741, 1979.
    • (1979) , vol.44 , Issue.741
    • Bresler, S.E.1    Kazbekov, E.N.2    Sukhodolova, A.T.3    Shadrin, V.N.4
  • 87
    • 84952432244 scopus 로고
    • Pergamon Press
    • in Enzyme Chemistry of Phenolic Compounds, Pridham, J.B. Ed Oxford, 1.
    • Burges, N.A. Enzymes associated with phenols, in Enzyme Chemistry of Phenolic Compounds, Pridham, J.B. Ed. Pergamon Press, Oxford, 1963, 1.
    • (1963) Enzymes associated with phenols
    • Burges, N.A.1
  • 88
    • 84952432245 scopus 로고
    • Academic Press
    • in The Biochemistry of Copper, Peisach, W.E. Eds New York, 371.
    • Levine, W.G. Lacease. A review, in The Biochemistry of Copper, Peisach, J. Aisen, P. and Blumberg, W.E. Eds. Academic Press, New York, 1966, 371.
    • (1966) Lacease. A review
    • Levine, W.G.1    Aisen, J.2    Blumberg, P.3
  • 90
    • 84986517149 scopus 로고
    • Pink discoloration in canned Williams' Bon Chretien pears, J. Food Sei
    • Czerkaskij, A. Pink discoloration in canned Williams' Bon Chretien pears, J. Food Sei. 35, 608, 1970.
    • (1970) , vol.35 , Issue.608
    • Czerkaskij, A.1
  • 91
    • 84952432247 scopus 로고
    • aoeber die Bildung von Metallchelaten bei Obstkonserven in Weissblechdosen, Dtsch. Lebensm. Rundsch
    • Heintze, K. aoeber die Bildung von Metallchelaten bei Obstkonserven in Weissblechdosen, Dtsch. Lebensm. Rundsch. 56, 194, 1960.
    • (1960) , vol.56 , Issue.194
    • Heintze, K.1
  • 92
    • 84982335347 scopus 로고
    • After-cooking blackening in potatoes. III.
    • Examination of the interaction of factors by in vitro experiments. J. Sei. Food Agrie. 13, 358
    • Hughes, J.C. and Swain, T. After-cooking blackening in potatoes. III. Examination of the interaction of factors by in vitro experiments. J. Sei. Food Agrie. 13, 358, 1962.
    • (1962)
    • Hughes, J.C.1    Swain, T.2
  • 93
    • 84952432249 scopus 로고
    • Removal of phenolic substances from wine, Kerteszeti Egyetem Közl
    • Erdass, T. and Fodor, I. Removal of phenolic substances from wine, Kerteszeti Egyetem Közl. 40, 283, 1976.
    • (1976) , vol.40 , Issue.283
    • Erdass, T.1    Fodor, I.2
  • 94
    • 84952432250 scopus 로고
    • Pergamon Press
    • in Enzyme Chemistry of Phenolic Compounds, Pridham, J.B. Ed Oxford, 87.
    • Williams, A.H. Enzyme inhibition by phenolic compounds, in Enzyme Chemistry of Phenolic Compounds, Pridham, J.B. Ed. Pergamon Press, Oxford, 1963, 87.
    • (1963) Enzyme inhibition by phenolic compounds
    • Williams, A.H.1
  • 95
    • 84952414732 scopus 로고
    • Effect of polyphenolic compounds on pectinase action, Eiyo To Shokuryo
    • Negoro, H. Effect of polyphenolic compounds on pectinase action, Eiyo To Shokuryo, 25, 1, 1972.
    • (1972) , vol.25 , Issue.1
    • Negoro, H.1
  • 96
    • 84952432251 scopus 로고
    • Verlust des fruchteigenen Wohlgeschmackes bei verarbeiteten Lebensmitteln pflanzlicher Herkunft, der im Zusammenhang mit der Spaltung von Hydroxyzimtsaureestern Depsiden steht, Dtsch. Lebensm. Rdsch
    • Burckhardt, R. Verlust des fruchteigenen Wohlgeschmackes bei verarbeiteten Lebensmitteln pflanzlicher Herkunft, der im Zusammenhang mit der Spaltung von Hydroxyzimtsaureestern (Depsiden) steht, Dtsch. Lebensm. Rdsch. 74, 205, 1978.
    • (1978) , vol.74 , Issue.205
    • Burckhardt, R.1
  • 97
    • 0015789920 scopus 로고
    • Phenolische Pflanzeninhaltsstoffe als natarliche Antioxydantien, Fette, Seifen, Anstrichm
    • Herrmann, K. Phenolische Pflanzeninhaltsstoffe als natarliche Antioxydantien, Fette, Seifen, Anstrichm. 75, 499, 1973.
    • (1973) , vol.75 , Issue.499
    • Herrmann, K.1
  • 98
    • 84984086888 scopus 로고
    • The action of potato phenolase on flavonoid compounds, J. Sei. Food Agrie
    • Baruah, P. and Swain, T. The action of potato phenolase on flavonoid compounds, J. Sei. Food Agrie. 10, 125, 1959.
    • (1959) , vol.10 , Issue.125
    • Baruah, P.1    Swain, T.2
  • 99
    • 84952392857 scopus 로고
    • Pergamon Press
    • in The Chemistry of Flavonoid Compounds, Geissmann, T.A. Ed Oxford, chap.
    • Freudenberg, K. and Weinges, K. Catechins and flavonoid tannins, in The Chemistry of Flavonoid Compounds, Geissmann, T.A. Ed. Pergamon Press, Oxford, 1962, chap. 7.
    • (1962) Catechins and flavonoid tannins , pp. 7
    • Freudenberg, K.1    Weinges, K.2
  • 101
    • 0012118922 scopus 로고
    • The conversion by phenolase of p-coumaric acid to caffeic acid with special reference to the role of ascorbic acid, Phytochemistry
    • Sata, M. The conversion by phenolase of p-coumaric acid to caffeic acid with special reference to the role of ascorbic acid, Phytochemistry, 8, 353, 1962.
    • (1962) , vol.8 , Issue.353
    • Sata, M.1
  • 102
    • 84952432255 scopus 로고
    • Studies on the enzymic browning of apples. II.
    • Properties of apple polyphenoloxidase, Aust. J. Biol. Sei. 17, 360
    • Walker, J.R.L. Studies on the enzymic browning of apples. II. Properties of apple polyphenoloxidase, Aust. J. Biol. Sei. 17, 360, 1964.
    • (1964)
    • Walker, J.R.L.1
  • 103
    • 0006531520 scopus 로고
    • Purification and multiplicity of catechol oxidase from apple chloroplasts, Phytochemistry
    • Harel, E. Mayer, A.M. and Shain, Y. Purification and multiplicity of catechol oxidase from apple chloroplasts, Phytochemistry. 4, 783, 1965.
    • (1965) , vol.4 , Issue.783
    • Harel, E.1    Mayer, A.M.2    Shain, Y.3
  • 104
    • 0042415547 scopus 로고
    • Catechol oxidase of Red Delicious apple peel, Phytochemistry
    • Stelzig, D.A. Akhtar, S. and Ribeiro, S. Catechol oxidase of Red Delicious apple peel, Phytochemistry, 11, 535, 1972.
    • (1972) , vol.11 , Issue.535
    • Stelzig, D.A.1    Akhtar, S.2    Ribeiro, S.3
  • 105
    • 84952391666 scopus 로고
    • Characterization of polyphenoloxidase in peaches grown in the Southeast, Hort Science
    • Jen, J.J. and Kahler, K.R. Characterization of polyphenoloxidase in peaches grown in the Southeast, Hort Science. 9, 590, 1974.
    • (1974) , vol.9 , Issue.590
    • Jen, J.J.1    Kahler, K.R.2
  • 106
    • 85005732363 scopus 로고
    • Flavonols and flavones in food plants: a review, J. Food Technol
    • Herrmann, K. Flavonols and flavones in food plants: a review, J. Food Technol. 11, 433, 1976.
    • (1976) , vol.11 , Issue.433
    • Herrmann, K.1
  • 107
    • 15844401072 scopus 로고
    • Inhibition and substrate specificity of lettuce phenolase, Phytochemistry
    • Mayer, A.M. Inhibition and substrate specificity of lettuce phenolase, Phytochemistry, 1, 237, 1962.
    • (1962) , vol.1 , Issue.237
    • Mayer, A.M.1
  • 108
    • 0001050533 scopus 로고
    • Die phenolischen Inhaltsstoffe des Obstes. II. Die Flavonole des Obstes, Z. Lebensm. Unters. Forsch
    • Wildanger, W. and Herrmann, K. Die phenolischen Inhaltsstoffe des Obstes. II. Die Flavonole des Obstes, Z. Lebensm. Unters. Forsch. 151, 103, 1973.
    • (1973) , vol.151 , Issue.103
    • Wildanger, W.1    Herrmann, K.2
  • 109
    • 84952432256 scopus 로고
    • aoeber die Phenolsauren des Gemases. III. Hydroxyzimtsauren des Wurzelgemases, Z. Lebensm. Unters. Forsch
    • Stahr, H. and Herrmann, K. aoeber die Phenolsauren des Gemases. III. Hydroxyzimtsauren des Wurzelgemases, Z. Lebensm. Unters. Forsch. 159, 219, 1975.
    • (1975) , vol.159 , Issue.219
    • Stahr, H.1    Herrmann, K.2
  • 110
    • 84952432257 scopus 로고
    • aoeber Verfarbungen des Gemases durch phenolische Inhaltsstoffe, Dtsch. Lebensm.
    • Rdsch. 72,90
    • Herrmann, K. aoeber Verfarbungen des Gemases durch phenolische Inhaltsstoffe, Dtsch. Lebensm. Rdsch. 72,90,1976.
    • (1976)
    • Herrmann, K.1
  • 111
    • 1542415011 scopus 로고
    • Kenntnisse aber Vorkommen, Gehalte sowie Veranderungen wahrend des Fruchtwachstums, Z. Lebensm. Unters. Forsch
    • Bisherige
    • Herrmann, K. Die phenolischen Inhaltsstoffe des Obstes. I. Bisherige Kenntnisse aber Vorkommen, Gehalte sowie Veranderungen wahrend des Fruchtwachstums, Z. Lebensm. Unters. Forsch. 151, 41, 1973.
    • (1973) Die phenolischen Inhaltsstoffe des Obstes. I. , vol.151 , Issue.41
    • Herrmann, K.1
  • 112
    • 0016907158 scopus 로고
    • aoeber das Vorkommen von Proanthocyanidinen, Leukoanthocyaniden and Catechinen in Gemase, Z. Lebensm. Unters. Forsch
    • Hanefold, M. and Herrmann, K. aoeber das Vorkommen von Proanthocyanidinen, Leukoanthocyaniden and Catechinen in Gemase, Z. Lebensm. Unters. Forsch. 161, 243, 1976.
    • (1976) , vol.161 , Issue.243
    • Hanefold, M.1    Herrmann, K.2
  • 113
    • 0003784095 scopus 로고
    • aoeber das Nichtvorkommen der in hAheren Pflanzen verbreiteten phenolischen Inhaltsstoffe im Champignon, Z. Lebensm. Unters. Forsch
    • Herrmann, K. aoeber das Nichtvorkommen der in hAheren Pflanzen verbreiteten phenolischen Inhaltsstoffe im Champignon, Z. Lebensm. Unters. Forsch. 155, 295, 1974.
    • (1974) , vol.155 , Issue.295
    • Herrmann, K.1
  • 114
    • 0014198059 scopus 로고
    • Detection and study by fluorescence spectrometry of stereospecificity in mushroom tyrosinase catalyzed oxidations. Proposal of a copper-containing reaction rate control site, J. Biol. Chem
    • Harrison, W.H. Whisler, W.W. and Ko, S. Detection and study by fluorescence spectrometry of stereospecificity in mushroom tyrosinase catalyzed oxidations. Proposal of a copper-containing reaction rate control site, J. Biol. Chem. 242, 1660, 1967.
    • (1967) , vol.242
    • Harrison, W.H.1    Whisler, W.W.2    Ko, S.3
  • 115
    • 84952432261 scopus 로고
    • Die Bedeutung der Polyphenole bei der enzymatischen Braunung von Obst. Ernaehrungsforschung
    • Taufel, K. and Voigt, J. Die Bedeutung der Polyphenole bei der enzymatischen Braunung von Obst. Ernaehrungsforschung, 8, 406, 1963.
    • (1963) , vol.8 , Issue.406
    • Taufel, K.1    Voigt, J.2
  • 116
    • 0017782634 scopus 로고
    • und phenolische Inhaltsstoffe verschiedener
    • Lebensm. Unters. Forsch. 163, 92
    • Matheis, G. and Belitz, H.-D. Untersuchungen zur enzymatischen Braunung bei Kartoffeln (Solanum tuberosum). I. Phenoloxydasen und phenolische Inhaltsstoffe verschiedener Sorten, Z. Lebensm. Unters. Forsch. 163, 92, 1977.
    • (1977)
    • Matheis, G.1    Belitz, H.-D.2    Phenoloxydasen, I.3    Sorten, Z.4
  • 117
    • 0002511848 scopus 로고
    • Detection and identification of the polyphenoloxidase substrate of the banana, Nature
    • Griffiths, L.A. Detection and identification of the polyphenoloxidase substrate of the banana, Nature. 184, 58, 1959.
    • (1959) , vol.184 , Issue.58
    • Griffiths, L.A.1
  • 118
    • 0013772886 scopus 로고
    • 3-O-Caffeoylshikimic acid dactylifric acid and its isomers, a new class of enzymatic browning substrates, Biochem. Biophys. Res. Commun
    • Maier, V.P. Metzler, D.M. and Huber, A.F. 3-O-Caffeoylshikimic acid (dactylifric acid) and its isomers, a new class of enzymatic browning substrates, Biochem. Biophys. Res. Commun. 14, 124, 1964.
    • (1964) , vol.14 , Issue.124
    • Maier, V.P.1    Metzler, D.M.2    Huber, A.F.3
  • 119
    • 0242623652 scopus 로고
    • and Rubertac, R. The polyphenol of Dioscorea alata yam tubers associated with oxidative browning, J. Agrie. Food Chem
    • Martin, W. and Rubertac, R. The polyphenol of Dioscorea alata (yam) tubers associated with oxidative browning, J. Agrie. Food Chem. 24, 67, 1976.
    • (1976) , vol.24 , Issue.67
    • Martin, W.1
  • 120
    • 84952432265 scopus 로고
    • The polyphenoloxidase of pear fruit, Aust. J.
    • Biol. Sei. 17, 575
    • Walker, J.R.L. The polyphenoloxidase of pear fruit, Aust. J. Biol. Sei. 17, 575, 1964.
    • (1964)
    • Walker, J.R.L.1
  • 121
    • 84952432266 scopus 로고
    • Polyphenoloxydase-Aktivitat und Braunung bei BartlettBirnen, Fruchtsaft-Ind. ver Confructa
    • Luh, B.S. Tate, J.N. and Villarreal, F. Polyphenoloxydase-Aktivitat und Braunung bei BartlettBirnen, Fruchtsaft-Ind. ver Confructa, 8, 274, 1963.
    • (1963) , vol.8 , Issue.274
    • Luh, B.S.1    Tate, J.N.2    Villarreal, F.3
  • 122
    • 84952432267 scopus 로고
    • del complejo fenolasa de albaricoque, Rev. Agroquim.
    • Tecnol. Aliment. 6,94
    • Soler, A. Sabater, F. and Lozano, J.A. Sustratos del complejo fenolasa de albaricoque, Rev. Agroquim. Tecnol. Aliment. 6,94,1966.
    • (1966)
    • Soler, A.1    Sabater, F.2    Sustratos, J.A.3
  • 123
    • 84987332253 scopus 로고
    • Characteristics of polyphenol oxidase related to browning in cling peaches, J. Food Sei
    • Luh, B.S. and Phithakpol, B. Characteristics of polyphenol oxidase related to browning in cling peaches, J. Food Sei. 37, 264, 1972.
    • (1972) , vol.37 , Issue.264
    • Luh, B.S.1    Phithakpol, B.2
  • 125
    • 84952391974 scopus 로고
    • Ricerche sulla polifenolossidasi delle uve: II. Estrazione, puriflcazione e caratterizzazione dell'enzima, Ind. Agrar
    • Montedoro, M. Ricerche sulla polifenolossidasi delle uve: II. Estrazione, puriflcazione e caratterizzazione dell'enzima, Ind. Agrar. 7, 259, 1969.
    • (1969) , vol.7 , Issue.259
    • Montedoro, M.1
  • 126
    • 84952385776 scopus 로고
    • Characteristics of Concord grape polyphenoloxidase involved in juice color loss, J. Food Sei
    • Cash, J.N. Sistrunk, W.A. and Stutte, C.A. Characteristics of Concord grape polyphenoloxidase involved in juice color loss, J. Food Sei. 41, 1398, 1976.
    • (1976) , vol.41
    • Cash, J.N.1    Sistrunk, W.A.2    Stutte, C.A.3
  • 127
    • 84952432268 scopus 로고
    • Oxidation and browning reaction of pyrogallol with the polyphenoloxidase from the immature fruit of Satsuma mandarin, Eiyo To Shokuryo
    • Fujita, S. and Sono, T. Oxidation and browning reaction of pyrogallol with the polyphenoloxidase from the immature fruit of Satsuma mandarin, Eiyo To Shokuryo, 29, 457, 1976.
    • (1976) , vol.29 , Issue.457
    • Fujita, S.1    Sono, T.2
  • 128
    • 84987265526 scopus 로고
    • Polyphenoloxidase activity and browning of mango fruits induced by gamma irradiation, J. Food, Sei
    • Thomas, P. and Janave, M.T. Polyphenoloxidase activity and browning of mango fruits induced by gamma irradiation, J. Food, Sei. 38, 1149, 1973.
    • (1973) , vol.38
    • Thomas, P.1    Janave, M.T.2
  • 129
    • 84952418823 scopus 로고
    • Some biochemical properties of polyphenol oxidase from two avocado varieties differing in their browning rates, J. Food Sei
    • Kahn, V. Some biochemical properties of polyphenol oxidase from two avocado varieties differing in their browning rates, J. Food Sei. 42, 38, 1977.
    • (1977) , vol.42 , Issue.38
    • Kahn, V.1
  • 131
    • 0011281462 scopus 로고
    • Cinnamyl and p-coumaryl esters as intermediates in the biosynthesis of chlorogenic acid, J. Biol. Chem
    • Levy, C.C. and Zucker, M. Cinnamyl and p-coumaryl esters as intermediates in the biosynthesis of chlorogenic acid, J. Biol. Chem. 235, 2418, 1960.
    • (1960) , vol.235
    • Levy, C.C.1    Zucker, M.2
  • 132
    • 84952432270 scopus 로고
    • Enzymatic browning of the pods of broad beans and prevention of browning by CO treatment, Eiyo to Shokuryo
    • Fujimoto, K. Shindo, S. and Kaneda, T. Enzymatic browning of the pods of broad beans and prevention of browning by CO treatment, Eiyo to Shokuryo, 25, 349, 1972.
    • (1972) , vol.25 , Issue.349
    • Fujimoto, K.1    Shindo, S.2    Kaneda, T.3
  • 133
    • 85022366855 scopus 로고
    • Enzymatic browning of stored parsnip roots, J. Am. Soc. Hortic. Sei
    • Chubey, B.B. and Dorell, G.D. Enzymatic browning of stored parsnip roots, J. Am. Soc. Hortic. Sei. 97, 107, 1972.
    • (1972) , vol.97 , Issue.107
    • Chubey, B.B.1    Dorell, G.D.2
  • 134
    • 8644271365 scopus 로고
    • The browning of parsnips, Can. Inst. Food Sei. Technol. J
    • Kaldy, M.S. and Markakis, P. The browning of parsnips, Can. Inst. Food Sei. Technol. J. 5, 37, 1972.
    • (1972) , vol.5 , Issue.37
    • Kaldy, M.S.1    Markakis, P.2
  • 135
    • 84952432273 scopus 로고
    • Jpn. Soc.
    • 11. The effects of maturation and harvesting season on pitting injury and browning of seeds and pulp during Hortic. Sei. 45, 307, FST Abstr. 9, 10 J 1322, 1977.
    • Abe, K. Chachin, K. and Ogata, K. Chilling injury in eggplant fruits, 11. The effects of maturation and harvesting season on pitting injury and browning of seeds and pulp during storage, J. Jpn. Soc. Hortic. Sei. 45, 307, 1976; FST Abstr. 9, 10 J 1322, 1977.
    • (1976) Chilling injury in eggplant fruits
    • Abe, K.1    Chachin, K.2    Ogata, K.3
  • 136
    • 84952389894 scopus 로고
    • A comparison of chlorogenic acid and catechol as substrates for the polyphenol oxidase from tobacco and mushroom, Plant Physiol
    • Sisler, E.C. and Evans, H.J. A comparison of chlorogenic acid and catechol as substrates for the polyphenol oxidase from tobacco and mushroom, Plant Physiol. 33, 255, 1958.
    • (1958) , vol.33 , Issue.255
    • Sisler, E.C.1    Evans, H.J.2
  • 137
    • 84952432274 scopus 로고
    • Extraccian y purificacian parcial de la polifenoloxidasa de manzanas Red Delicious. Determinacian de la actividad mediante un electrodo de plata-plomo, Rev.
    • Agroquim. Tecnol. Aliment, 15, 434
    • Chaves, A.A. and Tomais, J.O. Extraccian y purificacian parcial de la polifenoloxidasa de manzanas Red Delicious. Determinacian de la actividad mediante un electrodo de plata-plomo, Rev. Agroquim. Tecnol. Aliment, 15, 434, 1975.
    • (1975)
    • Chaves, A.A.1    Tomais, J.O.2
  • 138
    • 84952410952 scopus 로고
    • Isolation and purification of polyphenol oxidase isozymes of clingstone peach, Plant Physiol
    • Wong, T.C. Luh, B.S. and Whitaker, J.R. Isolation and purification of polyphenol oxidase isozymes of clingstone peach, Plant Physiol. 48, 19, 1971.
    • (1971) , vol.48 , Issue.19
    • Wong, T.C.1    Luh, B.S.2    Whitaker, J.R.3
  • 139
    • 84952432275 scopus 로고
    • Characteristics of browning enzymes in Fay Elberta freestone peaches, Food Technol
    • Ph. and
    • Reyes, Ph. and Luh, B.S. Characteristics of browning enzymes in Fay Elberta freestone peaches, Food Technol. 14, 570, 1960.
    • (1960) Reyes , vol.14 , Issue.570
    • Luh, B.S.1
  • 140
    • 84952384086 scopus 로고
    • Polyphenoloxidase of Solanum melongena and its natural substrate, Acta Aliment. Acad. Sei. Hung
    • Ramaswamy, S. and Rege, D.V. Polyphenoloxidase of Solanum melongena and its natural substrate, Acta Aliment. Acad. Sei. Hung. 4, 355, 1975.
    • (1975) , vol.4 , Issue.355
    • Ramaswamy, S.1    Rege, D.V.2
  • 141
    • 84981867394 scopus 로고
    • Some characteristics of eggplant and avocado polyphenoloxidases, J. Food Sei
    • Knapp, F.W. Some characteristics of eggplant and avocado polyphenoloxidases, J. Food Sei. 30, 930, 1965.
    • (1965) , vol.30 , Issue.930
    • Knapp, F.W.1
  • 142
    • 0000103867 scopus 로고
    • Separation and purification of the phenolases of the common mushroom, J. Biol. Chem
    • Smith, L.L. and Kruger, R.C. Separation and purification of the phenolases of the common mushroom, J. Biol. Chem. 237, 1121, 1962.
    • (1962) , vol.237
    • Smith, L.L.1    Kruger, R.C.2
  • 143
    • 84952432276 scopus 로고
    • Substrate specificity of the enzymic browning of apples, Acta Aliment. Acad.
    • Sei. Hung. 7, 79
    • Vaimos-Vigyaiza, L. and Gajzaigo, I. Substrate specificity of the enzymic browning of apples, Acta Aliment. Acad. Sei. Hung. 7, 79, 1978.
    • (1978)
    • Vaimos-Vigyaiza, L.1    Gajzaigo, I.2
  • 144
    • 0014617017 scopus 로고
    • Oxidation systems in fruits and vegetables-their relation to the quality of preserved products, Adv. Food Res
    • Aylward, F. and Haisman, D.R. Oxidation systems in fruits and vegetables-their relation to the quality of preserved products, Adv. Food Res. 17, 1, 1969.
    • (1969) , vol.17 , Issue.1
    • Aylward, F.1    Haisman, D.R.2
  • 145
    • 84984083565 scopus 로고
    • Changes in the enzymic browning of Bramley's Seedling apples during their development, J. Sei. Food Agrie
    • Weurman, C. and Swain, T. Changes in the enzymic browning of Bramley's Seedling apples during their development, J. Sei. Food Agrie. 6, 186, 1955.
    • (1955) , vol.6 , Issue.186
    • Weurman, C.1    Swain, T.2
  • 146
    • 0015978637 scopus 로고
    • Studies into the o-diphenol oxidase activity of potatoes, Part II. Some characteristics of the enzyme, its amount in different varieties and its changes on storage, Acta Aliment.
    • Acad. Sei. Hung. 3, 49
    • Vaimos-Vigyaiza, L. and Kiss-Kutz, N. Studies into the o-diphenol oxidase activity of potatoes, Part II. Some characteristics of the enzyme, its amount in different varieties and its changes on storage, Acta Aliment. Acad. Sei. Hung. 3, 49, 1974.
    • (1974)
    • Vaimos-Vigyaiza, L.1    Kiss-Kutz, N.2
  • 147
    • 84952432278 scopus 로고
    • The activities of polyphenol oxidase and peroxidase in fruits and vegetables as related to pH and temperature. Acta Aliment.
    • N. and Acad. Sei. Hung. 7, 57
    • Mihailyi, K. Vaimos-Vigyaiza, L. Kiss-Kutz, N. and Babos-Szebenyi, A. The activities of polyphenol oxidase and peroxidase in fruits and vegetables as related to pH and temperature. Acta Aliment. Acad. Sei. Hung. 7, 57, 1978.
    • (1978) Vaimos-Vigyaiza
    • Mihailyi, K.1    Kiss-Kutz, L.2    Babos-Szebenyi, A.3
  • 148
    • 84952403332 scopus 로고
    • Ascorbic acid oxidation and browning in apple tissue extract, Arch. Biochem
    • Ponting, J.D. and Joslyn, M.A. Ascorbic acid oxidation and browning in apple tissue extract, Arch. Biochem. 19, 47, 1948.
    • (1948) , vol.19 , Issue.47
    • Ponting, J.D.1    Joslyn, M.A.2
  • 149
    • 84952432279 scopus 로고
    • Banana polyphenoloxidase. Varietal differences and partial characterization in 5th Int.
    • Congr. Food Sei. Technol. Kyoto, Japan, September 237.
    • Galeazzi, M.A. and Sgarbieri, V.C. Banana polyphenoloxidase. Varietal differences and partial characterization in 5th Int. Congr. Food Sei. Technol. Kyoto, Japan, September 1978, 237.
    • (1978)
    • Galeazzi, M.A.1    Sgarbieri, V.C.2
  • 150
    • 84952402074 scopus 로고
    • Polyphenol oxidase activity and browning of three avocado varieties, J. Sei. Food Agrie
    • Kahn, V. Polyphenol oxidase activity and browning of three avocado varieties, J. Sei. Food Agrie. 26, 1319, 1975.
    • (1975) , vol.26
    • Kahn, V.1
  • 151
    • 28444442552 scopus 로고
    • Zur Bestimmung der Polyphenoloxidaseaktivitat in Kartoffelknollen, Z. Lebensm. Unters. Forsch
    • Schaller, K. Zur Bestimmung der Polyphenoloxidaseaktivitat in Kartoffelknollen, Z. Lebensm. Unters. Forsch. 150, 211, 1972.
    • (1972) , vol.150 , Issue.211
    • Schaller, K.1
  • 152
    • 84952414382 scopus 로고
    • Polyphenol oxidase of Capsicum frutescens var. grossa Sendt, J. Food Sei. Technol
    • Luhadiya, A.P. and Kulkarni, P.R. Polyphenol oxidase of Capsicum frutescens var. grossa Sendt, J. Food Sei. Technol. 15, 214, 1978.
    • (1978) , vol.15 , Issue.214
    • Luhadiya, A.P.1    Kulkarni, P.R.2
  • 153
    • 84952432281 scopus 로고
    • tyrosinase polyphenol oxidase
    • Ch. R. and Mager, in Methods in Enzymology, Colowick, N.O. Eds Academic Press New York, 817.
    • Dawson, Ch. R. and Mager, R.J. Plant tyrosinase (polyphenol oxidase), in Methods in Enzymology, Vol. 5, Colowick, S.P. and Kaplan, N.O. Eds. Academic Press, New York, 1962, 817.
    • (1962) Dawson , vol.5
    • Plant, R.J.1    Kaplan, S.P.2
  • 154
    • 84952432282 scopus 로고
    • Le froid et les qualitacs organoleptiques des produits alimentaires, Rev. Gen. Froid
    • Ulrich, M.R. Le froid et les qualitacs organoleptiques des produits alimentaires, Rev. Gen. Froid, 12, 1025, 1975.
    • (1975) , vol.12
    • Ulrich, M.R.1
  • 155
    • 84952432283 scopus 로고
    • Thermobacteriology in Food Processing
    • Academic Press, New York, chap.
    • Stumbo, C.R. Thermobacteriology in Food Processing, Academic Press, New York, 1966, chap. 6.
    • (1966) , pp. 6
    • Stumbo, C.R.1
  • 156
    • 84952432284 scopus 로고
    • Cinetica delle reazioni nella sterilizzazione degli alimenti in scatola, Ind. Aliment. Pinerolo, Italy
    • Nehring, P. Cinetica delle reazioni nella sterilizzazione degli alimenti in scatola, Ind. Aliment. (Pinerolo, Italy), 14, 129, 1975.
    • (1975) , vol.14 , Issue.129
    • Nehring, P.1
  • 157
    • 84952409612 scopus 로고
    • Heat inactivation of polyphenolase in fruit purees, Food Technol
    • Dimick, K.P. Ponting, J.D. and Makower, B. Heat inactivation of polyphenolase in fruit purees, Food Technol. 5, 237, 1950.
    • (1950) , vol.5 , Issue.237
    • Dimick, K.P.1    Ponting, J.D.2    Makower, B.3
  • 158
    • 84952389746 scopus 로고
    • Neuere Arbeiten aber die Technologie der Apfelnektar-Herstellung, Ind. Obst- Gemaseverwert
    • Strubi, P. Escher, F. and Neukom, H. Neuere Arbeiten aber die Technologie der Apfelnektar-Herstellung, Ind. Obst- Gemaseverwert. 60, 349, 1975.
    • (1975) , vol.60 , Issue.349
    • Strubi, P.1    Escher, F.2    Neukom, H.3
  • 159
    • 84952432285 scopus 로고
    • Anon. Desactivacian de polifenoloxidasa en membrillos. Informacian taccnica. Rev. Agroquim. Tecnol. Aliment.18
    • 265
    • Anon. Desactivacian de polifenoloxidasa en membrillos. Informacian taccnica. Rev. Agroquim. Tecnol. Aliment.18, 265, 1978.
    • (1978)
  • 160
    • 84952432286 scopus 로고
    • and Yankov, St. Thermostability of the enzyme polyphenoloxidase in stone fruits, Nauchni Tr. Vissh. Inst. Khranit. Vkusova Promst
    • Dang, F. and Yankov, St. Thermostability of the enzyme polyphenoloxidase in stone fruits, Nauchni Tr. Vissh. Inst. Khranit. Vkusova Promst. 17, 297, 1970.
    • (1970) , vol.17 , Issue.297
    • Dang, F.1
  • 161
    • 84952432287 scopus 로고
    • ÜFber die thermische Inaktivierung der Oxydasen in Obst und Gemase, Lebensm. Ind
    • Jankow, C.I. ÜFber die thermische Inaktivierung der Oxydasen in Obst und Gemase, Lebensm. Ind. 10, 23, 1963.
    • (1963) , vol.10 , Issue.23
    • Jankow, C.I.1
  • 162
    • 84952432288 scopus 로고
    • Comportamiento de fenolasa de albaricoque frente a pH, tiempo y temperatura, Rev. Agroquim. Tecnol. Aliment
    • Soler-Marta-Nez, A. Sabater-Garca-A, F. and Lozano, J.A. Comportamiento de fenolasa de albaricoque frente a pH, tiempo y temperatura, Rev. Agroquim. Tecnol. Aliment. 5, 353, 1965.
    • (1965) , vol.5 , Issue.353
    • Sabater-Garca-A, A.1    Lozano, J.A.2
  • 163
    • 84952385979 scopus 로고
    • Degree of heat inactivation of polyphenol oxidase and quality of frozen apricot puree, Food Technol
    • Ponting, J.D. Bean, R.S. Notter, G.K. and Makower, B. Degree of heat inactivation of polyphenol oxidase and quality of frozen apricot puree, Food Technol. 8, 573, 1954.
    • (1954) , vol.8 , Issue.573
    • Ponting, J.D.1    Bean, R.S.2    Notter, G.K.3    Makower, B.4
  • 164
    • 84952432289 scopus 로고
    • and Vemos-Vigyaiza, L. Ergebnisse von Untersuchungen hinsichtlich der Thermostabilitat von o-Diphenoloxidasen des Mesocarps verschiedener gelbfleischiger Pfirsichsorten, Confructa
    • Schaller, A. and Vemos-Vigyaiza, L. Ergebnisse von Untersuchungen hinsichtlich der Thermostabilitat von o-Diphenoloxidasen des Mesocarps verschiedener gelbfleischiger Pfirsichsorten, Confructa. 23, 90, 1978.
    • (1978) , vol.23 , Issue.90
    • Schaller, A.1
  • 165
    • 84952386240 scopus 로고
    • Etude de l'inactivation par la chaleur de la Polyphenoloxydase du jus de raisin, Ann. Technol. Agrie
    • Demeaux, M. and Bidan, P. Etude de l'inactivation par la chaleur de la Polyphenoloxydase du jus de raisin, Ann. Technol. Agrie. 16, 75, 1967.
    • (1967) , vol.16 , Issue.75
    • Demeaux, M.1    Bidan, P.2
  • 166
    • 84952432290 scopus 로고
    • Le chauffage continu du raisin avant pressurage, C R. Acad. Agrie
    • Guinot, Y. and Menoret, Y. Le chauffage continu du raisin avant pressurage, C R. Acad. Agrie. 51, 866, 1965.
    • (1965) , vol.51 , Issue.866
    • Guinot, Y.1    Menoret, Y.2
  • 167
    • 84952432291 scopus 로고
    • Thermostabilitat der Polyphenoloxidasen in Saften verschiedener Traubensorten, Confructa
    • St. I. and
    • Jankow, St. I. and Kirov, M.B. Thermostabilitat der Polyphenoloxidasen in Saften verschiedener Traubensorten, Confructa, 17, 4, 1972.
    • (1972) Jankow , vol.17 , Issue.4
    • Kirov, M.B.1
  • 168
    • 84963237707 scopus 로고
    • Der Einfluss des pH-Wertes auf die Polyphenoloxydase-Aktivitat im Temperaturbereich von 20A C bis 30AC, Wein- Wissenschaft
    • Enkelmann, R. Der Einfluss des pH-Wertes auf die Polyphenoloxydase-Aktivitat im Temperaturbereich von 20A C bis 30AC, Wein- Wissenschaft. 24, 452, 1969.
    • (1969) , vol.24 , Issue.452
    • Enkelmann, R.1
  • 170
    • 84952432294 scopus 로고
    • Comportamento di alcuni enzimi di fragole congelate e conservate a - 20AC per un lungo periodo, Ind. Agrar
    • Pallavicini, C. Comportamento di alcuni enzimi di fragole congelate e conservate a - 20AC per un lungo periodo, Ind. Agrar. 7, 268, 1969.
    • (1969) , vol.7 , Issue.268
    • Pallavicini, C.1
  • 171
    • 84952432295 scopus 로고
    • La daccongaclation des denraces d'origine vacgactale, Rev. Gen. Froid
    • Philippon, J. La daccongaclation des denraces d'origine vacgactale, Rev. Gen. Froid, 66, 947, 1975.
    • (1975) , vol.66 , Issue.947
    • Philippon, J.1
  • 172
    • 84952432296 scopus 로고
    • Yankov
    • St. Heat inactivation of oxidation enzymes, Khranit. Promst. 12(4,5), 19
    • Yankov, St. Heat inactivation of oxidation enzymes, Khranit. Promst. 12(4,5), 19, 1963.
    • (1963)
  • 173
    • 84952432297 scopus 로고    scopus 로고
    • of enzyme systems in vegetables prior to freezing, Izv. Vyssh.
    • Uchebn. Zaved. Pishch. Tekhnol. 5, 42, I97I.
    • Krotov, E.G. Pluzhnikov, I.I. and Golubyatnikova, L.A. Inactivation of enzyme systems in vegetables prior to freezing, Izv. Vyssh. Uchebn. Zaved. Pishch. Tekhnol. 5, 42, I97I.
    • Krotov, E.G.1    Pluzhnikov, I.I.2    Inactivation, L.A.3
  • 174
    • 84952432298 scopus 로고
    • Controllo periodico durante vari mesi della resistenza e dell'attivita a -20AC di alcuni enzimi estratti da fagiolini e piselli surgelati, Ind. Agrar
    • Spettoli, P. and Bolcato, V. Controllo periodico durante vari mesi della resistenza e dell'attivita a -20AC di alcuni enzimi estratti da fagiolini e piselli surgelati, Ind. Agrar. 11, 76, 1973.
    • (1973) , vol.11 , Issue.76
    • Spettoli, P.1    Bolcato, V.2
  • 175
    • 84952432299 scopus 로고
    • Resistenza di alcuni enzimi di fagiolini e piselli al surgelamento e ad una lunga conservazione a -20AC Ind. Agrar
    • Pallavicini, C. Spettoli, P. and Bolcato, V. Resistenza di alcuni enzimi di fagiolini e piselli al surgelamento e ad una lunga conservazione a -20AC Ind. Agrar. 8, 194, 1970.
    • (1970) , vol.8 , Issue.194
    • Pallavicini, C.1    Spettoli, P.2    Bolcato, V.3
  • 176
    • 84986761413 scopus 로고
    • Latency properties of polyphenol oxidase in two avocado cultivars differing in their rate of browning, J. Sei. Food Agrie
    • Kahn, V. Latency properties of polyphenol oxidase in two avocado cultivars differing in their rate of browning, J. Sei. Food Agrie. 28, 233, 1977.
    • (1977) , vol.28 , Issue.233
    • Kahn, V.1
  • 177
    • 0000604385 scopus 로고
    • Evidence for conformational changes in grape catechol oxidase, Phytochemistry
    • Lerner, H.R. Mayer, A.H. and Harel, E. Evidence for conformational changes in grape catechol oxidase, Phytochemistry, 11, 2415, 1972.
    • (1972) , vol.11
    • Lerner, H.R.1    Mayer, A.H.2    Harel, E.3
  • 178
    • 0011275617 scopus 로고
    • On the heterogeneity of the tyrosinase of broad bean Vicia faba L. Phytochemistry
    • Robb, D.A. Mapson, L.W. and Swain, T. On the heterogeneity of the tyrosinase of broad bean (Vicia faba L.) Phytochemistry, 4, 731, 1965.
    • (1965) , vol.4 , Issue.731
    • Robb, D.A.1    Mapson, L.W.2    Swain, T.3
  • 179
    • 84952399322 scopus 로고
    • Studies on the relationship between L-ascorbic acid and o-diphenol oxidase activity in Radish Raphanus sativus L., Eiyo To Shokuryo
    • Ishiguro, R. Shinohara, R. and Aoyama, Y. Studies on the relationship between L-ascorbic acid and o-diphenol oxidase activity in Radish (Raphanus sativus L.), Eiyo To Shokuryo, 23, 13, 1970.
    • (1970) , vol.23 , Issue.13
    • Ishiguro, R.1    Shinohara, R.2    Aoyama, Y.3
  • 180
    • 8644231449 scopus 로고
    • The association of copper with tyrosinase activity and internal discoloration blackspot in Russet Burbank potatoes, Am. Potato J
    • Weaver, M.L. Brown, R.C. and Steen, H.A. The association of copper with tyrosinase activity and internal discoloration (blackspot) in Russet Burbank potatoes, Am. Potato J. 45, 132, 1968.
    • (1968) , vol.45 , Issue.132
    • Weaver, M.L.1    Brown, R.C.2    Steen, H.A.3
  • 181
    • 84963102867 scopus 로고
    • A study on increase in o-diphenol oxidase activity during incubation of sliced sweet potato tissue, Plant Cell Physiol
    • Hyodo, H. and Uritani, I. A study on increase in o-diphenol oxidase activity during incubation of sliced sweet potato tissue, Plant Cell Physiol. 7, 137, 1966.
    • (1966) , vol.7 , Issue.137
    • Hyodo, H.1    Uritani, I.2
  • 182
    • 84952432300 scopus 로고
    • Etude par ultracentrifugation analytique d'un systame enzymatique monomare-polymare Polyphenoloxydase. J.
    • Polym. Sei. Part C, 16(7), 4103
    • Arnaud, Y. Etude par ultracentrifugation analytique d'un systame enzymatique monomare-polymare (Polyphenoloxydase). J. Polym. Sei. Part C, 16(7), 4103, 1965.
    • (1965)
    • Arnaud, Y.1
  • 184
    • 84952432302 scopus 로고
    • of germination stimulators on potato shoots and tubers, Fiziol. Rast
    • Effect
    • Palladina, T.A. and Pervova, Yu. A. Effect of germination stimulators on potato shoots and tubers, Fiziol. Rast. 13, 238, 1966.
    • (1966) Pervova, Yu. A. , vol.13 , Issue.238
    • Palladina, T.A.1
  • 187
    • 84952432304 scopus 로고
    • Chem.
    • Abstr. 63, 3289g, 1965.
    • Tagi-Zade, A.H. and Guseinov, S.G. The effect of ionizing radiation on oxidation-reduction processes of some plants, Izv. Akad. Nauk Azerb. SSR, Ser. Biol. Nauk, 6,91, 1964; Chem. Abstr. 63, 3289g, 1965.
    • (1964) , vol.6 , Issue.91
    • Guseinov, A.H.1    Tagi-Zade, S.G.2
  • 188
    • 0014202599 scopus 로고
    • Inhibition of banana polyphenoloxidase by 2-mercaptobenzthiazole, Science
    • Palmer, J.K. and Roberts, J.B. Inhibition of banana polyphenoloxidase by 2-mercaptobenzthiazole, Science. 157, 200, 1967.
    • (1967) , vol.157 , Issue.200
    • Palmer, J.K.1    Roberts, J.B.2
  • 189
    • 0014828689 scopus 로고
    • The action of o-dihydric phenols in the hydroxylation of p-coumaric acid by a phenolase from leaves of spinach beet Beta vulgaris L., Biochem. J
    • Vaughan, P.F.T. and Butt, V.S. The action of o-dihydric phenols in the hydroxylation of p-coumaric acid by a phenolase from leaves of spinach beet (Beta vulgaris L.), Biochem. J. 119, 89, 1970.
    • (1970) , vol.119 , Issue.89
    • Vaughan, P.F.T.1    Butt, V.S.2
  • 190
    • 84952385044 scopus 로고
    • Mechanism of borate inhibition of diphenol oxidation by tyrosinase, J. Biol. Chem
    • Yasunobu, K.T. and Norris, E.R. Mechanism of borate inhibition of diphenol oxidation by tyrosinase, J. Biol. Chem. 227, 473, 1957.
    • (1957) , vol.227 , Issue.473
    • Yasunobu, K.T.1    Norris, E.R.2
  • 191
    • 0014315255 scopus 로고
    • Hemmung der o-Diphenol-Oxydase-Aktivitat durch Borat und Germanat, Hoppe-Seyler's Z. Physiol. Chem
    • Weser, U. Hemmung der o-Diphenol-Oxydase-Aktivitat durch Borat und Germanat, Hoppe-Seyler's Z. Physiol. Chem. 349, 982, 1968.
    • (1968) , vol.349 , Issue.982
    • Weser, U.1
  • 192
    • 0016040099 scopus 로고
    • Inhibition by carboxylic acids of an o-diphenol oxidase from Prunus avium fruits, J. Sei. Food Agrie
    • Pifferi, P.G. Baldassari, L. and Cultrera, R. Inhibition by carboxylic acids of an o-diphenol oxidase from Prunus avium fruits, J. Sei. Food Agrie. 25, 263, 1974.
    • (1974) , vol.25 , Issue.263
    • Pifferi, P.G.1    Baldassari, L.2    Cultrera, R.3
  • 193
    • 84952417551 scopus 로고
    • Studies on the enzymis browning of apples. Inhibition of apple o-diphenol oxidase by phenolic acids, J. Sei. Food Agrie
    • Walker, J.R.L. and Wilson, E.L. Studies on the enzymis browning of apples. Inhibition of apple o-diphenol oxidase by phenolic acids, J. Sei. Food Agrie. 26, 1825, 1975.
    • (1975) , vol.26
    • Walker, J.R.L.1    Wilson, E.L.2
  • 194
    • 85005461750 scopus 로고
    • The control of enzymic browning in fruit juices by cinnamic acid, J. Food Technol
    • Walker, J.R.L. The control of enzymic browning in fruit juices by cinnamic acid, J. Food Technol. 11, 341, 1976.
    • (1976) , vol.11 , Issue.341
    • Walker, J.R.L.1
  • 195
    • 84952432305 scopus 로고
    • Inhibidores estructurales de fenolasa de albaricoque, Rev. Esp. Fisiol
    • Soler-Marta-nez, A. Sabater-García, F. and Lozano, J.A. Inhibidores estructurales de fenolasa de albaricoque, Rev. Esp. Fisiol, 21, 139, 1965.
    • (1965) Sabater-García, F. and , vol.21 , Issue.139
    • Lozano, J.A.1
  • 196
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase, J. Biol. Chem
    • Duckworth, H.W. and Coleman, J.E. Physicochemical and kinetic properties of mushroom tyrosinase, J. Biol. Chem. 245, 1613, 1970.
    • (1970) , vol.245
    • Duckworth, H.W.1    Coleman, J.E.2
  • 197
    • 84952432306 scopus 로고
    • Inhibition of apple catechol oxidase by a galactose oxidase inhibitor from Dactilium dendroides, Irs. J.
    • Bot. 16, 38
    • Harel, E. Mayer, A.M. Markus, Z. and Avigad, G. Inhibition of apple catechol oxidase by a galactose oxidase inhibitor from Dactilium dendroides, Irs. J. Bot. 16, 38, 1967.
    • (1967)
    • Harel, E.1    Mayer, A.M.2    Markus, Z.3    Avigad, G.4
  • 198
    • 84952410678 scopus 로고
    • Natriumchlorid als Inhibitor bei der enzymatischen Braunung von a.pfeln, Nahrung
    • Taufel, K. and Voigt, T. Natriumchlorid als Inhibitor bei der enzymatischen Braunung von a.pfeln, Nahrung, 8, 80, 1964.
    • (1964) , vol.8 , Issue.80
    • Taufel, K.1    Voigt, T.2
  • 199
    • 84952432307 scopus 로고
    • The action of polyphenolic compounds on enzymes, Biochem. J.
    • 95, 24P
    • Sanderson, G.W. The action of polyphenolic compounds on enzymes, Biochem. J. 95, 24P, 1965.
    • (1965)
    • Sanderson, G.W.1
  • 200
    • 0017602076 scopus 로고
    • Extraction and some properties of the o-diphenoloxidase and peroxidase inhibitor from the leaves of the tea plant, Prikl. Biokhim. Mikrobiol
    • Pruidze, G.N. and Grigorashvili, G.Z. Extraction and some properties of the o-diphenoloxidase and peroxidase inhibitor from the leaves of the tea plant, Prikl. Biokhim. Mikrobiol. 13, 104, 1977.
    • (1977) , vol.13 , Issue.104
    • Pruidze, G.N.1    Grigorashvili, G.Z.2
  • 201
    • 3643134198 scopus 로고
    • Use of poly(vinyl-) pyrrolidinone in the isolation of enzymes from chloroplasts, Phytochemistry
    • Jones, J.D. Hulme, A.C. and Wooltorton, L.S.C. Use of poly(vinyl-) pyrrolidinone in the isolation of enzymes from chloroplasts, Phytochemistry, 4, 659, 1965.
    • (1965) , vol.4 , Issue.659
    • Jones, J.D.1    Hulme, A.C.2    Wooltorton, L.S.C.3
  • 202
    • 0008065947 scopus 로고
    • 2,3-Naphthalenediol, a specific competitive inhibitor of phenolase, Phytochemistry
    • Mayer, A.M. Harel, E. and Shain, Y. 2,3-Naphthalenediol, a specific competitive inhibitor of phenolase, Phytochemistry, 3, 447, 1964.
    • (1964) , vol.3 , Issue.447
    • Mayer, A.M.1    Harel, E.2    Shain, Y.3
  • 203
    • 85007903070 scopus 로고
    • of antibiotics on the enzyme formation, Agrie. Biol. Chem
    • Effect
    • Takeo, T. Tea leaf polyphenol oxidase. V. Effect of antibiotics on the enzyme formation, Agrie. Biol. Chem. 30, 1211, 1966.
    • (1966) Tea leaf polyphenol oxidase. V. , vol.30
    • Takeo, T.1
  • 204
    • 0040937201 scopus 로고
    • Effect of succinic acid-2,2-dimethyl-hydrazide on mushroom o-diphenol oxidase, J. Am. Soc. Hortic. Sei
    • Murr, D.P. and Morris, L.L. Effect of succinic acid-2,2-dimethyl-hydrazide on mushroom o-diphenol oxidase, J. Am. Soc. Hortic. Sei. 99, 3, 1974.
    • (1974) , vol.99 , Issue.3
    • Murr, D.P.1    Morris, L.L.2
  • 205
    • 84987368447 scopus 로고
    • Inhibition of o-diphenol oxidase by dichlorodi-fluoromethane, J. Food Sei
    • Warmbier, H.C. Fennema, O. and Marth, E.H. Inhibition of o-diphenol oxidase by dichlorodi-fluoromethane, J. Food Sei. 37, 702, 1972.
    • (1972) , vol.37 , Issue.702
    • Warmbier, H.C.1    Fennema, O.2    Marth, E.H.3
  • 206
    • 0016088109 scopus 로고
    • The effect of sulphur dioxide on oxidising enzyme systems in plant tissues, J. Sei. Food Agrie
    • Haisman, D.R. The effect of sulphur dioxide on oxidising enzyme systems in plant tissues, J. Sei. Food Agrie. 25, 803, 1974.
    • (1974) , vol.25 , Issue.803
    • Haisman, D.R.1
  • 207
    • 84982361122 scopus 로고
    • Action of a ring-cleaving oxygenase in preventing oxidative darkening of apple juice, J. Sei. Food Agrie
    • Kelly, S.H. and Finkle, B.J. Action of a ring-cleaving oxygenase in preventing oxidative darkening of apple juice, J. Sei. Food Agrie. 20, 629, 1969.
    • (1969) , vol.20 , Issue.629
    • Kelly, S.H.1    Finkle, B.J.2
  • 208
    • 1842532834 scopus 로고
    • Enzyme reactions with phenolic compounds: effect of o-methyltransferase on a natural substrate of fruit polyphenol oxidase, Nature
    • Finkle, B.J. and Nelson, R.F. Enzyme reactions with phenolic compounds: effect of o-methyltransferase on a natural substrate of fruit polyphenol oxidase, Nature, 197, 902, 1963.
    • (1963) , vol.197 , Issue.902
    • Finkle, B.J.1    Nelson, R.F.2
  • 209
    • 84952405843 scopus 로고
    • Effect of syrup density on colour, texture and flavour of canned cling peaches, Food Technol. Aust
    • Czerkaskyj, A. Effect of syrup density on colour, texture and flavour of canned cling peaches, Food Technol. Aust. 25, 246, 1973.
    • (1973) , vol.25 , Issue.246
    • Czerkaskyj, A.1
  • 211
    • 84952380725 scopus 로고
    • Chem.
    • Univ. P.R. 50, 113, Abstr. 65, 2542h, 1966.
    • Alexander, A.G. The oxidizing enzymes of sugar cane tyrosinase (polyphenoloxidase), J. Agrie. Univ. P.R. 50, 113, 1966; Chem. Abstr. 65, 2542h, 1966.
    • (1966)
    • Alexander, A.G.1
  • 212
    • 0013905182 scopus 로고
    • On the purification and properties of mushroom tyrosinase, J. Biochem
    • Nakamura, T. Sho, S. and Ogura, Y. On the purification and properties of mushroom tyrosinase, J. Biochem. 59, 481, 1966.
    • (1966) , vol.59 , Issue.481
    • Nakamura, T.1    Sho, S.2    Ogura, Y.3
  • 213
    • 84952432311 scopus 로고
    • Efectos del diaxido de carbono sobre la actividad de la polifenoloxidasa de manzanas Red Delicious, Rev. Agroquim. Tecnol. Aliment
    • Chaves, A.R. and Tomais, J.O. Efectos del diaxido de carbono sobre la actividad de la polifenoloxidasa de manzanas Red Delicious, Rev. Agroquim. Tecnol. Aliment. 16, 114, 1976.
    • (1976) , vol.16 , Issue.114
    • Chaves, A.R.1    Tomais, J.O.2
  • 214
    • 0011985180 scopus 로고
    • Influence of carbon monoxide, carbon dioxide, and oxygen levels on brown stain, respiration rate and visual quality of lettuce, J. Am. Soc. Hortic. Sei
    • Kader, A.A. Brecht, P.E. Woodruff, R. and Morris, L.L. Influence of carbon monoxide, carbon dioxide, and oxygen levels on brown stain, respiration rate and visual quality of lettuce, J. Am. Soc. Hortic. Sei. 98, 485, 1973.
    • (1973) , vol.98 , Issue.485
    • Kader, A.A.1    Brecht, P.E.2    Woodruff, R.3    Morris, L.L.4
  • 215
    • 84952382990 scopus 로고
    • Ricerche sulla polifenolossidasi delle uve: III-Stabilita ed inattivazione dell'enzima, Ind. Agrar
    • Montedoro, G. and Cantarelli, C. Ricerche sulla polifenolossidasi delle uve: III-Stabilita ed inattivazione dell'enzima, Ind. Agrar. 7, 323, 1969.
    • (1969) , vol.7 , Issue.323
    • Montedoro, G.1    Cantarelli, C.2
  • 216
    • 84952420292 scopus 로고
    • Inhibition of friction discoloration on d-Anjou pears by 2-mercaptobenzthiazole, Hort Science
    • Wang, C.Y. and Mellenthin, W.M. Inhibition of friction discoloration on d-Anjou pears by 2-mercaptobenzthiazole, Hort Science, 9, 196, 1974.
    • (1974) , vol.9 , Issue.196
    • Wang, C.Y.1    Mellenthin, W.M.2
  • 217
    • 0013950964 scopus 로고
    • Catechol oxidases, endogenous substrates and browning in developing apples, J. Sei. Food Agrie
    • Harel, E. Mayer, M. and Shain, Y. Catechol oxidases, endogenous substrates and browning in developing apples, J. Sei. Food Agrie. 17, 389, 1966.
    • (1966) , vol.17 , Issue.389
    • Harel, E.1    Mayer, M.2    Shain, Y.3
  • 218
    • 84952398941 scopus 로고
    • Zur inhibierenden Wirkung von Ascorbinsaure gegenaber der Polyphenoloxidase des Apfels, Z. Lebensm. Unters. Forsch
    • Taufel, K. and Voigt, J. Zur inhibierenden Wirkung von Ascorbinsaure gegenaber der Polyphenoloxidase des Apfels, Z. Lebensm. Unters. Forsch. 126, 19, 1964.
    • (1964) , vol.126 , Issue.19
    • Taufel, K.1    Voigt, J.2
  • 220
    • 0016697349 scopus 로고
    • Enzymatische Braunung und ihre Hemmung durch verschiedene Substanzen, Mitt. Geb. Lobensmittelunters. Hyg
    • Dimpfl, D. and Somogyi, J.C. Enzymatische Braunung und ihre Hemmung durch verschiedene Substanzen, Mitt. Geb. Lobensmittelunters. Hyg. 66, 183, 1975.
    • (1975) , vol.66 , Issue.183
    • Dimpfl, D.1    Somogyi, J.C.2
  • 221
    • 0000797618 scopus 로고
    • The effect of ascorbic acid on the enzymatic oxidation of monohydric and o-dihydric phenols, J. Am. Chem. Soc
    • Krueger, R.C. The effect of ascorbic acid on the enzymatic oxidation of monohydric and o-dihydric phenols, J. Am. Chem. Soc. 72, 5582, 1950.
    • (1950) , vol.72
    • Krueger, R.C.1
  • 222
    • 8644264860 scopus 로고
    • Effect of ascorbic acid on polyphenol oxidase, J. Am. Chem. Soc
    • Ingraham, L.L. Effect of ascorbic acid on polyphenol oxidase, J. Am. Chem. Soc. 78, 5095, 1956.
    • (1956) , vol.78
    • Ingraham, L.L.1
  • 223
    • 8644278553 scopus 로고
    • The effect of ascorbic acid on the inactivation of tyrosinase, J. Am. Chem. Soc
    • Scharf, W. and Dawson, C.R. The effect of ascorbic acid on the inactivation of tyrosinase, J. Am. Chem. Soc. 80, 4627, 1958.
    • (1958) , vol.80
    • Scharf, W.1    Dawson, C.R.2
  • 224
    • 84952432314 scopus 로고
    • aoeber die Rolle der Ascorbinsaure als Inhibitor enzymatischer Braunungsreaktionen, Z. Lebensm. Unters. Forsch
    • Duden R. and Siddiqui, I.R. aoeber die Rolle der Ascorbinsaure als Inhibitor enzymatischer Braunungsreaktionen, Z. Lebensm. Unters. Forsch. 132, 1, 1966.
    • (1966) , vol.132 , Issue.1
    • Duden, R.1    Siddiqui, I.R.2
  • 225
    • 84952432315 scopus 로고
    • aoeber das Verhalten geschalter Tafelapfel wahrend kurzfristiger Lagerung bei Verwendung von L-Ascorbinsaure, Erwerbsobstbau
    • Eid, K. and Holfelder, E. aoeber das Verhalten geschalter Tafelapfel wahrend kurzfristiger Lagerung bei Verwendung von L-Ascorbinsaure, Erwerbsobstbau, 15, 55, 1973.
    • (1973) , vol.15 , Issue.55
    • Eid, K.1    Holfelder, E.2
  • 226
    • 84987324910 scopus 로고
    • Pre-freezing processing of Golden Delicious apple slices, J. Food Sei
    • Ponting, J.D. and Jackson, R. Pre-freezing processing of Golden Delicious apple slices, J. Food Sei. 37, 812, 1972.
    • (1972) , vol.37 , Issue.812
    • Ponting, J.D.1    Jackson, R.2
  • 227
    • 84952432316 scopus 로고
    • Preservation of apple slices with a solution consisting of ascorbic A.cid
    • calcium chloride and sodium bicarbonate, U.S. Patent 3,754,938
    • Ponting, J.D. Preservation of apple slices with a solution consisting of ascorbic A.cid, calcium chloride and sodium bicarbonate, U.S. Patent 3,754,938, 1973.
    • (1973)
    • Ponting, J.D.1
  • 228
    • 84952432317 scopus 로고
    • Influence of polyphenol oxidase inhibitors on the enzymic browning of apples, in Proc. 18th Hung.
    • Annu. Meet. Biochem. 201.
    • Gajzaiga, I. Vaimos-Vigyaiza, L. and Sameghy-Kerezsi, N. Influence of polyphenol oxidase inhibitors on the enzymic browning of apples, in Proc. 18th Hung. Annu. Meet. Biochem. 1978, 201.
    • (1978)
    • Gajzaiga, I.1    Vaimos-Vigyaiza, L.2    Sameghy-Kerezsi, N.3
  • 229
    • 84952389077 scopus 로고
    • The mechanism of sulfite inhibition of browning caused by polyphenol oxidase, J. Food Sei
    • Embs, R.J. and Markakis, P. The mechanism of sulfite inhibition of browning caused by polyphenol oxidase, J. Food Sei. 30, 753, 1965.
    • (1965) , vol.30 , Issue.753
    • Embs, R.J.1    Markakis, P.2
  • 230
    • 84952416590 scopus 로고
    • Effect of sulfite and ascorbic acid on mushroom phenol oxidase, J. Food Sei
    • Markakis, P. and Embs, R.J. Effect of sulfite and ascorbic acid on mushroom phenol oxidase, J. Food Sei. 31, 807, 1966.
    • (1966) , vol.31 , Issue.807
    • Markakis, P.1    Embs, R.J.2
  • 231
    • 51849178948 scopus 로고
    • Bisulfite inhibition of enzymatic blackening caused by tyrosine oxidation, Am. Potato J
    • Muneta, P. Bisulfite inhibition of enzymatic blackening caused by tyrosine oxidation, Am. Potato J. 43, 397, 1966.
    • (1966) , vol.43 , Issue.397
    • Muneta, P.1
  • 232
    • 77951505035 scopus 로고
    • and Hsi W. Influence of pH and bisulfite on the enzymatic blackening reaction in potatotes, Am. Potato J
    • Muneta, P. and Hsi W. Influence of pH and bisulfite on the enzymatic blackening reaction in potatotes, Am. Potato J. 54, 73, 1977.
    • (1977) , vol.54 , Issue.73
    • Muneta, P.1
  • 233
    • 85023285601 scopus 로고
    • The control of enzymatic browning of fruits
    • in Food Enzymes, Schultz, H.W. Ed. AVI Publishing, Westport, Conn., chap.
    • Ponting, J.D. The control of enzymatic browning of fruits, in Food Enzymes, Schultz, H.W. Ed. AVI Publishing, Westport, Conn. 1960, chap. 6.
    • (1960) , pp. 6
    • Ponting, J.D.1
  • 234
    • 84952432319 scopus 로고
    • Oxidative enzymes in grapes, Ann. Nutr.
    • Aliment. 21, B 205
    • Poux, C. Oxidative enzymes in grapes, Ann. Nutr. Aliment. 21, B 205, 1967.
    • (1967)
    • Poux, C.1
  • 236
    • 84952432321 scopus 로고
    • Chemical inactivation of enzymes in vegetables before dehydration. Food Technol
    • Makower, U. Chemical inactivation of enzymes in vegetables before dehydration. Food Technol. 15, 160, 1960.
    • (1960) , vol.15 , Issue.160
    • Makower, U.1
  • 237
    • 84952390191 scopus 로고
    • Bedeutung der schwefligen Saure far die Traubensaftherstellung und ihre lebensmittelrechtlichen Aspekte, Fluess. Obst
    • Wucherpfennig, K. Bedeutung der schwefligen Saure far die Traubensaftherstellung und ihre lebensmittelrechtlichen Aspekte, Fluess. Obst, 42, 451, 1975.
    • (1975) , vol.42 , Issue.451
    • Wucherpfennig, K.1
  • 238
    • 84952432322 scopus 로고
    • Anon. Reduccian del empleo de SO2 en vinos. Informacian taccnica
    • Rev. Agroquim. Tecnol. Aliment. 11, 480
    • Anon. Reduccian del empleo de SO2 en vinos. Informacian taccnica, Rev. Agroquim. Tecnol. Aliment. 11, 480, 1971.
    • (1971)
  • 239
    • 84952432323 scopus 로고
    • Additives Extend Shelf Ufe
    • 3,305,366, cited in Pintauro, Noyes Data Corporation, Oak Food Technol. Review, 17, 217, 1974.
    • Sutton, W.J. and Lauck, R.M. U.S. Patent 3,305,366, 1967; cited in Pintauro, N.D. Food Additives Extend Shelf Ufe, Noyes Data Corporation, Oak Ridge, N.J. ; Food Technol. Review, 17, 217, 1974.
    • (1967)
    • Sutton, W.J.1    Lauck, R.2    Food, N.D.3    Ridge, N.J.4
  • 240
    • 84952432324 scopus 로고
    • Stabilization of wine with insoluble poly(vinylpyrrolidone), Vinodel. Vinogr
    • Shpritsman, E.M. Roytburd, G.V. and Lukyanets, T.S. Stabilization of wine with insoluble poly(vinylpyrrolidone), Vinodel. Vinogr. 6, 14, 1977.
    • (1977) , vol.6 , Issue.14
    • Shpritsman, E.M.1    Roytburd, G.V.2    Lukyanets, T.S.3
  • 241
    • 84989990687 scopus 로고
    • Cysteine inhibition of enzymatic blackening with polyphenol oxidase from potatoes, J. Food Sei
    • Muneta, P. and Walradt, J. Cysteine inhibition of enzymatic blackening with polyphenol oxidase from potatoes, J. Food Sei. 33, 606, 1968.
    • (1968) , vol.33 , Issue.606
    • Muneta, P.1    Walradt, J.2
  • 242
    • 84968425471 scopus 로고
    • Enzymic browning in green olives and its prevention, J. Sei. Food Agrie
    • Ben-Shalom. N. Harel, E. and Mayer, A.M. Enzymic browning in green olives and its prevention, J. Sei. Food Agrie. 29, 398, 1978.
    • (1978) , vol.29 , Issue.398
    • Ben-Shalom, N.1    Harel, E.2    Mayer, A.M.3
  • 243
    • 0010272134 scopus 로고
    • Properties and solubility of phenolase in isolated chloroplasts, Nature
    • Mayer, M. and Friend, J. Properties and solubility of phenolase in isolated chloroplasts, Nature, 185, 464, 1960.
    • (1960) , vol.185 , Issue.464
    • Mayer, M.1    Friend, J.2
  • 245
    • 84982353224 scopus 로고
    • Peroxidase and polyphenol oxidase activities in developing peaches, J. Food Sei
    • Flurkey, W.H. and Jen, J.J. Peroxidase and polyphenol oxidase activities in developing peaches, J. Food Sei. 43, 1826, 1978.
    • (1978) , vol.43
    • Flurkey, W.H.1    Jen, J.J.2
  • 246
    • 0013889082 scopus 로고
    • Double behaviour of o-diphenol:O2 oxydoreductase from apricot, Rev. Esp. Fisiol
    • Soler, A. Lozano, J.A. and Sabater, F. Double behaviour of o-diphenol:O2 oxydoreductase from apricot, Rev. Esp. Fisiol. 22, 7, 1966.
    • (1966) , vol.22 , Issue.7
    • Soler, A.1    Lozano, J.A.2    Sabater, F.3
  • 247
    • 0000677924 scopus 로고
    • Extraction of soluble catechol oxidase from tea shoot tips, Biochim. Biophys. Acta
    • Sanderson, G.W. Extraction of soluble catechol oxidase from tea shoot tips, Biochim. Biophys. Acta, 92, 622, 1964.
    • (1964) , vol.92 , Issue.622
    • Sanderson, G.W.1
  • 248
    • 0001678949 scopus 로고
    • Extraction of enzymes and subcellular organelles from plant tissues, Phytochemistry
    • Anderson, J.W. Extraction of enzymes and subcellular organelles from plant tissues, Phytochemistry, 7, 1973, 1968.
    • (1968) , vol.7 , pp. 1973
    • Anderson, J.W.1
  • 249
    • 0000070711 scopus 로고
    • Plant phenolic compounds and the isolation of plant enzymes, Phytochemistry
    • Loomis, W.D. and Battaile, J. Plant phenolic compounds and the isolation of plant enzymes, Phytochemistry, 5, 423, 1966.
    • (1966) , vol.5 , Issue.423
    • Loomis, W.D.1    Battaile, J.2
  • 250
    • 0001403475 scopus 로고
    • Removal of phenolic compounds during the isolation of plant enzymes, Methods Enzymol
    • Loomis, W.D. Removal of phenolic compounds during the isolation of plant enzymes, Methods Enzymol, 13, 555, 1968.
    • (1968) , vol.13 , Issue.555
    • Loomis, W.D.1
  • 251
    • 0000517747 scopus 로고
    • Optimum conditions for bonding plant phenols to insoluble polyvinylpyrrolidone, Phytochemistry
    • Anderson, R.A. and Sowers, J.A. Optimum conditions for bonding plant phenols to insoluble polyvinylpyrrolidone, Phytochemistry, 7, 293, 1968.
    • (1968) , vol.7 , Issue.293
    • Anderson, R.A.1    Sowers, J.A.2
  • 252
    • 0001411488 scopus 로고
    • Polyethylene glycols-tannins interaction in extracting enzymes, Nature
    • Badran, A.M. and Jones, D.E. Polyethylene glycols-tannins interaction in extracting enzymes, Nature, 206, 622, 1965.
    • (1965) , vol.206 , Issue.622
    • Badran, A.M.1    Jones, D.E.2
  • 253
    • 49849116188 scopus 로고
    • The use of a fungal pectate lyase in the purification of laccase from peaches, Phytochemistry
    • Harel, E. and Mayer, M. The use of a fungal pectate lyase in the purification of laccase from peaches, Phytochemistry, 9, 2447, 1970.
    • (1970) , vol.9
    • Harel, E.1    Mayer, M.2
  • 254
    • 0016845131 scopus 로고
    • forms of soluble monophenol, dihydroxyphenylalanine: oxygen-oxidoreductase E.C.
    • 14.18.1 from potato tubers Solanum tuberosum, Z. Lebensm. Unters Forsch. 157, 221
    • Matheis, G. and Belitz, H.-D. Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen-oxidoreductase (E.C. 1.14.18.1) from potato tubers (Solanum tuberosum), Z. Lebensm. Unters Forsch. 157, 221, 1975.
    • (1975)
    • Matheis, G.1    Belitz, H.-D.2
  • 255
    • 84981868588 scopus 로고
    • Multiple forms of phenoloxidase, J. Food Sei
    • Constantinides, S.M. and Bedford, C.L. Multiple forms of phenoloxidase, J. Food Sei. 32, 446, 1967.
    • (1967) , vol.32 , Issue.446
    • Constantinides, S.M.1    Bedford, C.L.2
  • 256
    • 0016223415 scopus 로고
    • localization, isoenzyme composition and activity of apple o-diphenoloxidase, Prikt. Biokhim. Mikrobiol
    • Intracellular
    • Demenyuk, M.N. Nizharadze, A.N. and Sal'Kova, E.G. Intracellular localization, isoenzyme composition and activity of apple o-diphenoloxidase, Prikt. Biokhim. Mikrobiol. 10, 659, 1974.
    • (1974) , vol.10 , Issue.659
    • Demenyuk, M.N.1    Nizharadze, A.N.2    Sal'Kova, E.G.3
  • 257
    • 4544340068 scopus 로고
    • and Ribacreau-Gayon, P. Isoelectric point changes in Vitis vinifera catechol oxidase, Phytochemistry
    • Dubernet, M. and Ribacreau-Gayon, P. Isoelectric point changes in Vitis vinifera catechol oxidase, Phytochemistry, 13, 1085, 1974.
    • (1974) , vol.13
    • Dubernet, M.1
  • 258
    • 84952432329 scopus 로고
    • Proteine solubili ed isoenzimi della perossidasi, fosfatasi acida, amilasi, invertasi, fenolasi, esterasi e catalasi delle bucce e dei succhi di sei uve, Ind. Agrar
    • Pallavicini, C. Proteine solubili ed isoenzimi della perossidasi, fosfatasi acida, amilasi, invertasi, fenolasi, esterasi e catalasi delle bucce e dei succhi di sei uve, Ind. Agrar. 9, 301, 1971.
    • (1971) , vol.9 , Issue.301
    • Pallavicini, C.1
  • 259
    • 1842331392 scopus 로고
    • Electrophoretic separation of the phenolases from potato tubers, Nature
    • Patil, S. and Evans, H.J. Electrophoretic separation of the phenolases from potato tubers, Nature. 200, 1322, 1963.
    • (1963) , vol.200
    • Patil, S.1    Evans, H.J.2
  • 260
    • 0018233160 scopus 로고
    • Thin-layer isoelectric focusing of polyphenoloxidase on Sephadex and its detection by the print technique, Anal. Biochem
    • Thomas, P. Delincee, H. and Diehl, J.F. Thin-layer isoelectric focusing of polyphenoloxidase on Sephadex and its detection by the print technique, Anal. Biochem. 88, 138, 1978.
    • (1978) , vol.88 , Issue.138
    • Thomas, P.1    Delincee, H.2    Diehl, J.F.3
  • 261
    • 0018195665 scopus 로고
    • Isolation and some properties of potato o-diphenoloxidase, Biokhimiya
    • Anisimov, V.D. Kastal'Eva, T.B. and Loginova, L.N. Isolation and some properties of potato o-diphenoloxidase, Biokhimiya, 43, 1616, 1978.
    • (1978) , vol.43
    • Anisimov, V.D.1    Kastal'Eva, T.B.2    Loginova, L.N.3
  • 262
    • 0016864398 scopus 로고
    • Lebensm. Unters. Forsch
    • Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamid-Gelen von Proteinen und Enzymen aus Tomaten, Gurken, Zuckermais and
    • Drawert, F. and Garg, A. aoeber die elektrophoretische Differenzierung and Klassifizierung von Proteinen. VI. Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamid-Gelen von Proteinen und Enzymen aus Tomaten, Gurken, Zuckermais and Zwiebeln, Z. Lebensm. Unters. Forsch. 159, 23, 1975.
    • (1975) aoeber die elektrophoretische Differenzierung and Klassifizierung von Proteinen. VI. , vol.159 , Issue.23
    • Drawert, F.1    Zwiebeln, Z.2
  • 263
    • 0000411077 scopus 로고
    • The multiple forms of mushroom tyrosinase. Purification and molecular properties, J. Biol. Chem
    • Bouchilloux, M. Mcmahill, P. and Mason, H.S. The multiple forms of mushroom tyrosinase. Purification and molecular properties, J. Biol. Chem. 238, 1699, 1963.
    • (1963) , vol.238
    • Bouchilloux, M.1    Mcmahill, P.2    Mason, H.S.3
  • 264
    • 0001998592 scopus 로고
    • The multiple forms of mushroom tyrosinase. Interconversion, J.
    • Biol. Chem. 240, PC1489
    • Jolley, R.L. and Mason, H.S. The multiple forms of mushroom tyrosinase. Interconversion, J. Biol. Chem. 240, PC1489, 1965.
    • (1965)
    • Jolley, R.L.1    Mason, H.S.2
  • 266
    • 0006011496 scopus 로고
    • Catechol oxidase: enzymic liberation from sugar beet chloroplasts, Phytochemistry
    • Mayer, A.M. Catechol oxidase: enzymic liberation from sugar beet chloroplasts, Phytochemistry, 5, 1297, 1966.
    • (1966) , vol.5
    • Mayer, A.M.1
  • 267
    • 0039833249 scopus 로고
    • Polyphenoloxidase “tyrosinase”: purification and molecular properties, Nature
    • Kertesz, D. and Zito, R. Polyphenoloxidase (“tyrosinase”): purification and molecular properties, Nature. 170, 1017, 1957.
    • (1957) , vol.170
    • Kertesz, D.1    Zito, R.2
  • 268
    • 0017784967 scopus 로고
    • Lebensm. Unters.
    • C. 1.14.18.1 from potato tubers Solanum tuberosum. II. Partial characterization of the enzyme forms with different molecular Forsch. 163, 279
    • Matheis, G. and Belitz, H.-D. Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen-oxidoreductase. (E.C. 1.14.18.1) from potato tubers (Solanum tuberosum). II. Partial characterization of the enzyme forms with different molecular Weights, Z. Lebensm. Unters. Forsch. 163, 279, 1977.
    • (1977)
    • Matheis, G.1    Belitz, H.-D.2    Weights, Z.3
  • 269
    • 0005967496 scopus 로고
    • Multiple forms of Vitis vinifera catechol oxidase, Phytochemistry
    • Harel, E. Mayer, A.M. and Lehman, E. Multiple forms of Vitis vinifera catechol oxidase, Phytochemistry, 12, 2649, 1973.
    • (1973) , vol.12
    • Harel, E.1    Mayer, A.M.2    Lehman, E.3
  • 270
    • 0018518099 scopus 로고
    • forms of soluble monophenol, dihydroxyphenylalanine: oxygen oxidoreductase E.C.
    • 14.18.1 from potato tubers Solanum tuberosum, Z. Lebensm. Unters. Forsch. 169, 271
    • Matheis, G. and Belitz, H.-D. Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen oxidoreductase (E.C. 1.14.18.1) from potato tubers (Solanum tuberosum), Z. Lebensm. Unters. Forsch. 169, 271, 1979.
    • (1979)
    • Matheis, G.1    Belitz, H.-D.2
  • 271
    • 0016524088 scopus 로고
    • Study of oxidative enzymes of the lignindegrading fungus Pleurotus ostreatus, Prikl. Biokhim. Mikrobiol
    • Ulezlo, I.V. Uporova, T.M. and Feniksova, R.V. Study of oxidative enzymes of the lignindegrading fungus Pleurotus ostreatus, Prikl. Biokhim. Mikrobiol. 11, 535, 1975.
    • (1975) , vol.11 , Issue.535
    • Ulezlo, I.V.1    Uporova, T.M.2    Feniksova, R.V.3
  • 272
    • 0017312637 scopus 로고
    • Isoelectric points and molecular weights of proteins. A table, J. Chromatogr
    • Righetti, P.G. and Caravaggio, T. Isoelectric points and molecular weights of proteins. A table, J. Chromatogr. 127, 1, 1976.
    • (1976) , vol.127 , Issue.1
    • Righetti, P.G.1    Caravaggio, T.2
  • 273
    • 0000838740 scopus 로고
    • Harel, E. and Ben-Shaul, R. Assay of catechol oxidase-a critical comparison of methods, Phytochemistry
    • Mayer, A.M. Harel, E. and Ben-Shaul, R. Assay of catechol oxidase-a critical comparison of methods, Phytochemistry, 5, 783, 1966.
    • (1966) , vol.5 , Issue.783
    • Mayer, A.M.1
  • 274
    • 84952432336 scopus 로고
    • aber die Anwendung der colorimetrischen Methoden, Z. Lebensm. Unters. Forsch
    • I. Untersuchungen
    • Heimann, W. and Andler, St. Zur Aktivitatsbestimmung der Polyphenoloxidase. I. Untersuchungen aber die Anwendung der colorimetrischen Methoden, Z. Lebensm. Unters. Forsch. 117, 121, 1962.
    • (1962) Andler, St. Zur Aktivitatsbestimmung der Polyphenoloxidase. , vol.117 , Issue.121
    • Heimann, W.1
  • 276
    • 84916775752 scopus 로고
    • A method for determining polyphenol oxidase activity in fruits and vegetables applying a natural substrate, Acta Aliment. Acad. Sei. Hung
    • Mihailyi, K. and Vaimos-Vigyaiza, L. A method for determining polyphenol oxidase activity in fruits and vegetables applying a natural substrate, Acta Aliment. Acad. Sei. Hung. 5, 69, 1976.
    • (1976) , vol.5 , Issue.69
    • Mihailyi, K.1    Vaimos-Vigyaiza, L.2
  • 277
    • 84952432338 scopus 로고
    • Preliminary studies of mushroom tyrosinase polyphenol oxidase, Mushroom Sei
    • Long, T.J. and Alben, J.O. Preliminary studies of mushroom tyrosinase (polyphenol oxidase), Mushroom Sei. 7, 69, 1969.
    • (1969) , vol.7 , Issue.69
    • Long, T.J.1    Alben, J.O.2
  • 278
    • 84952432339 scopus 로고
    • and Andler, St. Zur Aktivitatsbestimmung der Polyphenoloxidase. III. Eine polarometrische Methode zur Bestimmung der Phenolaseaktivitat, Z. Lebensm. Unters. Forsch
    • Heimann, W. and Andler, St. Zur Aktivitatsbestimmung der Polyphenoloxidase. III. Eine polarometrische Methode zur Bestimmung der Phenolaseaktivitat, Z. Lebensm. Unters. Forsch. 117, 203, 1962.
    • (1962) , vol.117 , Issue.203
    • Heimann, W.1
  • 279
    • 0001178114 scopus 로고
    • Frieden, E. A spectrophotometric method for the determination of the catecholase activity of tyrosinase and some of its applications, J. Am. Chem. Soc
    • El-Bayoumi, M.A. and Frieden, E. A spectrophotometric method for the determination of the catecholase activity of tyrosinase and some of its applications, J. Am. Chem. Soc. 79, 4854, 1957.
    • (1957) , vol.79
    • El-Bayoumi, M.A.1
  • 280
    • 0345178046 scopus 로고
    • A comparison of the properties of two forms of tyrosinase from Neurospora crassa, Arch. Biochem. Biophys
    • Sussmann, A.S. A comparison of the properties of two forms of tyrosinase from Neurospora crassa, Arch. Biochem. Biophys. 95, 407, 1961.
    • (1961) , vol.95 , Issue.407
    • Sussmann, A.S.1
  • 281
    • 84952432341 scopus 로고
    • Reinvestigation of phenol oxidase activity by improved analytical techniques, Diss. Abstr.
    • 36(7), 3340-B
    • Garrett, B.C. Reinvestigation of phenol oxidase activity by improved analytical techniques, Diss. Abstr. 36(7), 3340-B, 1976.
    • (1976)
    • Garrett, B.C.1
  • 282
    • 0015611566 scopus 로고
    • A spectrophotometric method for the determination of the catecholase activity of tyrosinase by Besthorn's hydrazone, Anal. Biochem
    • Pifferi, P.G. and Baldassari, L. A spectrophotometric method for the determination of the catecholase activity of tyrosinase by Besthorn's hydrazone, Anal. Biochem. 52, 325, 1973.
    • (1973) , vol.52 , Issue.325
    • Pifferi, P.G.1    Baldassari, L.2
  • 283
    • 0017165709 scopus 로고
    • An improvement of the spectrophotometric method for the determination of tyrosinase catecholase activity by Besthorn's hydrazone, Anal. Biochem
    • Mazzocco, F. and Pifferi, P.G. An improvement of the spectrophotometric method for the determination of tyrosinase catecholase activity by Besthorn's hydrazone, Anal. Biochem. 72, 643, 1976.
    • (1976) , vol.72 , Issue.643
    • Mazzocco, F.1    Pifferi, P.G.2
  • 284
    • 0017359959 scopus 로고
    • A rapid assay for catechol oxidase and lacease using 2-nitro-5-thiobenzoic acid, Anal. Biochem
    • Esterbauer, H. Schwarzl, E. and Hayn, M. A rapid assay for catechol oxidase and lacease using 2-nitro-5-thiobenzoic acid, Anal. Biochem. 77, 486, 1977.
    • (1977) , vol.77 , Issue.486
    • Esterbauer, H.1    Schwarzl, E.2    Hayn, M.3
  • 286
    • 84952432343 scopus 로고
    • Valoracian de los principales sustratos causantes del pardeamiento enzimaitico en diversas variedades de manzanas chilenas, An. Fac. Quim. Farm. Univ. Chile
    • Scheel Mahn, M. Valoracian de los principales sustratos causantes del pardeamiento enzimaitico en diversas variedades de manzanas chilenas, An. Fac. Quim. Farm. Univ. Chile, 19, 112, 1968.
    • (1968) , vol.19 , Issue.112
    • Scheel, M.1
  • 287
    • 84952432344 scopus 로고
    • Studies into the enzymic browning and the polyphenol-polyphenol oxidase complex of apple cultivars
    • I. and Confructa, 21, 24
    • Vaimos-Vigyaiza, L. Mihailyi, K. Gajzaigo, I. and Naidudvari-Mairkus, V. Studies into the enzymic browning and the polyphenol-polyphenol oxidase complex of apple cultivars, Confructa, 21, 24, 1976.
    • (1976)
    • Vaimos-Vigyaiza, L.1    Gajzaigo, K.2    Naidudvari-Mairkus, V.3
  • 288
    • 84952432345 scopus 로고
    • The role of enzyme-substrate ratio in the enzymatic browning of fruit tissue homogenates, Acta Aliment. Acad.
    • I. and Sei. Hung. 6, 379
    • Vaimos-Vigyaiza, L. Mihailyi, K. Gajzaigo, I. and Naidudvari-Mairkus, V. The role of enzyme-substrate ratio in the enzymatic browning of fruit tissue homogenates, Acta Aliment. Acad. Sei. Hung. 6, 379, 1977.
    • (1977)
    • Vaimos-Vigyaiza, L.1    Gajzaigo, K.2    Naidudvari-Mairkus, V.3
  • 289
    • 0347824126 scopus 로고
    • The effect of bruising on discoloration and concentration of phenolic compounds in apple tissue, Proc. Am. Soc. Hortic. Sei
    • Ingle, M. and Hyde, J.F. The effect of bruising on discoloration and concentration of phenolic compounds in apple tissue, Proc. Am. Soc. Hortic. Sei. 93, 738, 1968.
    • (1968) , vol.93 , Issue.738
    • Ingle, M.1    Hyde, J.F.2
  • 290
    • 84914022784 scopus 로고
    • Transformations des constituants phacnoliques de la “peau” des pommes et des poires pendant la croissance et sacnescence, Bull. Soc. Fr. Physiol. Veg
    • Hulme, A.C. Transformations des constituants phacnoliques de la “peau” des pommes et des poires pendant la croissance et sacnescence, Bull. Soc. Fr. Physiol. Veg. 4, 43, 1958.
    • (1958) , vol.4 , Issue.43
    • Hulme, A.C.1
  • 291
    • 1842300960 scopus 로고
    • Detection and identification of polyphenol oxidase substrates in apple and pear skin, Arch. Biochem. Biophys
    • Siegelmann, H.W. Detection and identification of polyphenol oxidase substrates in apple and pear skin, Arch. Biochem. Biophys. 56, 97, 1955.
    • (1955) , vol.56 , Issue.97
    • Siegelmann, H.W.1
  • 292
    • 84952432347 scopus 로고
    • Rale de divers facteurs intervenant dans le brunissement enzymatique des pommes pendant la croissance, Physiol. Veg
    • Macheix, J.J. Rale de divers facteurs intervenant dans le brunissement enzymatique des pommes pendant la croissance, Physiol. Veg. 8, 585, 1970.
    • (1970) , vol.8 , Issue.585
    • Macheix, J.J.1
  • 293
    • 84952432348 scopus 로고
    • von Untersuchungen bezaglich der Neigung einiger Apfelsorten zur enzymatischen Braunung, Confructa
    • St. I. Ergebnisse
    • Jankov, St. I. Ergebnisse von Untersuchungen bezaglich der Neigung einiger Apfelsorten zur enzymatischen Braunung, Confructa. 19, 29, 1974.
    • (1974) Jankov , vol.19 , Issue.29
  • 294
    • 84952432349 scopus 로고
    • and Gajzaigo, I. Messung der enzymatischen Braunung von Obst mit dem Spektralkolorimeter “Spekol”. Nahrung
    • Vamos, L. and Gajzaigo, I. Messung der enzymatischen Braunung von Obst mit dem Spektralkolorimeter “Spekol”. Nahrung, 18, 76, 1974.
    • (1974) , vol.18 , Issue.76
    • Vamos, L.1
  • 297
    • 0017389338 scopus 로고
    • Changes in polyphenols during storage of fruits and vegetables, Prikl. Biokhim. Mikrobiol
    • V.S. and
    • Kolesnik, A.A. Elizarova, L.G. Starodubtseva, T.V. Afanasyeva, V.S. and Erokhina, T.S. Changes in polyphenols during storage of fruits and vegetables, Prikl. Biokhim. Mikrobiol. 13, 333, 1977.
    • (1977) , vol.13 , Issue.333
    • Kolesnik, A.A.1    Elizarova, L.G.2    Afanasyeva, T.V.3    Erokhina, T.S.4
  • 298
    • 84952432352 scopus 로고
    • Formation des arames a diffacrents stades de l'acvolution du fruit: enzymes intervenant dans cette formation, Colloq. Int. C.N.R.S
    • Drawert, F. Formation des arames a diffacrents stades de l'acvolution du fruit: enzymes intervenant dans cette formation, Colloq. Int. C.N.R.S. 258, 309, 1975.
    • (1975) , vol.258 , Issue.309
    • Drawert, F.1
  • 299
    • 84952432353 scopus 로고
    • Anon. Biochemical changes with fruits stored at room and low temperature with reference to polyphenolic changes
    • Annu. Rep. Cent. Food Technol. Res. Inst. Mysore, 55.
    • Anon. Biochemical changes with fruits stored at room and low temperature with reference to polyphenolic changes, Annu. Rep. Cent. Food Technol. Res. Inst. Mysore, 1974, 55.
    • (1974)
  • 300
    • 84952432354 scopus 로고
    • Über die elektrophoretische Differenzierung und Klassifizierung von Proteinen. VII. Disk-EIektrophorese und isoelektrische Fokussierung in Polyacrylamid-Gelen von Proteinen und Enzymen aus a.pfeln. Einfluss von Dangungsmassnahmen, Lebensm. Wiss. Technol
    • Drawert, F. GArg, A. and Matzner, F. Über die elektrophoretische Differenzierung und Klassifizierung von Proteinen. VII. Disk-EIektrophorese und isoelektrische Fokussierung in Polyacrylamid-Gelen von Proteinen und Enzymen aus a.pfeln. Einfluss von Dangungsmassnahmen, Lebensm. Wiss. Technol. 9, 345, 1976.
    • (1976) , vol.9 , Issue.345
    • Drawert, F.1    Matzner, F.2
  • 301
    • 84952432355 scopus 로고
    • Changes in enzymic browning, polyphenol oxidase and polyphenol contents of Jonathan apples during storage, Acta Aliment. Acad.
    • K. and Sei. Hung. 6, 389
    • Vaimos-Vigyaiza, L. Gajzaiga, I. Mihailyi, K. and Naidudvari-Mairkus, V. Changes in enzymic browning, polyphenol oxidase and polyphenol contents of Jonathan apples during storage, Acta Aliment. Acad. Sei. Hung. 6, 389, 1977.
    • (1977)
    • Vaimos-Vigyaiza, L.1    Mihailyi, I.2    Naidudvari-Mairkus, V.3
  • 302
    • 84952432356 scopus 로고
    • and Bunemann, G. Der Tafelapfel als Rohware far die Verarbeitungsindustrie. II. aoeber den Einfluss des Reifezustandes auf die Qualitat von Verarbeitungsprodukten, Erwerbsobstbau
    • Schenker, D. and Bunemann, G. Der Tafelapfel als Rohware far die Verarbeitungsindustrie. II. aoeber den Einfluss des Reifezustandes auf die Qualitat von Verarbeitungsprodukten, Erwerbsobstbau, 16, 44, 1974.
    • (1974) , vol.16 , Issue.44
    • Schenker, D.1
  • 303
    • 84952432357 scopus 로고
    • Changes in the activity of oxidizing-reducing enzymes in apples during storage, Khranit. Promsl
    • Kolev, D. Changes in the activity of oxidizing-reducing enzymes in apples during storage, Khranit. Promsl. 5, 33, 1977.
    • (1977) , vol.5 , Issue.33
    • Kolev, D.1
  • 304
    • 84952432358 scopus 로고
    • Quality tests of apple cultivars, Meld. Nor.
    • Landbrukshoegs. 56(9), 1
    • Redalen, G. Quality tests of apple cultivars, Meld. Nor. Landbrukshoegs. 56(9), 1, 1977.
    • (1977)
    • Redalen, G.1
  • 305
    • 84952432359 scopus 로고
    • Seltener gezachtete Apfelsorten far die Saftproduktion und der Einfluss von Polyphenolen und zugefagter Ascorbinsaure auf die Saftqualitat, Fluess. Obst
    • Kuusi, T. and Pajunen, E. Seltener gezachtete Apfelsorten far die Saftproduktion und der Einfluss von Polyphenolen und zugefagter Ascorbinsaure auf die Saftqualitat, Fluess. Obst, 5, 208, 1972.
    • (1972) , vol.5 , Issue.208
    • Kuusi, T.1    Pajunen, E.2
  • 306
    • 84952432360 scopus 로고
    • Phenolic materials in Golden Delicious apple juice Abstracts of Papers, Am. Chem. Soc. 166, AGFD
    • Buren, J. van, Vos L. de, and Pilnik, W. Phenolic materials in Golden Delicious apple juice, Abstracts of Papers, Am. Chem. Soc. 166, AGFD 75, 1973.
    • (1973)
    • Buren, J.1    van, V.L.2    Pilnik, W.3
  • 307
    • 84952432361 scopus 로고
    • and Darr, P. Oxydationserscheinungen bei der Enzymatisierung von Apfelmaische, Fluess. Obst
    • Schobinger, U. and Darr, P. Oxydationserscheinungen bei der Enzymatisierung von Apfelmaische, Fluess. Obst. 41, 454, 1974.
    • (1974) , vol.41 , Issue.454
    • Schobinger, U.1
  • 308
    • 84985182664 scopus 로고
    • Changes in polyphenolics on ripening of selected pear varieties, J. Sei. Food Agrie
    • Ranadive, A.S. and Haard, N.F. Changes in polyphenolics on ripening of selected pear varieties, J. Sei. Food Agrie. 22, 86, 1971.
    • (1971) , vol.22 , Issue.86
    • Ranadive, A.S.1    Haard, N.F.2
  • 309
    • 84952411825 scopus 로고
    • Chlorogenic acid levels, ethylene production and respiration of d'Anjou pears affected with cork spot, Hortic. Sei
    • Wang, C.Y. and Mellenthin, W.M. Chlorogenic acid levels, ethylene production and respiration of d'Anjou pears affected with cork spot, Hortic. Sei. 8, 180, 1973.
    • (1973) , vol.8 , Issue.180
    • Wang, C.Y.1    Mellenthin, W.M.2
  • 310
    • 84952432362 scopus 로고
    • Review of the international literature on diphenol oxidases of peach fruits, Confructa
    • Vaimos-Vigyaiza, L. Mihailyi, K. and Schaller, A. Review of the international literature on diphenol oxidases of peach fruits, Confructa. 21, 234, 1976.
    • (1976) , vol.21 , Issue.234
    • Vaimos-Vigyaiza, L.1    Mihailyi, K.2    Schaller, A.3
  • 311
    • 0040642182 scopus 로고
    • entre la teneur en o-diphacnols, l'activitac polyphacnoloxydasique et l'aptitude au brunissement de quelques variactacs de paaches, Lebensm. Wiss. Technol
    • Bureau, D. Macheix, J.-J. and Rouet-Mayer, M.A. Relations entre la teneur en o-diphacnols, l'activitac polyphacnoloxydasique et l'aptitude au brunissement de quelques variactacs de paaches, Lebensm. Wiss. Technol. 10, 211, 1977.
    • (1977) , vol.10 , Issue.211
    • Bureau, D.1    Macheix, J.-J.2    Relations, M.A.3
  • 312
    • 84952432364 scopus 로고
    • St. Enzymatic browning of stone fruits
    • Nauchni Tr. Vissh. Inst. Khranit. Vkusova Promst. 18, 249
    • Dang F. and Yankov, St. Enzymatic browning of stone fruits, Nauchni Tr. Vissh. Inst. Khranit. Vkusova Promst. 18, 249, 1971.
    • (1971)
    • Dang, F.1
  • 313
    • 84952432365 scopus 로고
    • Mihailyi, K. and Vaimos-Vigyaiza, L. Ergebnisse von Untersuchungen hinsichtlich der massebezogenen Diphenoloxidaseaktivitat im Mesocarp verschiedener gelbfleischiger Pfirsichsorten, Confructa
    • Schaller, A. Mihailyi, K. and Vaimos-Vigyaiza, L. Ergebnisse von Untersuchungen hinsichtlich der massebezogenen Diphenoloxidaseaktivitat im Mesocarp verschiedener gelbfleischiger Pfirsichsorten, Confructa. 23, 1, 1978.
    • (1978) , vol.23 , Issue.1
    • Schaller, A.1
  • 314
    • 84986804669 scopus 로고
    • Changes in the levels of catechol oxidase and laccase activity in developing peaches, J. Sei. Food Agrie
    • Harel, E. Mayer, A.M. and Lerner, H.R. Changes in the levels of catechol oxidase and laccase activity in developing peaches, J. Sei. Food Agrie. 21, 542, 1970.
    • (1970) , vol.21 , Issue.542
    • Harel, E.1    Mayer, A.M.2    Lerner, H.R.3
  • 315
    • 84952432366 scopus 로고
    • Brown discoloration in canned peaches in relation to polyphenol oxidase activity and anthocyanin, Confructa
    • Chung, J.I. and Luh, B.S. Brown discoloration in canned peaches in relation to polyphenol oxidase activity and anthocyanin, Confructa, 17, 8, 1972.
    • (1972) , vol.17 , Issue.8
    • Chung, J.I.1    Luh, B.S.2
  • 316
    • 84952432367 scopus 로고
    • Influence of location and year of harvest on enzymic browning and the polyphenol oxidase-polyphenol complex of apricot cultivars, Proc. 19th Hung.
    • L. and Annu. Meet. Biochem. 221.
    • Gajzaigo, I. Naidudvari-Mairkus, V. Vaimos-Vigyaiza, L. and Babos-Szebenyi, A. Influence of location and year of harvest on enzymic browning and the polyphenol oxidase-polyphenol complex of apricot cultivars, Proc. 19th Hung. Annu. Meet. Biochem. 1979, 221.
    • (1979) Naidudvari-Mairkus
    • Gajzaigo, I.1    Vaimos-Vigyaiza, V.2    Babos-Szebenyi, A.3
  • 317
    • 84952432368 scopus 로고
    • Sour cherries and apricots as raw materials of nectars Konservn. Ovoshchesush. Promst
    • Yu. G. Kharchenkova
    • Skorikova, Yu. G. Kharchenkova, O.V. and Bonenko, Zh. N. Sour cherries and apricots as raw materials of nectars, Konservn. Ovoshchesush. Promst. 10, 21, 1974.
    • (1974) Skorikova , vol.10 , Issue.21
    • Bonenko, O.V.1    Zh, N.2
  • 318
    • 84952432354 scopus 로고
    • aoeber die elektrophoretische Differenzierung und Klassifizierung von Proteinen. VIII. Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamid-gelen von Proteinen und Enzymen aus Sauerkirschen. Einfluss von Schmitt- und Dangungsmassnahmen, Lebensm. Wiss. Technol
    • Drawert, F. GArg, A. and Matzner, F. aoeber die elektrophoretische Differenzierung und Klassifizierung von Proteinen. VIII. Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamid-gelen von Proteinen und Enzymen aus Sauerkirschen. Einfluss von Schmitt- und Dangungsmassnahmen, Lebensm. Wiss. Technol. 9, 353, 1976.
    • (1976) , vol.9 , Issue.353
    • Drawert, F.1    Matzner, F.2
  • 319
    • 84952382557 scopus 로고
    • Ricerche sulla prolifenolossidasi delle uve. 1. Distribuzione ed evoluzione dell'attivita enzimatica del frutto di diverse cultivars, Ind. Agrar
    • Montedoro, G. Ricerche sulla prolifenolossidasi delle uve. 1. Distribuzione ed evoluzione dell'attivita enzimatica del frutto di diverse cultivars, Ind. Agrar. 7, 197, 1969.
    • (1969) , vol.7 , Issue.197
    • Montedoro, G.1
  • 320
    • 0008739693 scopus 로고
    • and GArg, A. aoeber die eJektrophoretische Differenzierung und Klassifizierung von Proteinen. III. Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamidgelen von Proteinen and Enzymen aus Trauben verschiedener Rebsorten, Z. Lebensm. Unters. Forsch
    • Drawert, F. and GArg, A. aoeber die eJektrophoretische Differenzierung und Klassifizierung von Proteinen. III. Disk-Elektrophorese und isoelektrische Fokussierung in Polyacrylamidgelen von Proteinen and Enzymen aus Trauben verschiedener Rebsorten, Z. Lebensm. Unters. Forsch. 154, 328, 1974.
    • (1974) , vol.154 , Issue.328
    • Drawert, F.1
  • 321
    • 0016226111 scopus 로고
    • Über die elektrophoretische Differenzierung und Klassifizierung von Proteinen. IV. Disk-Elektrophorese und isoelektrische Fokussierung in Poly-Acrylamidgelen von Proteinen und Enzymen aus verschiedenen Erdbeerarten, -Sorten und Artkreuzungsversuchen, Z. Lebensm. Unters. Forsch
    • Drawert, F. GArg, A. and Staudt, G. Über die elektrophoretische Differenzierung und Klassifizierung von Proteinen. IV. Disk-Elektrophorese und isoelektrische Fokussierung in Poly-Acrylamidgelen von Proteinen und Enzymen aus verschiedenen Erdbeerarten, -Sorten und Artkreuzungsversuchen, Z. Lebensm. Unters. Forsch. 156, 129, 1974.
    • (1974) , vol.156 , Issue.129
    • Drawert, F.1    Staudt, G.2
  • 322
    • 84987305201 scopus 로고
    • Enzymatic browning of ripening bananas, J. Food Sei
    • Weaver, C. and Charley, M. Enzymatic browning of ripening bananas, J. Food Sei. 39, 1200, 1974.
    • (1974) , vol.39
    • Weaver, C.1    Charley, M.2
  • 323
    • 84952432372 scopus 로고
    • Polyphenols in the aqueous acetone extracts of the peel of ripening fruits, Plant Biochem. J
    • Venkajar, B. and Babu, C.K. Polyphenols in the aqueous acetone extracts of the peel of ripening fruits, Plant Biochem. J. 4, 39, 1977.
    • (1977) , vol.4 , Issue.39
    • Venkajar, B.1    Babu, C.K.2
  • 324
    • 0006924054 scopus 로고
    • of different storage temperatures on phenolic compounds in banana and mango fruits, Sei. Hortic
    • Abou Aziz, A.B. Abdel-Wahab, F.K. and El-Ghandour, M.A. Effect of different storage temperatures on phenolic compounds in banana and mango fruits, Sei. Hortic. 4, 309, 1976.
    • (1976) Abdel-Wahab , vol.4 , Issue.309
    • Abou, A.B.1    El-Ghandour, F.K.2    Effect, M.A.3
  • 325
    • 0004639388 scopus 로고
    • Effect of gamma irradiation on polyphenol oxidase activity and its relation to skin browning in bananas, Phytochemistry
    • Thomas, P. and Nair, P.M. Effect of gamma irradiation on polyphenol oxidase activity and its relation to skin browning in bananas, Phytochemistry, 10, 771, 1971.
    • (1971) , vol.10 , Issue.771
    • Thomas, P.1    Nair, P.M.2
  • 327
    • 77951506319 scopus 로고
    • Potato composition: III. Tissue selection and its effects on total nitrogen, free amino acid nitrogen and enzyme activity polyphenolase, monophenolase, peroxidase and catalase, Am. Potato J
    • K.C. and
    • Weaver, M.L. Timm, H. Nonaka, M. Sayre, R.N. Ng, K.C. and Whitehand, L.C. Potato composition: III. Tissue selection and its effects on total nitrogen, free amino acid nitrogen and enzyme activity (polyphenolase, monophenolase, peroxidase and catalase), Am. Potato J. 55, 319, 1978.
    • (1978) , vol.55 , Issue.319
    • Weaver, M.L.1    Timm, H.2    Sayre, M.3    Ng, R.N.4    Whitehand, L.C.5
  • 328
    • 84952432375 scopus 로고
    • Vorlaufige Mitteilungen aber den Einfluss von Sorte, Anbauort und Kulturmassnahmen sowie Lagerung auf Kartoffeln far Speisezwecke und zur Veredelung, Kartoffelbau
    • Chr. and
    • Heilinger, F. Patzold, Chr. and Radatz, W. Vorlaufige Mitteilungen aber den Einfluss von Sorte, Anbauort und Kulturmassnahmen sowie Lagerung auf Kartoffeln far Speisezwecke und zur Veredelung, Kartoffelbau, 6, 144, 1963.
    • (1963) Patzold , vol.6 , Issue.144
    • Heilinger, F.1    Radatz, W.2
  • 329
    • 51849175519 scopus 로고
    • Studies on phenolase and internal discoloration blackspot in Russet Burbank potatoes, Am. Potato J
    • Weaver, M.L. and Hautala, E. Studies on phenolase and internal discoloration (blackspot) in Russet Burbank potatoes, Am. Potato J. 46, 259, 1969.
    • (1969) , vol.46 , Issue.259
    • Weaver, M.L.1    Hautala, E.2
  • 330
    • 0016391450 scopus 로고
    • Einfluss von Sorte and Standort auf die an der enzymatischen Verfarbung beteiligten Inhaltsstoffe der Kartoffel, Z. Lebensm. Unters. Forsch
    • Amberger, A. and Schaller, K. Einfluss von Sorte and Standort auf die an der enzymatischen Verfarbung beteiligten Inhaltsstoffe der Kartoffel, Z. Lebensm. Unters. Forsch. 156, 231, 1974.
    • (1974) , vol.156 , Issue.231
    • Amberger, A.1    Schaller, K.2
  • 331
    • 0016391450 scopus 로고
    • Einfluss von Sorte und Lagertemperatur auf die an der enzymatischen Verfarbung der Kartoffelknolle beteiligton Inhaltsstoffe, Z. Lebensm. Unters. Forsch
    • Amberger, A. and Schaller, K. Einfluss von Sorte und Lagertemperatur auf die an der enzymatischen Verfarbung der Kartoffelknolle beteiligton Inhaltsstoffe, Z. Lebensm. Unters. Forsch. 156, 231, 1974.
    • (1974) , vol.156 , Issue.231
    • Amberger, A.1    Schaller, K.2
  • 332
    • 33947415868 scopus 로고
    • Zusammenhange zwischen den far die Blaufleckigkeit der Kartoffelknolle verantwortlichen Inhaltsstoffen, Qual. Plant. Plant Foods Hum. Nutr
    • Schaller, K. and Amberger, A. Zusammenhange zwischen den far die Blaufleckigkeit der Kartoffelknolle verantwortlichen Inhaltsstoffen, Qual. Plant. Plant Foods Hum. Nutr. 24, 191, 1974.
    • (1974) , vol.24 , Issue.191
    • Schaller, K.1    Amberger, A.2
  • 333
    • 0001577116 scopus 로고
    • Zusammenhange zwischen den far die Roh Verfarbung der Kartoffelknolle verantwortlichen Inhaltsstoffen, Qual. Plant. Plant Foods Hum. Nutr
    • Schaller, K. and Amberger, A. Zusammenhange zwischen den far die Roh Verfarbung der Kartoffelknolle verantwortlichen Inhaltsstoffen, Qual. Plant. Plant Foods Hum. Nutr. 24, 183, 1974.
    • (1974) , vol.24 , Issue.183
    • Schaller, K.1    Amberger, A.2
  • 334
    • 0017780423 scopus 로고
    • Lebensm. Unters.
    • Quantitative Beziehungen zwischen Braunung und Forsch. 163, 186
    • Matheis, G. and Belitz, H.-D. Untersuchungen zur enzymatischen Braunung bei Kartoffeln (Solanum tuberosum). II. Quantitative Beziehungen zwischen Braunung und Inhaltsstoffen, Z. Lebensm. Unters. Forsch. 163, 186, 1977.
    • (1977)
    • Matheis, G.1    Belitz, H.-D.2    Inhaltsstoffen, Z.3
  • 335
    • 84982072864 scopus 로고
    • Influence of variety, cultural conditions and temperature of storage on enzymic browning of potato tubers, J. Sei. Food Agrie
    • Mapson, L.W. Swain, T. and Tomalin, A.W. Influence of variety, cultural conditions and temperature of storage on enzymic browning of potato tubers, J. Sei. Food Agrie. 14, 673, 1963.
    • (1963) , vol.14 , Issue.673
    • Mapson, L.W.1    Swain, T.2    Tomalin, A.W.3
  • 336
    • 84986804785 scopus 로고
    • Changes in some nitrogenous constituents of potato tubers during aerobic autolysis, J. Sei. Food Agrie
    • Davie, A.M.C. and Laird, W.M. Changes in some nitrogenous constituents of potato tubers during aerobic autolysis, J. Sei. Food Agrie. 27, 377, 1976.
    • (1976) , vol.27 , Issue.377
    • Davie, A.M.C.1    Laird, W.M.2
  • 337
    • 0018279742 scopus 로고
    • Lebensm. Unters.
    • Relationship between tyrosine turnover and rate of Forsch. 167, 97
    • Matheis, G. and Belitz, H.-D. Studies on enzymic browning of potatoes (Solanum tuberosum). IV. Relationship between tyrosine turnover and rate of browning, Z. Lebensm. Unters. Forsch. 167, 97, 1978.
    • (1978)
    • Matheis, G.1    Belitz, H.-D.2
  • 338
    • 84982334577 scopus 로고
    • The effect of maturity and storage on phenolic content, enzymatic activity and discoloration of potatoes, Food Res
    • Mondy, N.I. Klein, B.P. and Smith, L.I. The effect of maturity and storage on phenolic content, enzymatic activity and discoloration of potatoes, Food Res. 25, 693, 1960.
    • (1960) , vol.25 , Issue.693
    • Mondy, N.I.1    Klein, B.P.2    Smith, L.I.3
  • 339
    • 34250415532 scopus 로고
    • Influence of potassium supply and storage conditions on the discoloration of raw and cooked potato tubers of cv. Pimpernel, Potato Res
    • Baerug, R. and Enge, R. Influence of potassium supply and storage conditions on the discoloration of raw and cooked potato tubers of cv. Pimpernel, Potato Res. 17, 271, 1974.
    • (1974) , vol.17 , Issue.271
    • Baerug, R.1    Enge, R.2
  • 340
    • 17044430055 scopus 로고
    • Enzymic browning and free tyrosine in potatoes as affected by pentachloronitrobenzene, J. Agrie. Food Chem
    • Sweeney, J.P. and Simandle, P.A. Enzymic browning and free tyrosine in potatoes as affected by pentachloronitrobenzene, J. Agrie. Food Chem. 16, 25, 1968.
    • (1968) , vol.16 , Issue.25
    • Sweeney, J.P.1    Simandle, P.A.2
  • 341
    • 84987368176 scopus 로고
    • Effect of sprout inhibition on the lipid composition of potatoes, J. Food Sei
    • Mueller, T.O. and Mondy, N.I. Effect of sprout inhibition on the lipid composition of potatoes, J. Food Sei. 42, 618, 1977.
    • (1977) , vol.42 , Issue.618
    • Mueller, T.O.1    Mondy, N.I.2
  • 342
    • 84952414934 scopus 로고
    • Studies on the browning of potato tubers by gamma radiation. IV. Food Irradial
    • Tatsumi, Y. Chachin, K. and Ogata, K. Studies on the browning of potato tubers by gamma radiation. IV. Food Irradial. 9, 74, 1974.
    • (1974) , vol.9 , Issue.74
    • Tatsumi, Y.1    Chachin, K.2    Ogata, K.3
  • 343
    • 0347212022 scopus 로고
    • of physiological stress on potato polyphenol oridase
    • Phytochemistry 11, 1255
    • Cheung, K.W. -K. and Henderson, H.M. Effect of physiological stress on potato polyphenol oridase, Phytochemistry 11, 1255, 1972.
    • (1972)
    • Cheung, K.1    Henderson, W.-K.2    Effect, H.M.3
  • 344
    • 84952398569 scopus 로고
    • Tissue browning of potato tubers induced by gamma irradiation, Agrie. Biol. Chem
    • Ogawa, M. and Uritani, I. Tissue browning of potato tubers induced by gamma irradiation, Agrie. Biol. Chem. 34, 870, 1970.
    • (1970) , vol.34 , Issue.870
    • Ogawa, M.1    Uritani, I.2
  • 345
    • 84952432381 scopus 로고
    • Radioinhibition de la germination des pommes de terre. Polyphenols, activitac polyphacnoloxydasique, noircissement a la cuisson. Effets comparacs des radiations β et y, Lebensm. Wiss. Technol
    • Berset, C. and Sandret, F. Radioinhibition de la germination des pommes de terre. Polyphenols, activitac polyphacnoloxydasique, noircissement a la cuisson. Effets comparacs des radiations β et y, Lebensm. Wiss. Technol. 9, 85, 1976.
    • (1976) , vol.9 , Issue.85
    • Berset, C.1    Sandret, F.2
  • 346
    • 84952386187 scopus 로고
    • Studies on the browning of potatoes by gamma radition. III. Food Irradiat
    • Tatsumi, Y. Chachin, K. and Ogata, K. Studies on the browning of potatoes by gamma radition. III. Food Irradiat. 7, 82, 1972.
    • (1972) , vol.7 , Issue.82
    • Tatsumi, Y.1    Chachin, K.2    Ogata, K.3
  • 347
    • 0343551023 scopus 로고
    • Comparison of nutrient composition and of enzyme activity in purple, green and white eggplants, J. Agrie. Food Chem
    • Flick, G.J. Ory, R.L. and St. Angelo, A.J. Comparison of nutrient composition and of enzyme activity in purple, green and white eggplants, J. Agrie. Food Chem. 25, 117, 1977.
    • (1977) , vol.25 , Issue.117
    • Flick, G.J.1    Ory, R.L.2    Angelo, A.J.3
  • 348
    • 0016873233 scopus 로고
    • Protein and enzyme changes in tomato fruit in relation to blotchy ripening and potassium nutrition, J. Sei. Food Agrie
    • Hobson, G.E. and Davies, J.N. Protein and enzyme changes in tomato fruit in relation to blotchy ripening and potassium nutrition, J. Sei. Food Agrie. 27, 15, 1976.
    • (1976) , vol.27 , Issue.15
    • Hobson, G.E.1    Davies, J.N.2
  • 349
    • 0017388676 scopus 로고
    • Moinova, K. and Mal'tseva, S. Study on the effect of comparatively low doses of Co-60 γ-rays on the PPO activity in tomato seeds, Radiobiologiya
    • Daskalov, H. Moinova, K. and Mal'tseva, S. Study on the effect of comparatively low doses of Co-60 γ-rays on the PPO activity in tomato seeds, Radiobiologiya, 17, 589, 1977.
    • (1977) , vol.17 , Issue.589
    • Daskalov, H.1
  • 351
    • 11244269400 scopus 로고
    • The effect of maturity and environment on phenolic compounds and oxidative browning in carrots, J. Am. Soc. Hortic. Sei
    • Chubey, B.B. and Nylund, R.E. The effect of maturity and environment on phenolic compounds and oxidative browning in carrots, J. Am. Soc. Hortic. Sei. 95, 393, 1970.
    • (1970) , vol.95 , Issue.393
    • Chubey, B.B.1    Nylund, R.E.2
  • 352
    • 85005670799 scopus 로고
    • Is. Effect of γ-irradiation on quality and enzyme activities of prepacked cut chicory, J. Food Technol
    • Tanaka, Y. and Langerak, D. Is. Effect of γ-irradiation on quality and enzyme activities of prepacked cut chicory, J. Food Technol. 10, 415, 1975.
    • (1975) , vol.10 , Issue.415
    • Tanaka, Y.1    Langerak, D.2
  • 353
    • 84952432385 scopus 로고
    • Langerak, D. Is. and van Kooy, J. Effect of γ-irradiation on the activities of peroxidase and polyphenol oxidase in cut, prepacked leaves of endives Cichorium endivia, Nauchni Tr. Nauchnoizsled. Inst. Konservna Promst. Plovdiv
    • Kalinov, V. Langerak, D. Is. and van Kooy, J. Effect of γ-irradiation on the activities of peroxidase and polyphenol oxidase in cut, prepacked leaves of endives (Cichorium endivia), Nauchni Tr. Nauchnoizsled. Inst. Konservna Promst. Plovdiv, 10, 67, 1973.
    • (1973) , vol.10 , Issue.67
    • Kalinov, V.1
  • 354
    • 0001026906 scopus 로고
    • Effect of storage temperature on post-harvest changes in mushrooms, J. Am. Soc. Hortic. Sei
    • Murr, D.P. and Morris, L.L. Effect of storage temperature on post-harvest changes in mushrooms, J. Am. Soc. Hortic. Sei. 100, 16, 1975.
    • (1975) , vol.100 , Issue.16
    • Murr, D.P.1    Morris, L.L.2
  • 355
    • 0344367555 scopus 로고
    • Gamma-irradiation of mushrooms and its effect on active and latent forms of o-diphenol oxidase, Radiat. Bot
    • Yamaguchi, M. and Campbell, J.D. Gamma-irradiation of mushrooms and its effect on active and latent forms of o-diphenol oxidase, Radiat. Bot. 13, 55, 1973.
    • (1973) , vol.13 , Issue.55
    • Yamaguchi, M.1    Campbell, J.D.2
  • 356
    • 84952432386 scopus 로고
    • of enzymes and changes in the carbohydrate complex of edible mushrooms during the drying period, Izv. Vyssh.
    • Yu. T. and Tsapalova, Uchebn. Zaved. Pishch. Tekhnol. 3,60
    • Zhuk, Yu. T. and Tsapalova, I.E. Activity of enzymes and changes in the carbohydrate complex of edible mushrooms during the drying period, Izv. Vyssh. Uchebn. Zaved. Pishch. Tekhnol. 3,60,1974.
    • (1974) Zhuk
    • Activity, I.E.1
  • 357
    • 84952401072 scopus 로고
    • Academic Press
    • in The Enzymes, Boyer, H. and New York, chap.
    • Paul, K.G. Peroxidases, in The Enzymes, Vol. 8, Boyer, P.D. Lardy, H. and Myrback, K. Eds. Academic Press, New York, 1963, chap. 7.
    • (1963) Peroxidases , vol.8 , pp. 7
    • Paul, K.G.1    Lardy, P.D.2    Myrback, K.3
  • 358
    • 84952404307 scopus 로고
    • Oxidoreductases, in Enzymes in Food Processing, 2nd ed. Reed, G.
    • Ed. Academic Press, New York, chap.
    • Scott, D. Oxidoreductases, in Enzymes in Food Processing, 2nd ed. Reed, G. Ed. Academic Press, New York, 1975, chap. 9.
    • (1975) , pp. 9
    • Scott, D.1
  • 359
    • 84952432387 scopus 로고
    • Cytochemical localization of peroxidase A' in developing stem tissues of extreme dwarf tomato, Can. J.
    • Bot. 49, 1487
    • Gordon, A.R. and Alldridge, A. Cytochemical localization of peroxidase A' in developing stem tissues of extreme dwarf tomato, Can. J. Bot. 49, 1487, 1971.
    • (1971)
    • Gordon, A.R.1    Alldridge, A.2
  • 360
    • 84987367649 scopus 로고
    • Chilling injury in green banana fruit: changes in peroxidase isozymes in soluble and particulate pools, J. Food Sei
    • Haard, N.F. and Timbie, D. Chilling injury in green banana fruit: changes in peroxidase isozymes in soluble and particulate pools, J. Food Sei. 38, 642, 1973.
    • (1973) , vol.38 , Issue.642
    • Haard, N.F.1    Timbie, D.2
  • 361
    • 84985053077 scopus 로고
    • Patterns of soluble peroxidase in ripening banana fruit, J. Food Sei
    • Haard, N.F. and Tobin, C.L. Patterns of soluble peroxidase in ripening banana fruit, J. Food Sei. 36, 854, 1971.
    • (1971) , vol.36 , Issue.854
    • Haard, N.F.1    Tobin, C.L.2
  • 362
    • 84952432388 scopus 로고
    • Properties and subcellular distribution of peroxidases in onion stem, Proc. Indiana Acad. Sei
    • Twohig, F. Morre, D.J. and Vigil, E.L. Properties and subcellular distribution of peroxidases in onion stem, Proc. Indiana Acad. Sei. 83, 86, 1973.
    • (1973) , vol.83 , Issue.86
    • Twohig, F.1    Morre, D.J.2    Vigil, E.L.3
  • 363
    • 0000529091 scopus 로고
    • Hydroxyproline and peroxidases in cell walls of Pisum sativum: regulation by ethylene, J. Exp. Bot
    • Ridge, I. and Osborne, D.J. Hydroxyproline and peroxidases in cell walls of Pisum sativum: regulation by ethylene, J. Exp. Bot. 21, 843, 1970.
    • (1970) , vol.21 , Issue.843
    • Ridge, I.1    Osborne, D.J.2
  • 364
    • 0039394229 scopus 로고
    • Upsurge of particulate peroxidasein ripening banana fruit, Phytochemistry
    • Haard, N.F. Upsurge of particulate peroxidasein ripening banana fruit, Phytochemistry, 12, 555, 1973.
    • (1973) , vol.12 , Issue.555
    • Haard, N.F.1
  • 365
    • 0005865282 scopus 로고
    • Isoperoxidase changes in soluble and particulate fractions of sweet potato root resulting from cut injury, ethylene and black rot infection, Physiol. Plant Pathol
    • Haard, N.F. and Marshall, M. Isoperoxidase changes in soluble and particulate fractions of sweet potato root resulting from cut injury, ethylene and black rot infection, Physiol. Plant Pathol. 8, 195, 1976.
    • (1976) , vol.8 , Issue.195
    • Haard, N.F.1    Marshall, M.2
  • 366
    • 84952401319 scopus 로고
    • An accounting of horseradish peroxidase isozymes associated with the cell wall and evidence that peroxidase does not contain hydroxyproline, Plant Physiol
    • Liu, E.H. and Lamport, D.T.A. An accounting of horseradish peroxidase isozymes associated with the cell wall and evidence that peroxidase does not contain hydroxyproline, Plant Physiol. 54, 870, 1974.
    • (1974) , vol.54 , Issue.870
    • Liu, E.H.1    Lamport, D.T.A.2
  • 367
    • 84985043532 scopus 로고
    • Changes in soluble and bound peroxidases during low-temperature storage of green beans, J. Food Sei
    • Gkinis, H. and Fennema, O.R. Changes in soluble and bound peroxidases during low-temperature storage of green beans, J. Food Sei. 43, 527, 1978.
    • (1978) , vol.43 , Issue.527
    • Gkinis, H.1    Fennema, O.R.2
  • 368
    • 0016654474 scopus 로고
    • On the localization of catalase and peroxidase in isolated chloroplasts of green peas and their fragments, Biokhimiya
    • Murzaeva, S.V. and Akulova, E.A. On the localization of catalase and peroxidase in isolated chloroplasts of green peas and their fragments, Biokhimiya, 40, 166, 1975.
    • (1975) , vol.40 , Issue.166
    • Murzaeva, S.V.1    Akulova, E.A.2
  • 369
    • 84987313877 scopus 로고
    • Peroxidase localization and lignin formation in developing pear fruit, J. Food Sei
    • Ranadive, A.S. and Haard, N.F. Peroxidase localization and lignin formation in developing pear fruit, J. Food Sei. 37, 381, 1972.
    • (1972) , vol.37 , Issue.381
    • Ranadive, A.S.1    Haard, N.F.2
  • 370
    • 49649154776 scopus 로고
    • Peroxidase isoenzymes in leaves of cucumber Cucumis sativus L. cultivars systemically infected with the W strain of cucumber mosaic virus, Physiol. Plant Pathol
    • Wood, K.R. Peroxidase isoenzymes in leaves of cucumber (Cucumis sativus L.) cultivars systemically infected with the W strain of cucumber mosaic virus, Physiol. Plant Pathol. 1, 133, 1971.
    • (1971) , vol.1 , Issue.133
    • Wood, K.R.1
  • 371
    • 0018449166 scopus 로고
    • Activity, isoenzyme composition, thermostability and molecular weight of peroxidase from intact and virus infected tobacco plant leaves, Biokhimiya
    • Andreeva, V.A. Voronova, V.A. and Ugarova, N.N. Activity, isoenzyme composition, thermostability and molecular weight of peroxidase from intact and virus infected tobacco plant leaves, Biokhimiya, 44, 394, 1979.
    • (1979) , vol.44 , Issue.394
    • Andreeva, V.A.1    Voronova, V.A.2    Ugarova, N.N.3
  • 372
    • 84952432390 scopus 로고
    • Plant isoenzymes, Annu. Rev. Plant Physiol
    • Shannon, L.M. Plant isoenzymes, Annu. Rev. Plant Physiol. 19, 187, 1968.
    • (1968) , vol.19 , Issue.187
    • Shannon, L.M.1
  • 373
    • 84952399821 scopus 로고
    • Physiological role of peroxidase in postharvest fruits and vegetables
    • in Enzymes in Food and Beverage Processing, Ory, R.L. and St. Angelo, ACS Symposium Series 47, American Chemical Society, chap.
    • Haard, N.F. Physiological role of peroxidase in postharvest fruits and vegetables, in Enzymes in Food and Beverage Processing, Ory, R.L. and St. Angelo, A.J. St. Eds. ACS Symposium Series 47, American Chemical Society, Washington, D.C. 1977, chap. 9.
    • (1977) , pp. 9
    • Haard, N.F.1    St, A.J.2    Washington, D.C.3
  • 374
    • 84987311756 scopus 로고
    • Wolfe, R. and Frenkel, Ch. Ethylene induced isoperoxidase changes during fiber formation in postharvest asparagus, J. Food Sei
    • Haard, N.F. Sharma, S.C. Wolfe, R. and Frenkel, Ch. Ethylene induced isoperoxidase changes during fiber formation in postharvest asparagus, J. Food Sei. 39, 452, 1974.
    • (1974) , vol.39 , Issue.452
    • Haard, N.F.1    Sharma, S.C.2
  • 375
    • 0004794990 scopus 로고
    • Activity of enzymes involved in lignin biosynthesis in swede root disks, Phytochemistry
    • Rhodes, M.J.C. Hill, A.C.R. and Wooltorton, L.S.C. Activity of enzymes involved in lignin biosynthesis in swede root disks, Phytochemistry, 15, 707, 1976.
    • (1976) , vol.15 , Issue.707
    • Rhodes, M.J.C.1    Hill, A.C.R.2    Wooltorton, L.S.C.3
  • 376
    • 34250490087 scopus 로고
    • Pathways of ethylene biosynthesis, Qual. Plant. Mater. Veg
    • Yang, S.F. and Baur, A.H. Pathways of ethylene biosynthesis, Qual. Plant. Mater. Veg. 19, 201, 1969.
    • (1969) , vol.19 , Issue.201
    • Yang, S.F.1    Baur, A.H.2
  • 377
    • 84952432392 scopus 로고
    • Involvement of peroxidase and indoIe-3-acetic oxidase isozymes from pear, tomato and blueberry fruit in ripening, Plant Physiol
    • Ch.
    • Frenkel, Ch. Involvement of peroxidase and indoIe-3-acetic oxidase isozymes from pear, tomato and blueberry fruit in ripening, Plant Physiol. 49, 757, 1972.
    • (1972) Frenkel , vol.49 , Issue.757
  • 378
    • 0016295703 scopus 로고
    • Induction of peroxidase activity by ethylene and indole-3-acetic acid in tea shoots, Agrie. Biol. Chem
    • Saijo, R. and Takeo, T. Induction of peroxidase activity by ethylene and indole-3-acetic acid in tea shoots, Agrie. Biol. Chem. 38, 2283, 1974.
    • (1974) , vol.38
    • Saijo, R.1    Takeo, T.2
  • 379
    • 0014029991 scopus 로고
    • Hormone-induced repression of a peroxidase isozyme in plant tissue, Science
    • Ockerse, R. Siegel, N.Z. and Galston, A.W. Hormone-induced repression of a peroxidase isozyme in plant tissue, Science, 151, 452, 1966.
    • (1966) , vol.151 , Issue.452
    • Ockerse, R.1    Siegel, N.Z.2    Galston, A.W.3
  • 380
    • 0016874376 scopus 로고
    • Peroxidase activity in Golden Delicious apples as a possible parameter of senescence, J. Agrie. Food Chem
    • Gorin, N. and Heidema, F.T. Peroxidase activity in Golden Delicious apples as a possible parameter of senescence, J. Agrie. Food Chem. 24, 200, 1976.
    • (1976) , vol.24 , Issue.200
    • Gorin, N.1    Heidema, F.T.2
  • 381
    • 0017785535 scopus 로고
    • Isoenzyme patterns of peroxidase in Golden Delicious apples during the ripening and senescence stages, Z. Lebensm. Unters. Forsch
    • Bonisolli, F. and Gorin, N. Isoenzyme patterns of peroxidase in Golden Delicious apples during the ripening and senescence stages, Z. Lebensm. Unters. Forsch. 164, 177, 1977.
    • (1977) , vol.164 , Issue.177
    • Bonisolli, F.1    Gorin, N.2
  • 382
    • 34250427288 scopus 로고
    • Peroxidase as biochemical measure of fresh weight and sugar yield in sugar-beet, Experientia
    • Th. and
    • Gaspar, Th. and Bouchet, M. Peroxidase as biochemical measure of fresh weight and sugar yield in sugar-beet, Experientia, 29, 1212, 1973.
    • (1973) Gaspar , vol.29
    • Bouchet, M.1
  • 383
    • 84981867113 scopus 로고
    • Color determination in frozen French beans Phaseolus vulgaris. J. Food Sei
    • Walker, G.C. Color determination in frozen French beans (Phaseolus vulgaris). J. Food Sei. 29, 383, 1964.
    • (1964) , vol.29 , Issue.383
    • Walker, G.C.1
  • 384
    • 84987305340 scopus 로고
    • Carotene oxidizing factors in red pepper fruits Capsicum annuum L.: peroxidase activity, J. Food Sei
    • Kanner, J. Mendel, H. and Budowski, P. Carotene oxidizing factors in red pepper fruits (Capsicum annuum L.): peroxidase activity, J. Food Sei. 42, 1549, 1977.
    • (1977) , vol.42
    • Kanner, J.1    Mendel, H.2    Budowski, P.3
  • 385
    • 84952432394 scopus 로고
    • Changes induced in foods by tissue enzymes
    • Macrnöki Tovaibbkacpzo Intaczet, Budapest
    • Vas, K. Changes induced in foods by tissue enzymes, Macrnöki Tovaibbkacpzo Intaczet, Budapest, 1954.
    • (1954)
    • Vas, K.1
  • 386
    • 84985165999 scopus 로고
    • Peroxidase and its relationship to food flavor and quality: a review, J. Food Sei
    • Burnette, F.S. Peroxidase and its relationship to food flavor and quality: a review, J. Food Sei. 42, 1, 1977.
    • (1977) , vol.42 , Issue.1
    • Burnette, F.S.1
  • 387
    • 84982060346 scopus 로고
    • Enzyme action and off-flavor in frozen peas, Food Res
    • Wagenknecht, A.C. and Lee, F.A. Enzyme action and off-flavor in frozen peas, Food Res. 23, 25, 1958.
    • (1958) , vol.23 , Issue.25
    • Wagenknecht, A.C.1    Lee, F.A.2
  • 388
    • 84952418575 scopus 로고
    • Der Einfluss thermischer Behandlung von Spinat im Temperaturbereich bis 100A C auf den Gehalt an wesentlichen Inhaltsstoffen. IV. Peroxydase, Lebensm. Wiss. Technol
    • K. and
    • Duden, R. Fricker, A. Heintze, K. Paulus, K. and Zohm, H. Der Einfluss thermischer Behandlung von Spinat im Temperaturbereich bis 100A C auf den Gehalt an wesentlichen Inhaltsstoffen. IV. Peroxydase, Lebensm. Wiss. Technol. 8, 147, 1975.
    • (1975) , vol.8 , Issue.147
    • Duden, R.1    Fricker, A.2    Paulus, K.3    Zohm, H.4
  • 389
    • 0013853336 scopus 로고
    • Reaction of peroxidase with reduced nicotinamide-adenine dinucleotide and reduced nicotinamide-adenine dinucleotide phosphate, Biochim. Biophys. Acta
    • Yokota, K. and Yamazakl, I. Reaction of peroxidase with reduced nicotinamide-adenine dinucleotide and reduced nicotinamide-adenine dinucleotide phosphate, Biochim. Biophys. Acta. 105, 301, 1965.
    • (1965) , vol.105 , Issue.301
    • Yokota, K.1    Yamazakl, I.2
  • 390
    • 77049151680 scopus 로고
    • The oxidation of certain dicarboxylic acids by peroxidase systems in presence of manganese, Biochem. J
    • Kenten, R.H. and Mann, P.J.G. The oxidation of certain dicarboxylic acids by peroxidase systems in presence of manganese, Biochem. J. 53, 498, 1953.
    • (1953) , vol.53 , Issue.498
    • Kenten, R.H.1    Mann, P.J.G.2
  • 391
    • 0014216672 scopus 로고
    • Peroxidase isozymes from horseradish roots, J. Biol. Chem
    • Kay, E. Shannon, L.M. and Lew, J.Y. Peroxidase isozymes from horseradish roots, J. Biol. Chem. 242, 2470, 1967.
    • (1967) , vol.242
    • Kay, E.1    Shannon, L.M.2    Lew, J.Y.3
  • 392
    • 0001706613 scopus 로고
    • The oxidation of reduced pyridine nucleotides by peroxidase, J. Biol. Chem
    • Akazawa, T. and Conn, E.E. The oxidation of reduced pyridine nucleotides by peroxidase, J. Biol. Chem. 232, 403, 1958.
    • (1958) , vol.232 , Issue.403
    • Akazawa, T.1    Conn, E.E.2
  • 394
    • 0016681994 scopus 로고
    • Kinetics and mechanism of action of horseradish peroxidase in the oxidation reaction of dihydroxyfumaric acid with the oxygen of air, Biokhimiya
    • M.P. and
    • Berezin, I.V. Ugarova, N.N. Dmitrieva-Getling, M.P. and Kershengoltz, B.M. Kinetics and mechanism of action of horseradish peroxidase in the oxidation reaction of dihydroxyfumaric acid with the oxygen of air, Biokhimiya, 40, 475, 1975.
    • (1975) , vol.40 , Issue.475
    • Berezin, I.V.1    Ugarova, N.N.2    Kershengoltz, B.M.3
  • 395
    • 0014220785 scopus 로고
    • Indoleacetic acid oxidase activity of apoperoxidase, Science
    • Siegel, B.Z. and Galston, A.W. Indoleacetic acid oxidase activity of apoperoxidase, Science, 157, 1557, 1967.
    • (1967) , vol.157
    • Siegel, B.Z.1    Galston, A.W.2
  • 396
    • 0013966369 scopus 로고
    • Peroxidases of the Alaska pea Pisum sativum L., Arch. Biochem. Biophys
    • Macnicol, P.K. Peroxidases of the Alaska pea (Pisum sativum L.), Arch. Biochem. Biophys. 117, 347, 1966.
    • (1966) , vol.117 , Issue.347
    • Macnicol, P.K.1
  • 397
    • 84952432396 scopus 로고    scopus 로고
    • Ya. On the active site of the oxidatic function of peroxidase.
    • F.G. and
    • Ramazanova, L. Kh. Miftakhudinova, F.G. and Alexeeva, V. Ya. On the active site of the oxidatic function of peroxidase.
    • Miftakhudinova
    • Ramazanova, L.1    Alexeeva, V.2
  • 398
    • 0015493842 scopus 로고
    • potentials and ionization states of two turnip peroxidases, Eur. J.
    • Biochem. 28, 566
    • Ricard, J.; Mazza, G. and Williams, J.P. Oxidation-reduction potentials and ionization states of two turnip peroxidases, Eur. J. Biochem. 28, 566, 1972.
    • (1972)
    • Ricard, J.1    Mazza, G.2
  • 399
    • 0542443900 scopus 로고
    • Evolution de l'activitac auxines-oxydasique et peroxydasique lors de l'induction photopacriodique et de la sexualisation de l'acpinard, Plant Cell Physiol
    • CI. and
    • Penel, CI. and Greppin, H. Evolution de l'activitac auxines-oxydasique et peroxydasique lors de l'induction photopacriodique et de la sexualisation de l'acpinard, Plant Cell Physiol, 13, 151, 1972.
    • (1972) Penel , vol.13 , Issue.151
    • Greppin, H.1
  • 400
    • 0013916024 scopus 로고
    • The behavior of horseradish peroxidase at high hydrogen peroxide concentrations. Biochemistry
    • Weinryb, I. The behavior of horseradish peroxidase at high hydrogen peroxide concentrations. Biochemistry, 5, 2003, 1966.
    • (1966) , vol.5
    • Weinryb, I.1
  • 401
    • 84952432399 scopus 로고
    • Dactermination de la Peroxydase dans le raisin, Ann. Technol Agrie
    • 47
    • Poux, C. and Ournac, A. Dactermination de la Peroxydase dans le raisin, Ann. Technol Agrie. 21,47, 1972.
    • (1972) , vol.21
    • Poux, C.1    Ournac, A.2
  • 402
    • 0343114983 scopus 로고
    • Determination, localization and heat inactivation of peroxidase in some vegetables, Acta Aliment. Acad. Sei. Hung
    • Mihailyi, K. and Vaimos-Vigyaiza, L. Determination, localization and heat inactivation of peroxidase in some vegetables, Acta Aliment. Acad. Sei. Hung. 4, 291, 1975.
    • (1975) , vol.4 , Issue.291
    • Mihailyi, K.1    Vaimos-Vigyaiza, L.2
  • 403
    • 84952432400 scopus 로고
    • Kohlrabi peroxidase: kinetics, heat inactivation and regeneration, Confructa
    • Vaimos-Vigyaiza, L. Mihailyi, K. and Farkas, J. Kohlrabi peroxidase: kinetics, heat inactivation and regeneration, Confructa, 24, 38, 1979.
    • (1979) , vol.24 , Issue.38
    • Vaimos-Vigyaiza, L.1    Mihailyi, K.2    Farkas, J.3
  • 404
    • 0015910532 scopus 로고
    • A new sensitive colorimetric assay for peroxidase using 3,3'-diaminobenzidine as hydrogen donor, Anal. Biochem
    • Herzog, V. and Fahimi, H.D. A new sensitive colorimetric assay for peroxidase using 3,3'-diaminobenzidine as hydrogen donor, Anal. Biochem. 55, 554, 1973.
    • (1973) , vol.55 , Issue.554
    • Herzog, V.1    Fahimi, H.D.2
  • 405
    • 0015229228 scopus 로고
    • Hydroxymethylhydroperoxide as inhibitor and peroxide substrate of horseradish peroxidase, Eur. J.
    • Biochem. 21, 348
    • Marklund, S. Hydroxymethylhydroperoxide as inhibitor and peroxide substrate of horseradish peroxidase, Eur. J. Biochem. 21, 348, 1971.
    • (1971)
    • Marklund, S.1
  • 406
    • 84952432402 scopus 로고    scopus 로고
    • Substrate specificity of plant eroxidases, FEBS Utters. 17, 181, I97I.
    • Chmfelnicka, J. Ohlsson, P.I. Paul, K.G. and Stigbrand, T. Substrate specificity of plant eroxidases, FEBS Utters. 17, 181, I97I.
    • Chmfelnicka, J.1    Ohlsson, P.I.2    Paul, K.G.3    Stigbrand, T.4
  • 408
    • 84952432404 scopus 로고
    • Untersuchungen aber die Inaktivierung von Isoenzymen in Lebensmitteln, I. Dannschich-isoelektrische Fokussierung, Dannschicht-Elektrophorese and Dannschicht-Gelchromatographie der Peroxidasen, Esterasen und Lipoxygenasen aus granen Bohnen, Chem. Mikrobiol. Technol. Lebensm
    • Delincace, H. Becker, E. and Radola, B.J. Untersuchungen aber die Inaktivierung von Isoenzymen in Lebensmitteln, I. Dannschich-isoelektrische Fokussierung, Dannschicht-Elektrophorese and Dannschicht-Gelchromatographie der Peroxidasen, Esterasen und Lipoxygenasen aus granen Bohnen, Chem. Mikrobiol. Technol. Lebensm. 4, 120, 1975.
    • (1975) , vol.4 , Issue.120
    • Delincace, H.1    Becker, E.2    Radola, B.J.3
  • 409
    • 84987336716 scopus 로고
    • Fractionation and characterization of peroxidase from ripe banana fruit, J. Food Sei
    • Nagle, N.E. and Haard, N.F. Fractionation and characterization of peroxidase from ripe banana fruit, J. Food Sei. 40, 576, 1975.
    • (1975) , vol.40 , Issue.576
    • Nagle, N.E.1    Haard, N.F.2
  • 410
    • 0016177594 scopus 로고
    • Electron microscopic and kinetic studies dealing with an artificial enzyme membrane. Application to a cytochemical model with the horseradish peroxidase-3,3'-diaminobenzidine system, J. Histochem. Cytochem
    • Barbotin, J.N. and Thomas, D. Electron microscopic and kinetic studies dealing with an artificial enzyme membrane. Application to a cytochemical model with the horseradish peroxidase-3,3'-diaminobenzidine system, J. Histochem. Cytochem. 22, 1048, 1974.
    • (1974) , vol.22
    • Barbotin, J.N.1    Thomas, D.2
  • 411
    • 84952432405 scopus 로고
    • Changes in peroxidase activity and peroxidase isozyme patterns of wheat during kernel growth and maturation
    • Cereal Chem. 51,345
    • Kruger, J.E. and LaBerge, D.E. Changes in peroxidase activity and peroxidase isozyme patterns of wheat during kernel growth and maturation, Cereal Chem. 51,345,1974.
    • (1974)
    • Kruger, J.E.1
  • 412
    • 0017381491 scopus 로고
    • Visualization of peroxidase isozymes with eugenol, a noncarcinogenic substrate, Anal. Biochem
    • Liu, E.H. and Gibson, D.M. Visualization of peroxidase isozymes with eugenol, a noncarcinogenic substrate, Anal. Biochem. 79, 597, 1977.
    • (1977) , vol.79 , Issue.597
    • Liu, E.H.1    Gibson, D.M.2
  • 413
    • 49849111681 scopus 로고
    • The oxidation of pyridoxal and related compounds by pea-seedling extracts or systems containing peroxidase, Phytochemistry
    • Hill, J.M. The oxidation of pyridoxal and related compounds by pea-seedling extracts or systems containing peroxidase, Phytochemistry, 9, 725, 1974.
    • (1974) , vol.9 , Issue.725
    • Hill, J.M.1
  • 414
    • 84987277432 scopus 로고
    • Some factors affecting rates of heat inactivation and reactivation of horseradish peroxidase, J. Food Sei
    • Lu, A.T. and Whitaker, J.R. Some factors affecting rates of heat inactivation and reactivation of horseradish peroxidase, J. Food Sei. 39, 1173, 1974.
    • (1974) , vol.39
    • Lu, A.T.1    Whitaker, J.R.2
  • 415
    • 0014559263 scopus 로고
    • Circular dichroism of Japanese radish peroxidase a. J. Biochem
    • Hamaguchi, K. Ikeda, K. Yoshida, Ch. and Morita, Y. Circular dichroism of Japanese radish peroxidase a. J. Biochem. 66, 191, 1969.
    • (1969) , vol.66 , Issue.191
    • Hamaguchi, K.1    Ikeda, K.2    Ch, Y.3
  • 417
    • 0015643644 scopus 로고
    • Thermal activation of peroxidase as a lipid oxidation catalyst, J. Am. Oil Chem. Soc
    • Eriksson, C.E. and Vallentin, K. Thermal activation of peroxidase as a lipid oxidation catalyst, J. Am. Oil Chem. Soc. 50, 264, 1973.
    • (1973) , vol.50 , Issue.264
    • Eriksson, C.E.1    Vallentin, K.2
  • 418
    • 0013893929 scopus 로고
    • Heme proteins. VII. Crystalline pineapple peroxidase B, Biochemistry
    • CI. and
    • Beaudreau, CI. and Yasunobu, K.T. Heme proteins. VII. Crystalline pineapple peroxidase B, Biochemistry, 5, 1405, 1966.
    • (1966) Beaudreau , vol.5
    • Yasunobu, K.T.1
  • 419
    • 84952432408 scopus 로고
    • Properties of peroxidase of healthy and Botrytis cinerea infected cabbage, Prikt. Biokhim. Mikrobiol
    • Kozhanova, O.N. and Aksenova, V.A. Properties of peroxidase of healthy and Botrytis cinerea infected cabbage, Prikt. Biokhim. Mikrobiol. 12, 753, 1976.
    • (1976) , vol.12 , Issue.753
    • Kozhanova, O.N.1    Aksenova, V.A.2
  • 420
    • 84952432409 scopus 로고    scopus 로고
    • Study into some properties of peroxidase in vegetable homogenates, Proc. 18th Hung.
    • Annu. Meeting Biochem. 1978, 197.
    • Vaimos-Vigyaiza, L. and Babos-Szebenyi, E. Study into some properties of peroxidase in vegetable homogenates, Proc. 18th Hung. Annu. Meeting Biochem. 1978, 197.
    • Vaimos-Vigyaiza, L.1    Babos-Szebenyi, E.2
  • 421
    • 84952432410 scopus 로고
    • Thermische Inaktivierung und Lagerungsverhalten technologisch wichtiger Enzyme
    • Doctoral thesis, Karlsruhe
    • Park, K.H. Thermische Inaktivierung und Lagerungsverhalten technologisch wichtiger Enzyme, Doctoral thesis, Karlsruhe, 1976.
    • (1976)
    • Park, K.H.1
  • 422
    • 84982634945 scopus 로고
    • Uber den Einfluss des Blanchierens, Gefrierens und Sterilisierens auf den Protein- und Aminosaurengehalt in grunen Erbsen, Nahrung
    • Kulesza, C. and Gertig, H. Uber den Einfluss des Blanchierens, Gefrierens und Sterilisierens auf den Protein- und Aminosaurengehalt in grunen Erbsen, Nahrung, 20, 369, 1976.
    • (1976) , vol.20 , Issue.369
    • Kulesza, C.1    Gertig, H.2
  • 423
    • 84982543208 scopus 로고
    • Zur Frage von Fermentaktivitat und Qualitat von Gemusegefrierkonserven. 2. Mitt. Einfluss auf die Qualitat des gefrorenen Gemuses, Nahrung
    • Bottcher, H. Zur Frage von Fermentaktivitat und Qualitat von Gemusegefrierkonserven. 2. Mitt. Einfluss auf die Qualitat des gefrorenen Gemuses, Nahrung, 19, 245, 1975.
    • (1975) , vol.19 , Issue.245
    • Bottcher, H.1
  • 424
    • 84981870093 scopus 로고
    • Thermal destruction of peroxidase in vegetables at high temperatures, Food Res
    • Esselen, W.B. and Anderson, E.E. Thermal destruction of peroxidase in vegetables at high temperatures, Food Res. 21, 322, 1956.
    • (1956) , vol.21 , Issue.322
    • Esselen, W.B.1    Anderson, E.E.2
  • 425
    • 84982335040 scopus 로고
    • Thermal destruction Tates and regeneration of peroxidase in green beans and turnips, Food Res
    • Zoueil, M.E. and Esselen, W.B. Thermal destruction Tates and regeneration of peroxidase in green beans and turnips, Food Res. 24, 119, 1958.
    • (1958) , vol.24 , Issue.119
    • Zoueil, M.E.1    Esselen, W.B.2
  • 426
    • 0017842701 scopus 로고
    • A new model to describe enzyme inactivation, Biotechnol. Bioeng
    • Cardoso, J.P. and Emery, A.N. A new model to describe enzyme inactivation, Biotechnol. Bioeng. 20, 1471, 1978.
    • (1978) , vol.20
    • Cardoso, J.P.1    Emery, A.N.2
  • 427
    • 84981851649 scopus 로고
    • Kinetics and energetics of thermal inactivation and the regeneration rates of a peroxidase system, J. Food Sei
    • Joffe, F.M. and Ball, C.O. Kinetics and energetics of thermal inactivation and the regeneration rates of a peroxidase system, J. Food Sei. 27, 587, 1962.
    • (1962) , vol.27 , Issue.587
    • Joffe, F.M.1    Ball, C.O.2
  • 428
    • 84952417231 scopus 로고
    • Thermal destruction and regeneration of enzymes in green bean and spinach puree, Food Technol
    • Resende, R. Francis, F.J. and Stumbo, C.R. Thermal destruction and regeneration of enzymes in green bean and spinach puree, Food Technol. 23, 63, 1969.
    • (1969) , vol.23 , Issue.63
    • Resende, R.1    Francis, F.J.2    Stumbo, C.R.3
  • 429
    • 84981873463 scopus 로고
    • Kinetic studies on the heat inactivation of peroxidase in sweet corn, J. Food Sei
    • Yamamoto, H.Y. Steinberg, M.P. and Nelson, A.I. Kinetic studies on the heat inactivation of peroxidase in sweet corn, J. Food Sei. 27, 113, 1962.
    • (1962) , vol.27 , Issue.113
    • Yamamoto, H.Y.1    Steinberg, M.P.2    Nelson, A.I.3
  • 430
    • 84952386090 scopus 로고
    • Destruction thermique de l'activitac peroxydasique. Interpretation des courbes experimentales, Rev. Gen. Froid
    • Clochard, A. and Guern, J. Destruction thermique de l'activitac peroxydasique. Interpretation des courbes experimentales, Rev. Gen. Froid. 64, 860, 1973.
    • (1973) , vol.64 , Issue.860
    • Clochard, A.1    Guern, J.2
  • 431
    • 84952432413 scopus 로고
    • Der Einfluss thermischer Behandlung von Spinat im Temperaturbereich bis 100C auf den Gehalt an wesentlichen Inhaltsstoffen. VII.
    • Mitteilung: Hitzeinaktivierung von Peroxidase-Isoenzymen in Spinat, Lebensm. Wiss. Technol. 8, 217
    • Delincace, H. and Schafer, W. Der Einfluss thermischer Behandlung von Spinat im Temperaturbereich bis 100C auf den Gehalt an wesentlichen Inhaltsstoffen. VII. Mitteilung: Hitzeinaktivierung von Peroxidase-Isoenzymen in Spinat, Lebensm. Wiss. Technol. 8, 217, 1975.
    • (1975)
    • Delincace, H.1    Schafer, W.2
  • 432
    • 84952419532 scopus 로고
    • Hitzebestandigkeit der Peroxidase, Z. Lebensm. Unters. Forsch
    • Winter, E. Hitzebestandigkeit der Peroxidase, Z. Lebensm. Unters. Forsch. 145, 3, 1971.
    • (1971) , vol.145 , Issue.3
    • Winter, E.1
  • 433
    • 0016702203 scopus 로고
    • Thermal denaturation and regeneration of Japanese-radish peroxidase, J. Biochem
    • Tamura, Y. and Morita, Y. Thermal denaturation and regeneration of Japanese-radish peroxidase, J. Biochem. 78, 561, 1975.
    • (1975) , vol.78 , Issue.561
    • Tamura, Y.1    Morita, Y.2
  • 434
    • 0017785532 scopus 로고
    • Verhalten von Holo-, Apo- und Coenzym der Peroxidase beim Erhitzen, Z. Lebensm. Unters, Forsch
    • Park, K.H. and Fricker, A. Verhalten von Holo-, Apo- und Coenzym der Peroxidase beim Erhitzen, Z. Lebensm. Unters, Forsch. 164, 167, 1977.
    • (1977) , vol.164 , Issue.167
    • Park, K.H.1    Fricker, A.2
  • 435
    • 84987300610 scopus 로고
    • Isolation and characterization of the native, thermally inactivated and regenerated horseradish peroxidase isozymes, J. Food Sei
    • Wang, S.S. and Dimarco, G.R. Isolation and characterization of the native, thermally inactivated and regenerated horseradish peroxidase isozymes, J. Food Sei. 37, 574, 1972.
    • (1972) , vol.37 , Issue.574
    • Wang, S.S.1    Dimarco, G.R.2
  • 437
    • 84952432415 scopus 로고
    • inactivation of peroxidase isoenzymes in green beans, Proc. 9 th Int.
    • Congr. Food Sei. Technol., 270.
    • Delincace, H. Becker, E. and Radola, B.J. Heat inactivation of peroxidase isoenzymes in green beans, Proc. 9 th Int. Congr. Food Sei. Technol. Vol. I, 1974, 270.
    • (1974) , vol.I
    • Delincace, H.1    Becker, E.2    Heat, B.J.3
  • 438
    • 84952390653 scopus 로고
    • Purification of Kohlrabi Peroxidase and a Study Into Its Isoenzymes
    • M.Sc. thesis, Budapest
    • Pozsair-Hajnal, K. Purification of Kohlrabi Peroxidase and a Study Into Its Isoenzymes, M.Sc. thesis, Budapest, 1979.
    • (1979)
    • Pozsair-Hajnal, K.1
  • 439
    • 0015182837 scopus 로고
    • The effect of heat on the isoelectric and size properties of horseradish peroxidase, Experientia
    • Delincace, H. Radola, J. and Drawert, F. The effect of heat on the isoelectric and size properties of horseradish peroxidase, Experientia, 27, 1264, 1971.
    • (1971) , vol.27
    • Delincace, H.1    Radola, J.2    Drawert, F.3
  • 440
    • 0015852144 scopus 로고
    • The effect of combined heat and irradiation treatment on the isoelectric and size properties of horseradish peroxidase, Acta Aliment. Acad. Sei. Hung
    • Delincace, H. Radola, J. and Drawert, F. The effect of combined heat and irradiation treatment on the isoelectric and size properties of horseradish peroxidase, Acta Aliment. Acad. Sei. Hung. 2, 259, 1973.
    • (1973) , vol.2 , Issue.259
    • Delincace, H.1    Radola, J.2    Drawert, F.3
  • 441
    • 84952398235 scopus 로고
    • The inactivation of peroxidase in relation to the high temperature-short time processing of vegetables, Lebensm. Wiss. Technol
    • Adams, J.B. The inactivation of peroxidase in relation to the high temperature-short time processing of vegetables, Lebensm. Wiss. Technol. 11, 71, 1978.
    • (1978) , vol.11 , Issue.71
    • Adams, J.B.1
  • 442
    • 0017148982 scopus 로고
    • Odor detectability of aldehydes and alcohols originating from lipid oxidation, Chem. Senses Flavor
    • Eriksson, C.E. Lundgren, B. and Vallentin, K. Odor detectability of aldehydes and alcohols originating from lipid oxidation, Chem. Senses Flavor, 2, 3, 1976.
    • (1976) , vol.2 , Issue.3
    • Eriksson, C.E.1    Lundgren, B.2    Vallentin, K.3
  • 443
    • 84952381027 scopus 로고
    • Thermal inactivation of lipoxygenase from peas Pisum sativum L. IV. Inactivation in whole peas, Lebensm. Wiss. Technol
    • Svensson, S.G. and Eriksson, C.E. Thermal inactivation of lipoxygenase from peas (Pisum sativum L. IV. Inactivation in whole peas, Lebensm. Wiss. Technol. 7, 145, 1974.
    • (1974) , vol.7 , Issue.145
    • Svensson, S.G.1    Eriksson, C.E.2
  • 445
    • 84982607598 scopus 로고
    • BAttcher
    • IL, Zur Frage von Fermentaktivitat and Qualitat von Gemasegefrierkonserven. I. Mitt. Die verbleibende Restaktivitat an Peroxydase, Nahrung, 19, 173
    • BAttcher, IL, Zur Frage von Fermentaktivitat and Qualitat von Gemasegefrierkonserven. I. Mitt. Die verbleibende Restaktivitat an Peroxydase, Nahrung, 19, 173, 1975.
    • (1975)
  • 446
    • 84981875144 scopus 로고
    • Thermal destruction and stability of peroxidase in acid foods, Food Res
    • Nebesky, E.A. Esselen, W.B. Kaplan, A.M. and Fellers, C.R. Thermal destruction and stability of peroxidase in acid foods, Food Res. 15, 114, 1950.
    • (1950) , vol.15 , Issue.114
    • Nebesky, E.A.1    Esselen, W.B.2    Kaplan, A.M.3    Fellers, C.R.4
  • 447
    • 84981753895 scopus 로고
    • Thermisch bedingte Aktivitatsanderungen bei Enzymen. I.
    • Mitt. Lipase, Acetylesterase, Peroxydase und Lipoxydase von Getreideprodukten, Nahrung, 11, 741
    • Rothe, M. and Stockei, J. Thermisch bedingte Aktivitatsanderungen bei Enzymen. I. Mitt. Lipase, Acetylesterase, Peroxydase und Lipoxydase von Getreideprodukten, Nahrung, 11, 741, 1967.
    • (1967)
    • Rothe, M.1    Stockei, J.2
  • 448
    • 0000618542 scopus 로고
    • Determining kinetic parameters for thermal inactivation of heat-resistant and heat-labile isozymes from thermal destruction curves, J. Food Sci
    • Ling, A.C. and Lund, D.B. Determining kinetic parameters for thermal inactivation of heat-resistant and heat-labile isozymes from thermal destruction curves, J. Food Sci. 43, 1307, 1978.
    • (1978) , vol.43
    • Ling, A.C.1    Lund, D.B.2
  • 449
    • 84952432418 scopus 로고
    • Dactermination automatique de l'inactivation thermique et de la racgacnacration des enzymes. Application a la peroxydase du pois Pisum sativum L., Lebensm. Wiss. Technol
    • Varoquaux, P. Clochard, A. Sarris, J. Avisse, CI. and Morfaux, J.N. Dactermination automatique de l'inactivation thermique et de la racgacnacration des enzymes. Application a la peroxydase du pois (Pisum sativum L.), Lebensm. Wiss. Technol. 8, 60, 1975.
    • (1975) , vol.8 , Issue.60
    • Varoquaux, P.1    Clochard, A.2    Morfaux, J.N.3
  • 450
    • 84952432419 scopus 로고
    • Stopping storage off-flavors by curbing peroxidase, Food Eng
    • Farkas, F.D. Goldblith, S.A. and Proctor, B.E. Stopping storage off-flavors by curbing peroxidase, Food Eng. 28, 52, 1956.
    • (1956) , vol.28 , Issue.52
    • Farkas, F.D.1    Goldblith, S.A.2    Proctor, B.E.3
  • 451
    • 84952403593 scopus 로고
    • Verhalten von Peroxydase beim Blanchieren von Gemase, Z. Lebensm. Unters. Forsch
    • Winter, E. Verhalten von Peroxydase beim Blanchieren von Gemase, Z. Lebensm. Unters. Forsch. 141, 201, 1969.
    • (1969) , vol.141 , Issue.201
    • Winter, E.1
  • 452
    • 84952419223 scopus 로고
    • Blanching of white potatoes by microwave energy followed by boiling water, J. Food Sei
    • Chen, S.C. Collins, J.L. McCarty, I.E. and Johnston, M.R. Blanching of white potatoes by microwave energy followed by boiling water, J. Food Sei. 36, 742, 1971.
    • (1971) , vol.36 , Issue.742
    • Chen, S.C.1    Collins, J.L.2    Johnston, M.R.3
  • 453
    • 84952413247 scopus 로고
    • Enzyme regeneration in high temperature-short time sterilized foods, Food Technol
    • Guyer, R.B. and Holmquist, J.W. Enzyme regeneration in high temperature-short time sterilized foods, Food Technol. 8, 547, 1954.
    • (1954) , vol.8 , Issue.547
    • Guyer, R.B.1    Holmquist, J.W.2
  • 454
    • 84952400538 scopus 로고
    • Regeneration of heat-inactivated peroxidase, J: Biol. Chem
    • Schwimmer, S. Regeneration of heat-inactivated peroxidase, J: Biol. Chem. 154, 487, 1944.
    • (1944) , vol.154 , Issue.487
    • Schwimmer, S.1
  • 455
    • 84981856199 scopus 로고
    • Peroxidase regeneration and its effect on quality in frozen peas and thawed peas,J. Food Sei
    • Pinsent, B.R.W. Peroxidase regeneration and its effect on quality in frozen peas and thawed peas,J. Food Sei. 27, 120, 1962.
    • (1962) , vol.27 , Issue.120
    • Pinsent, B.R.W.1
  • 456
    • 84952432420 scopus 로고
    • Investigations into the peroxidase activity of vegetables, Elelmez. Ipar.
    • Mihailyi, K. and Vaimos-Vigyaiza, L. Investigations into the peroxidase activity of vegetables, Elelmez. Ipar. 30, 314, 1976.
    • (1976) , vol.30 , Issue.314
    • Mihailyi, K.1    Vaimos-Vigyaiza, L.2
  • 457
    • 84952432421 scopus 로고
    • du blanchiment et de la durace de conservation, sur l'acvolution des caractares organoleptiques, de l'activitac peroxydasique et de l'acide ascorbique dans les haricots mange-tout congelacs, Rev. Gen. Froid
    • Philippon, J. and Rouet-Mayer, M.A. Incidence du blanchiment et de la durace de conservation, sur l'acvolution des caractares organoleptiques, de l'activitac peroxydasique et de l'acide ascorbique dans les haricots mange-tout congelacs, Rev. Gen. Froid, 62, 685, 1971.
    • (1971) Rouet-Mayer , vol.62 , Issue.685
    • Philippon, J.1    Incidence, M.A.2
  • 458
    • 2242476735 scopus 로고
    • Reversible inactivation of enzymes at low temperature. Studies of temperature dependence of phosphatase- and peroxidase-catalyzed reactions, J. Am. Chem. Soc
    • Maier, V.P. Tappel, A.L. and Volman, D.H. Reversible inactivation of enzymes at low temperature. Studies of temperature dependence of phosphatase- and peroxidase-catalyzed reactions, J. Am. Chem. Soc. 77, 1278, 1955.
    • (1955) , vol.77
    • Maier, V.P.1    Tappel, A.L.2    Volman, D.H.3
  • 459
    • 84952432422 scopus 로고
    • Modificazioni chimiche ed istologiche indotte dal congelamento negli ortaggi liofilizzati, Ind. Aliment
    • Crivelli, G. Modificazioni chimiche ed istologiche indotte dal congelamento negli ortaggi liofilizzati, Ind. Aliment. 127, 80, 1976.
    • (1976) , vol.127 , Issue.80
    • Crivelli, G.1
  • 460
    • 84952420135 scopus 로고
    • Le rale de l'acide sulfureux dans le processus d'oxydation peroxydasique de l'acide ascorbique en'pracsence de H2O2, Rev. Ferment.
    • Ind. Aliment19,113
    • Monikowski, C. and Chmialnicka, E. Le rale de l'acide sulfureux dans le processus d'oxydation peroxydasique de l'acide ascorbique en'pracsence de H2O2, Rev. Ferment. Ind. Aliment19,113,1964.
    • (1964)
    • Monikowski, C.1    Chmialnicka, E.2
  • 461
    • 84989998389 scopus 로고
    • Bisulfite effect on the chemistry and activity of horseradish peroxidase, J. Food Sei
    • Embs, R.J. and Markakis, P. Bisulfite effect on the chemistry and activity of horseradish peroxidase, J. Food Sei. 34, 500, 1969.
    • (1969) , vol.34 , Issue.500
    • Embs, R.J.1    Markakis, P.2
  • 462
    • 0014969963 scopus 로고
    • Partial purification and properties of enzyme inhibitors from unripe mangoes, Enzymologia
    • Mattoo, A.K. and Modi, V.V. Partial purification and properties of enzyme inhibitors from unripe mangoes, Enzymologia. 39, 237, 1970.
    • (1970) , vol.39 , Issue.237
    • Mattoo, A.K.1    Modi, V.V.2
  • 463
    • 0016162942 scopus 로고
    • Effect of naphthoquinones on the in vitro activity of peroxidase from horseradish, Prikl. Biokhim. Mikrobiol
    • Blagonravova, L.N. and Shcherbanovsky, L.R. Effect of naphthoquinones on the in vitro activity of peroxidase from horseradish, Prikl. Biokhim. Mikrobiol. 10, 666, 1974.
    • (1974) , vol.10 , Issue.666
    • Blagonravova, L.N.1    Shcherbanovsky, L.R.2
  • 464
    • 0017393683 scopus 로고
    • Thermische Inaktivierung und Lagerungsverhalten technologisch wichtiger Enzyme. III. Einfluss von Zusatzstoffen bei Peroxidase und Lipoxygenase, Z. Ernaehrungswiss
    • Park, K.H. Londn, M. and Fricker, A. Thermische Inaktivierung und Lagerungsverhalten technologisch wichtiger Enzyme. III. Einfluss von Zusatzstoffen bei Peroxidase und Lipoxygenase, Z. Ernaehrungswiss. 16, 98, 1977.
    • (1977) , vol.16 , Issue.98
    • Park, K.H.1    Londn, M.2    Fricker, A.3
  • 465
    • 84952432424 scopus 로고
    • Enzymatic reactions in the presence of polymers: influence of pH upon the interaction between horseradish peroxidase and ionic polymers, Lebensm. Wiss. Technol
    • Gatfield, I.L. and Stute, R. Enzymatic reactions in the presence of polymers: influence of pH upon the interaction between horseradish peroxidase and ionic polymers, Lebensm. Wiss. Technol. 8, 121, 1975.
    • (1975) , vol.8 , Issue.121
    • Gatfield, I.L.1    Stute, R.2
  • 466
    • 84952432425 scopus 로고
    • In vitro study of the effect of some ions on individual isoenzymes of pea and barley peroxidase, Dokl. Bolg. Akad. Nauk
    • Bakardjieva, N.T. In vitro study of the effect of some ions on individual isoenzymes of pea and barley peroxidase, Dokl. Bolg. Akad. Nauk. 30, 759, 1977.
    • (1977) , vol.30 , Issue.759
    • Bakardjieva, N.T.1
  • 467
    • 84952432426 scopus 로고    scopus 로고
    • Preparation of peroxidase isoenzymes from Kohlrabi, Abstr. 12th FEBS Meeting, Dresden, 1978, Abstr.
    • E. and 2417.
    • Vaimos-Vigyaiza, L. Pozsair-Hajnal, K. Babos-Szebenyi, E. and Hegedus-VAlgyesi, E. Preparation of peroxidase isoenzymes from Kohlrabi, Abstr. 12th FEBS Meeting, Dresden, 1978, (Abstr. 2417).
    • Vaimos-Vigyaiza, L.1    Babos-Szebenyi, K.2
  • 468
    • 84952432427 scopus 로고
    • The binding of plant enzymes for polyphenols. Study of ascorbic acid oxidase and peroxidase from squash, 9th Int.
    • Symp. on Chemistry of Natural Products
    • Marcheslni, A. Manitto, P. and Gallazzi, S. The binding of plant enzymes for polyphenols. Study of ascorbic acid oxidase and peroxidase from squash, 9th Int. Symp. on Chemistry of Natural Products, 1974.
    • (1974)
    • Marcheslni, A.1    Manitto, P.2    Gallazzi, S.3
  • 470
    • 0017134905 scopus 로고
    • The purification of horseradish peroxidase by affinity chromatography on Sepharose-bound Concanavalin A, Anal. Biochem.
    • 72,346
    • Brattain, M.G. Marks, M.E. and Pretlow, T.G. The purification of horseradish peroxidase by affinity chromatography on Sepharose-bound Concanavalin A, Anal. Biochem. 72,346,1976.
    • (1976)
    • Brattain, M.G.1    Marks, M.E.2    Pretlow, T.G.3
  • 471
    • 0016659527 scopus 로고
    • Fractionation of horseradish peroxidase by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography, Eur. J.
    • Biochem. 52, 321
    • Delincace, H. and Radola, J. Fractionation of horseradish peroxidase by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography, Eur. J. Biochem. 52, 321, 1975.
    • (1975)
    • Delincace, H.1    Radola, J.2
  • 472
    • 49949128467 scopus 로고
    • The effect of substrate concentration on the visualization of isoperoxidases in disc eletrophoresis, Phytochemistry
    • Novacky, A. and Hampton, R.E. The effect of substrate concentration on the visualization of isoperoxidases in disc eletrophoresis, Phytochemistry, 6, 1143, 1968.
    • (1968) , vol.6
    • Novacky, A.1    Hampton, R.E.2
  • 473
    • 49849108500 scopus 로고
    • Disc electrophoresis of analogous enzymes in hordeum, Phytochemistry
    • Mitra, R. Jagannath, D.R. and Bhatia, C.R. Disc electrophoresis of analogous enzymes in hordeum, Phytochemistry, 9, 1843, 1970.
    • (1970) , vol.9
    • Mitra, R.1    Jagannath, D.R.2    Bhatia, C.R.3
  • 474
    • 0014952478 scopus 로고
    • Thin-layer isoelectric focusing on Sephadex layers of horseradish peroxidase, Biochim. Biophys. Acta
    • Delincace, H. and Radola, B.J. Thin-layer isoelectric focusing on Sephadex layers of horseradish peroxidase, Biochim. Biophys. Acta, 200, 404, 1970.
    • (1970) , vol.200 , Issue.404
    • Delincace, H.1    Radola, B.J.2
  • 475
    • 29744460414 scopus 로고
    • Multiple components in horseradish peroxidase, Biochem. J
    • Jermyn, M.A. and Thomas, R. Multiple components in horseradish peroxidase, Biochem. J. 56, 631, 1954.
    • (1954) , vol.56 , Issue.631
    • Jermyn, M.A.1    Thomas, R.2
  • 476
    • 84952399466 scopus 로고
    • Four isoperoxidases from horseradish root, Acta Chem. Scand
    • Paul, K.G. and Stigbrand, T. Four isoperoxidases from horseradish root, Acta Chem. Scand. 24, 3607, 1970.
    • (1970) , vol.24
    • Paul, K.G.1    Stigbrand, T.2
  • 477
    • 50849150394 scopus 로고
    • Investigations on the multiple components of commercial horseradish peroxidase, Biochim. Biophys. Acta
    • Klapper, M.H. and Hackett, D.P. Investigations on the multiple components of commercial horseradish peroxidase, Biochim. Biophys. Acta, 96, 272, 1965.
    • (1965) , vol.96 , Issue.272
    • Klapper, M.H.1    Hackett, D.P.2
  • 478
    • 49949130126 scopus 로고
    • Chromatographic separation of horseradish peroxidase isozymes from commercial preparations, Phytochemistry
    • Kasinsky, H.E. and Hackett, D.P. Chromatographic separation of horseradish peroxidase isozymes from commercial preparations, Phytochemistry, 7, 1147, 1968.
    • (1968) , vol.7
    • Kasinsky, H.E.1    Hackett, D.P.2
  • 479
    • 84996276070 scopus 로고
    • Yoshida, Ch. Kitamura, I. and Ida, Sh. Isoenzymes of Japanese-radish peroxidase, Agrie. Biol. Chem
    • Morita, Y. Yoshida, Ch. Kitamura, I. and Ida, Sh. Isoenzymes of Japanese-radish peroxidase, Agrie. Biol. Chem. 34, 1191, 1970.
    • (1970) , vol.34
    • Morita, Y.1
  • 480
    • 84996364853 scopus 로고
    • Properties and Structures of peroxidase isoenzymes of Japanese-radish, Agrie. Biol. Chem
    • Ch. and
    • Morita, Y. Yoshida, Ch. and Maeda, Y. Properties and Structures of peroxidase isoenzymes of Japanese-radish, Agrie. Biol. Chem. 35, 1074, 1971.
    • (1971) Yoshida , vol.35
    • Morita, Y.1    Maeda, Y.2
  • 481
    • 3543108071 scopus 로고
    • Purification and properties of cytochrome c and two peroxidases from spinach leaves, Plant Cell Physiol
    • Asada, K. and Takahashi, M. Purification and properties of cytochrome c and two peroxidases from spinach leaves, Plant Cell Physiol. 12, 361, 1971.
    • (1971) , vol.12 , Issue.361
    • Asada, K.1    Takahashi, M.2
  • 482
    • 0014428899 scopus 로고
    • Doubly discontinuous electrophoresis on sucrose gradients for the analysis of plant peroxidases, Anal. Biochem
    • Racusen, D. and Foote, M. Doubly discontinuous electrophoresis on sucrose gradients for the analysis of plant peroxidases, Anal. Biochem. 25, 164, 1968.
    • (1968) , vol.25 , Issue.164
    • Racusen, D.1    Foote, M.2
  • 483
    • 0014679298 scopus 로고
    • Increased buffer density as a means of separating peroxidase isoenzymes by preparative continuous-flow carrier-free electrophoresis, Anal. Biochem
    • Evans, J.J. Increased buffer density as a means of separating peroxidase isoenzymes by preparative continuous-flow carrier-free electrophoresis, Anal. Biochem. 32, 101, 1969.
    • (1969) , vol.32 , Issue.101
    • Evans, J.J.1
  • 485
    • 84952432435 scopus 로고
    • Lopez, A. Evaluation of quantitative methods of determining peroxidase in vegetables, I. The indophenol and the o-phenylene diamine methods, Food Technol
    • Ch. B. and
    • Wood, Ch. B. and Lopez, A. Evaluation of quantitative methods of determining peroxidase in vegetables, I. The indophenol and the o-phenylene diamine methods, Food Technol. 17, 497, 1963.
    • (1963) Wood , vol.17 , Issue.497
  • 486
    • 0014466660 scopus 로고
    • Improved peroxidase assay method using leuco 2,3’, 6-trichloroindophenol and application to comparative measurements of peroxidatic catalysis, Anal. Biochem
    • Nickel, K.S. and Cunningham, B.A. Improved peroxidase assay method using leuco 2,3’, 6-trichloroindophenol and application to comparative measurements of peroxidatic catalysis, Anal. Biochem. 27, 292, 1969.
    • (1969) , vol.27 , Issue.292
    • Nickel, K.S.1    Cunningham, B.A.2
  • 487
    • 0014236699 scopus 로고
    • Homovanillic acid as a fluorimetric substrate for oxidative enzymes, Anal. Chem
    • Guilbault, G.C. Brignac, P. and Zimmer, M. Homovanillic acid as a fluorimetric substrate for oxidative enzymes, Anal. Chem. 40, 190, 1968.
    • (1968) , vol.40 , Issue.190
    • Guilbault, G.C.1    Brignac, P.2    Zimmer, M.3
  • 488
    • 0004105640 scopus 로고
    • Enzymatic Methods of Analysis
    • Pergamon Press, New York, 87.
    • Guilbault, G.C. Enzymatic Methods of Analysis, Pergamon Press, New York, 1968, 87.
    • (1968)
    • Guilbault, G.C.1
  • 489
    • 84952404508 scopus 로고
    • Studies on the oxidation of indole-3-acetic acid by peroxidase enzymes. Colorimetric determination of indole-3-acetic acid oxidation products, Plant Physiol
    • Meudt, W.J. and Gaines, T.P. Studies on the oxidation of indole-3-acetic acid by peroxidase enzymes. Colorimetric determination of indole-3-acetic acid oxidation products, Plant Physiol. 42, 1395, 1967.
    • (1967) , vol.42
    • Meudt, W.J.1    Gaines, T.P.2
  • 490
    • 84952420750 scopus 로고
    • The effect of water stress on indoleacetic acid oxidase in pea plants, Plant Physiol
    • Derbyshire, B. The effect of water stress on indoleacetic acid oxidase in pea plants, Plant Physiol. 47, 65, 1971.
    • (1971) , vol.47 , Issue.65
    • Derbyshire, B.1
  • 493
    • 84952432436 scopus 로고
    • La Peroxydase du raisin. Etude de quelques propriactacs, Ann. Technol. Agrie
    • Ournac, A. and Poux, C. La Peroxydase du raisin. Etude de quelques propriactacs, Ann. Technol. Agrie. 23, 17, 1974.
    • (1974) , vol.23 , Issue.17
    • Ournac, A.1    Poux, C.2
  • 494
    • 84985143809 scopus 로고
    • Peroxidase reactions and orange juice quality, J. Food Sei
    • Bruemmer, J.H. Roe, B. and Bowen, E.R. Peroxidase reactions and orange juice quality, J. Food Sei. 41, 186, 1976.
    • (1976) , vol.41 , Issue.186
    • Bruemmer, J.H.1    Roe, B.2    Bowen, E.R.3
  • 495
    • 33947391866 scopus 로고
    • Study of hydrogen peroxide, potato enzymes and blackspot, Am. Potato J
    • Weaver, M.L. and Hautala, E. Study of hydrogen peroxide, potato enzymes and blackspot, Am. Potato J. 47, 457, 1970.
    • (1970) , vol.47 , Issue.457
    • Weaver, M.L.1    Hautala, E.2
  • 496
    • 84952401835 scopus 로고
    • De novo synthesis of peroxidase isozymes in sweet potato slices, Plant Physiol
    • Shannon, M. Uritani, I. and Imaseki, H. De novo synthesis of peroxidase isozymes in sweet potato slices, Plant Physiol. 47, 493, 1971.
    • (1971) , vol.47 , Issue.493
    • Shannon, M.1    Uritani, I.2    Imaseki, H.3
  • 497
    • 84952432437 scopus 로고
    • Influence de certains sels de sodium sur la durace du blanchiment des haricots verts, Ind. Aliment. Agrie
    • Thomopoulos, C. Influence de certains sels de sodium sur la durace du blanchiment des haricots verts, Ind. Aliment. Agrie. 92, 531, 1975.
    • (1975) , vol.92 , Issue.531
    • Thomopoulos, C.1
  • 498
    • 84952399272 scopus 로고
    • Peroxidase activity in onion bulbs of long and short dormancy, HortSeienee
    • Poovaiah, B.W. Vest, G. and Rasmussen, H.P. Peroxidase activity in onion bulbs of long and short dormancy, HortSeienee, 7, 553, 1972.
    • (1972) , vol.7 , Issue.553
    • Poovaiah, B.W.1    Vest, G.2    Rasmussen, H.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.