메뉴 건너뛰기




Volumn 47, Issue 1, 2009, Pages 32-38

Biochemical properties of soluble and bound peroxidases from artichoke heads and leaves

Author keywords

Artichoke (Cynara cardunculus); Browning; Characterization; Regeneration; Soluble and bound peroxidases; Thermostability

Indexed keywords

BROWNING; CYNARA CARDUNCULUS; REGENERATION; SOLUBLE AND BOUND PEROXIDASES; THERMOSTABILITY;

EID: 69049083812     PISSN: 13309862     EISSN: 13342606     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0023110077 scopus 로고
    • Changes in phenolic compounds during the development and cold storage of artichoke (Cynara scolymus L.)
    • V. Lattanzio, C.F. van Sumere, Changes in phenolic compounds during the development and cold storage of artichoke (Cynara scolymus L.), Food Chem. 24 (1987) 37-50.
    • (1987) Food Chem. , vol.24 , pp. 37-50
    • Lattanzio, V.1    van Sumere, C.F.2
  • 3
    • 0347543938 scopus 로고    scopus 로고
    • Bioactive polyphenols: Their role in quality and storability of fruit and vegetables
    • V. Lattanzio, Bioactive polyphenols: Their role in quality and storability of fruit and vegetables, J. Appl. Bot. 77 (2003) 128-146.
    • (2003) J. Appl. Bot. , vol.77 , pp. 128-146
    • Lattanzio, V.1
  • 4
    • 38249026407 scopus 로고
    • The beneficial effect of citric and ascorbic acid on the phenolic browning reaction in stored artichoke (Cynara scolymus L.) heads
    • V. Lattanzio, V. Linsalata, S. Palmieri, C.F. van Sumere, The beneficial effect of citric and ascorbic acid on the phenolic browning reaction in stored artichoke (Cynara scolymus L.) heads, Food Chem. 33 (1989) 93-106.
    • (1989) Food Chem. , vol.33 , pp. 93-106
    • Lattanzio, V.1    Linsalata, V.2    Palmieri, S.3    van Sumere, C.F.4
  • 5
    • 77956995750 scopus 로고
    • Food Browning as a Polyphenol Reaction
    • C.O. Chichester, E.M. Mrak, G.F. Stewart (Eds.), Academic Press, USA
    • A.G. Mathew, H.A.B. Parpia: Food Browning as a Polyphenol Reaction. In: Advances in Food Research, Vol. 19, C.O. Chichester, E.M. Mrak, G.F. Stewart (Eds.), Academic Press, USA (1971) pp. 75-145.
    • (1971) Advances in Food Research , vol.19 , pp. 75-145
    • Mathew, A.G.1    Parpia, H.A.B.2
  • 6
    • 84985165999 scopus 로고
    • Peroxidase and its relationship to food flavor and quality: A review
    • F.S. Burnette, Peroxidase and its relationship to food flavor and quality: A review, J. Food Sci. 42 (1977) 1-6.
    • (1977) J. Food Sci. , vol.42 , pp. 1-6
    • Burnette, F.S.1
  • 9
    • 0019741905 scopus 로고
    • Polyphenol oxidase and peroxidase in fruits and vegetables
    • L. Vámos-Vigyázó, Polyphenol oxidase and peroxidase in fruits and vegetables, CRC Crit. Rev. Food Sci. Nutr. 15 (1981) 49-127.
    • (1981) CRC Crit. Rev. Food Sci. Nutr. , vol.15 , pp. 49-127
    • Vámos-Vigyázó, L.1
  • 10
    • 43949168895 scopus 로고
    • 2 during enzymic oxidation of catechin
    • 2 during enzymic oxidation of catechin, Phytochemistry, 33 (1993) 29-34.
    • (1993) Phytochemistry , vol.33 , pp. 29-34
    • Jiang, Y.1    Miles, P.W.2
  • 11
    • 0001384191 scopus 로고    scopus 로고
    • Oxidation of chlorogenic acid, catechins, and 4-methylcatechol in model solutions by combinations of pear (Pyrus communis cv. Williams) polyphenol oxidase and peroxidase: A possible involvement of peroxidase in enzymatic browning
    • F.C. Richard-Forget, F.A. Gauillard, Oxidation of chlorogenic acid, catechins, and 4-methylcatechol in model solutions by combinations of pear (Pyrus communis cv. Williams) polyphenol oxidase and peroxidase: A possible involvement of peroxidase in enzymatic browning, J. Agric. Food Chem. 45 (1997) 2472-2476.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2472-2476
    • Richard-Forget, F.C.1    Gauillard, F.A.2
  • 12
    • 0032799481 scopus 로고    scopus 로고
    • Age-dependent changes in levels of ascorbic acid and chlorogenic acid, and activities of peroxidase and superoxide dismutase in the apoplast of tobacco leaves: Mechanism of the oxidation of chlorogenic acid in the apoplast
    • U. Takahama, M. Hirotsu, T. Oniki, Age-dependent changes in levels of ascorbic acid and chlorogenic acid, and activities of peroxidase and superoxide dismutase in the apoplast of tobacco leaves: Mechanism of the oxidation of chlorogenic acid in the apoplast, Plant Cell Physiol. 40 (1999) 716-724.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 716-724
    • Takahama, U.1    Hirotsu, M.2    Oniki, T.3
  • 13
    • 0000481365 scopus 로고
    • 2-oxidoreductase, E.C. 1.11.1.7.). Part 1: Kaempferol
    • 2-oxidoreductase, E.C. 1.11.1.7.). Part 1: Kaempferol, Food Chem. 17 (1985) 143-154.
    • (1985) Food Chem. , vol.17 , pp. 143-154
    • Miller, E.1    Schreier, P.2
  • 14
    • 0001166185 scopus 로고
    • Peroxidases and Catalases in Food
    • D.S. Robinson, N.A.M. Eskin (Eds.) Amsterdam, The Netherlands
    • D.S. Robinson: Peroxidases and Catalases in Food. In: Oxidative Enzymes in Food, D.S. Robinson, N.A.M. Eskin (Eds.), Elsevier Applied Science, Amsterdam, The Netherlands (1991) pp. 1-48.
    • (1991) Oxidative Enzymes in Food. Elsevier Applied Science , pp. 1-48
    • Robinson, D.S.1
  • 15
    • 40749121309 scopus 로고    scopus 로고
    • Thermostability of soluble and bound peroxidases from artichoke and a mathematical model of its inactivation kinetics
    • L. Sergio, M. Pieralice, D. Di Venere, A. Cardinali, Thermostability of soluble and bound peroxidases from artichoke and a mathematical model of its inactivation kinetics, Food Technol. Biotechnol. 45 (2007) 367-373.
    • (2007) Food Technol. Biotechnol. , vol.45 , pp. 367-373
    • Sergio, L.1    Pieralice, M.2    Di Venere, D.3    Cardinali, A.4
  • 16
    • 0346058017 scopus 로고    scopus 로고
    • Purification and characterization of membrane-bound peroxidases from Metroxylon sagu
    • G.H. Onsa, N. bin Saari, J. Selamat, J. Bakar, Purification and characterization of membrane-bound peroxidases from Metroxylon sagu, Food Chem. 85 (2004) 365-376.
    • (2004) Food Chem. , vol.85 , pp. 365-376
    • Onsa, G.H.1    bin Saari, N.2    Selamat, J.3    Bakar, J.4
  • 17
    • 0041478906 scopus 로고
    • Heat stability of peroxidase from orange
    • K.M. McLellan, D.S. Robinson, Heat stability of peroxidase from orange, Food Chem. 13 (1984) 139-147.
    • (1984) Food Chem. , vol.13 , pp. 139-147
    • McLellan, K.M.1    Robinson, D.S.2
  • 21
    • 0034072280 scopus 로고    scopus 로고
    • Isolation and partial characterization of thermostable isoperoxidases from potato (Solanum tuberosum L.) tuber sprouts
    • C.F.S. Boucoiran, J.W. Kijne, K. Recourt, Isolation and partial characterization of thermostable isoperoxidases from potato (Solanum tuberosum L.) tuber sprouts, J. Agric. Food Chem. 48 (2000) 701-707.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 701-707
    • Boucoiran, C.F.S.1    Kijne, J.W.2    Recourt, K.3
  • 22
    • 33751330608 scopus 로고
    • The determination of enzyme dis-sociation constants
    • H. Lineweaver, D. Burk, The determination of enzyme dis-sociation constants, J. Am. Chem. Soc. 56 (1934) 658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 24
    • 34248187341 scopus 로고
    • Alteration of oxidative enzymes in potato tuber tissue by infection with Phytophtora infestans
    • K. Tomiyama, M.A. Stahmann, Alteration of oxidative enzymes in potato tuber tissue by infection with Phytophtora infestans, Plant Physiol. 39 (1964) 483-490.
    • (1964) Plant Physiol. , vol.39 , pp. 483-490
    • Tomiyama, K.1    Stahmann, M.A.2
  • 26
    • 0000506710 scopus 로고
    • Cross-linkage of matrix polymers in the growing cell wall of angiosperms
    • S.C. Fry, Cross-linkage of matrix polymers in the growing cell wall of angiosperms, Ann. Rev. Plant Physiol. 37 (1986) 165-186.
    • (1986) Ann. Rev. Plant Physiol. , vol.37 , pp. 165-186
    • Fry, S.C.1
  • 27
    • 3242685192 scopus 로고    scopus 로고
    • Effects of polyphenol oxidase and peroxidase activity, phenolics and lignin content on the browning of cut jicama
    • E.N. Aquino-Bolaños, E. Mercado-Silva, Effects of polyphenol oxidase and peroxidase activity, phenolics and lignin content on the browning of cut jicama, Postharvest Biol. Technol. 33 (2004) 275-283.
    • (2004) Postharvest Biol. Technol. , vol.33 , pp. 275-283
    • Aquino-Bolaños, E.N.1    Mercado-Silva, E.2
  • 28
    • 0002930551 scopus 로고
    • A comparative study of a cationic peroxidase from peanut and an anionic peroxidase from petunia
    • B.M. van den Berg, R.N. Chibbar, R.B. van Huystee, A comparative study of a cationic peroxidase from peanut and an anionic peroxidase from petunia, Plant Cell Rep. 2 (1983) 304-307.
    • (1983) Plant Cell Rep. , vol.2 , pp. 304-307
    • van den Berg, B.M.1    Chibbar, R.N.2    van Huystee, R.B.3
  • 29
    • 0002459043 scopus 로고
    • Integrated Relationships of Biochemical and Physiological Peroxidase Activities
    • H. Greppin, C. Penel, T. Gaspar (Eds.), University Press, Geneva, Switzerland
    • T. Gaspar: Integrated Relationships of Biochemical and Physiological Peroxidase Activities. In: Molecular and Physiological Aspects of Plant Peroxidases, H. Greppin, C. Penel, T. Gaspar (Eds.), University Press, Geneva, Switzerland (1986) pp. 455-468.
    • (1986) Molecular and Physiological Aspects of Plant Peroxidases , pp. 455-468
    • Gaspar, T.1
  • 30
    • 0027951318 scopus 로고
    • Apoplastic peroxidases and lignification in needles of Norway spruce (Picea abies L.)
    • A. Polle, T. Otter, F. Seifert, Apoplastic peroxidases and lignification in needles of Norway spruce (Picea abies L.), Plant Physiol. 106 (1994) 53-60.
    • (1994) Plant Physiol. , vol.106 , pp. 53-60
    • Polle, A.1    Otter, T.2    Seifert, F.3
  • 31
    • 0003105372 scopus 로고
    • Cell Compartmentation and Specific Roles of Isoenzymes
    • H. Greppin, C. Penel, T. Gaspar (Eds.), University Press, Geneva, Switzerland
    • M. Mäder, A. Nessel, P. Schloss: Cell Compartmentation and Specific Roles of Isoenzymes. In: Molecular and Physiological Aspects of Plant Peroxidases, H. Greppin, C. Penel, T. Gaspar (Eds.), University Press, Geneva, Switzerland (1986) pp. 246-260.
    • (1986) Molecular and Physiological Aspects of Plant Peroxidases , pp. 246-260
    • Mäder, M.1    Nessel, A.2    Schloss, P.3
  • 32
    • 0342813156 scopus 로고    scopus 로고
    • Structural properties of peroxidases
    • L. Banci, Structural properties of peroxidases, J. Biotechnol. 53 (1997) 253-263.
    • (1997) J. Biotechnol. , vol.53 , pp. 253-263
    • Banci, L.1
  • 33
    • 0000058708 scopus 로고
    • Effect of pH on Enzyme-Catalyzed Reactions
    • Marcel Dekker, New York, USA
    • J.R. Whitaker: Effect of pH on Enzyme-Catalyzed Reactions. In: Principles of Enzymology for the Food Science, Marcel Dekker, New York, USA (1994) pp. 271-300.
    • (1994) Principles of Enzymology for the Food Science , pp. 271-300
    • Whitaker, J.R.1
  • 34
    • 33750047838 scopus 로고    scopus 로고
    • The contribution of an ionic peroxidase isozyme to enzyme-mediated browning in Dioscorea esculenta L. tubers
    • O. Omidiji, J.E. Okpuzor, O. Otubu, The contribution of an ionic peroxidase isozyme to enzyme-mediated browning in Dioscorea esculenta L. tubers, Pakistan J. Nutr. 5 (2006) 478-480.
    • (2006) Pakistan J. Nutr. , vol.5 , pp. 478-480
    • Omidiji, O.1    Okpuzor, J.E.2    Otubu, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.