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Volumn 45, Issue 4, 2007, Pages 367-373

Thermostability of soluble and bound peroxidases from artichoke and a mathematical model of its inactivation kinetics

Author keywords

Artichoke; Blanching; Kinetic parameters; Mathematical model; Peroxidase; Thermal inactivation

Indexed keywords

ARTICHOKE; HEAT SENSITIVITY; HEAT STABILITY; INACTIVATION KINETICS; PEROXIDASE; PEROXIDASE (POD); SERIES-TYPE; THERMAL INACTIVATION;

EID: 40749121309     PISSN: 13309862     EISSN: 13342606     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 84985165999 scopus 로고
    • Peroxidase and its relationship to food flavour and quality: A review
    • F.S. Burnette, Peroxidase and its relationship to food flavour and quality: A review, J. Food Sci. 42 (1977) 1-6.
    • (1977) J. Food Sci , vol.42 , pp. 1-6
    • Burnette, F.S.1
  • 2
    • 0030922738 scopus 로고    scopus 로고
    • Guaiacol peroxidase associated to soybean root plasma membranes oxidized ascorbate
    • A. Vianello, M. Zancani, G. Nagy, F. Macri, Guaiacol peroxidase associated to soybean root plasma membranes oxidized ascorbate, J. Plant Physiol. 150 (1997) 573-577.
    • (1997) J. Plant Physiol , vol.150 , pp. 573-577
    • Vianello, A.1    Zancani, M.2    Nagy, G.3    Macri, F.4
  • 3
    • 0033150370 scopus 로고    scopus 로고
    • Isolation of tabaco isoperoxidases accumulated in cell-suspension culture medium and characterization of activities related to cell wall metabolism
    • A. De Marco, P. Guzzardi, È. Jamet, Isolation of tabaco isoperoxidases accumulated in cell-suspension culture medium and characterization of activities related to cell wall metabolism, Plant Physiol. 120 (1999) 371-381.
    • (1999) Plant Physiol , vol.120 , pp. 371-381
    • De Marco, A.1    Guzzardi, P.2    Jamet, E.3
  • 4
    • 0000089427 scopus 로고
    • Peroxidases and Their Significance in Fruit and Vegetables
    • P.F. Fox Ed, Elsevier Applied Science, Amsterdam, The Netherlands
    • D.S. Robinson: Peroxidases and Their Significance in Fruit and Vegetables. In: Food Enzymology, Vol. 1, P.F. Fox (Ed.), Elsevier Applied Science, Amsterdam, The Netherlands (1991) pp. 399-426.
    • (1991) Food Enzymology , vol.1 , pp. 399-426
    • Robinson, D.S.1
  • 5
    • 0001166185 scopus 로고
    • Peroxidases and Catalases in Foods
    • D.S. Robinson, N.A.M. Eskin Eds, Elsevier Applied Science, Amsterdam, The Netherlands
    • D.S. Robinson: Peroxidases and Catalases in Foods. In: Oxidative Enzymes in Foods, D.S. Robinson, N.A.M. Eskin (Eds.), Elsevier Applied Science, Amsterdam, The Netherlands (1991.) pp. 1-48.
    • (1991) Oxidative Enzymes in Foods , pp. 1-48
    • Robinson, D.S.1
  • 6
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • K.G. Welinder, Superfamily of plant, fungal and bacterial peroxidases, Curr. Opin. Struct. Biol. 2 (1992) 388-393.
    • (1992) Curr. Opin. Struct. Biol , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 7
    • 0030998838 scopus 로고    scopus 로고
    • Regeneration and the kinetics of peroxidase inactivation
    • J.B. Adams, Regeneration and the kinetics of peroxidase inactivation, Food Chem. 60 (1997) 201-206.
    • (1997) Food Chem , vol.60 , pp. 201-206
    • Adams, J.B.1
  • 8
    • 85005519705 scopus 로고    scopus 로고
    • P.H. Moulding, J. Goodfellow, K.M. McLellan, D.S. Robinson, The occurrence of isoperoxidases in Conference pears, Int. J. Food Sci. Technol. 24 (1989) 269-275.
    • P.H. Moulding, J. Goodfellow, K.M. McLellan, D.S. Robinson, The occurrence of isoperoxidases in Conference pears, Int. J. Food Sci. Technol. 24 (1989) 269-275.
  • 9
    • 85005622357 scopus 로고
    • The heat stability and isoenzyme composition of peroxidases in Ohane grapes
    • D.S. Robinson, M.R. Bretherick, J.K. Donnelly, The heat stability and isoenzyme composition of peroxidases in Ohane grapes, Int. J. Food Sci. Technol. 24 (1989) 613-618.
    • (1989) Int. J. Food Sci. Technol , vol.24 , pp. 613-618
    • Robinson, D.S.1    Bretherick, M.R.2    Donnelly, J.K.3
  • 10
    • 0027155644 scopus 로고
    • The thermostability of purified mango isoperoxidases
    • A.A. Khan, D.S. Robinson, The thermostability of purified mango isoperoxidases, Food Chem. 47 (1993) 53-59.
    • (1993) Food Chem , vol.47 , pp. 53-59
    • Khan, A.A.1    Robinson, D.S.2
  • 11
    • 0000618542 scopus 로고
    • Determining kinetic parameters for thermal inactivation of heat-resistant and heat-labile isozymes from thermal destruction curves
    • A.C. Ling, D.B. Lund, Determining kinetic parameters for thermal inactivation of heat-resistant and heat-labile isozymes from thermal destruction curves, J. Food Sci. 43 (1978) 1307-1310.
    • (1978) J. Food Sci , vol.43 , pp. 1307-1310
    • Ling, A.C.1    Lund, D.B.2
  • 12
    • 0000124213 scopus 로고
    • Inactivation of peroxidase, lipoxygenase, and polyphenol oxidase by manothermosonication
    • P. Lopez, F.J. Sala, J.L. Fuente, S. Condon, J. Raso, J. Burgos, Inactivation of peroxidase, lipoxygenase, and polyphenol oxidase by manothermosonication, J. Agric. Food Chem. 42 (1994) 252-256.
    • (1994) J. Agric. Food Chem , vol.42 , pp. 252-256
    • Lopez, P.1    Sala, F.J.2    Fuente, J.L.3    Condon, S.4    Raso, J.5    Burgos, J.6
  • 13
    • 0022013872 scopus 로고
    • Categorisation of enzyme deactivations using a series-type mechanism
    • J.P. Henley, A. Sadana, Categorisation of enzyme deactivations using a series-type mechanism, Enzyme Microb. Technol. 7 (1985) 50-60.
    • (1985) Enzyme Microb. Technol , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 14
    • 0031031813 scopus 로고    scopus 로고
    • Electrospray mass spectrometric study of haem changes during peroxidase denaturation
    • J.B. Adams, S.J. Lock, Electrospray mass spectrometric study of haem changes during peroxidase denaturation, Food Chem. 58 (1997) 173-175.
    • (1997) Food Chem , vol.58 , pp. 173-175
    • Adams, J.B.1    Lock, S.J.2
  • 15
    • 0033021165 scopus 로고    scopus 로고
    • The termostability of purified isoperoxidases from Brassica oleracea var. gemmifera
    • J.L. Forsyth, R.K. Owusu-Apenten, D.S. Robinson, The termostability of purified isoperoxidases from Brassica oleracea var. gemmifera, Food Chem. 65 (1999) 99-109.
    • (1999) Food Chem , vol.65 , pp. 99-109
    • Forsyth, J.L.1    Owusu-Apenten, R.K.2    Robinson, D.S.3
  • 16
    • 0034072280 scopus 로고    scopus 로고
    • Isolation and partial characterization of thermostable isoperoxidase from potato
    • C.F.S. Boucoiran, J.W. Kijne, K. Recourt, Isolation and partial characterization of thermostable isoperoxidase from potato, 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
  • 17
    • 0031670162 scopus 로고    scopus 로고
    • Purification and thermostability of isoperoxidase from oranges
    • E. Clemente, Purification and thermostability of isoperoxidase from oranges, Phytochemistry, 49 (1998) 29-36.
    • (1998) Phytochemistry , vol.49 , pp. 29-36
    • Clemente, E.1
  • 18
    • 0019741905 scopus 로고
    • Polyphenol oxidase and peroxidase in fruits and vegetables
    • L. Vamos-Vigyazo, 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
    • Vamos-Vigyazo, L.1
  • 19
    • 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
  • 22
    • 84962300028 scopus 로고
    • Characterization of the peroxidase system in winter rye seedlings: Compartmentation and dependance on leaf development and hydrogen donors used
    • G. Ievinsh, Characterization of the peroxidase system in winter rye seedlings: Compartmentation and dependance on leaf development and hydrogen donors used, J. Plant Physiol. 140 (1992) 257-263.
    • (1992) J. Plant Physiol , vol.140 , pp. 257-263
    • Ievinsh, G.1
  • 24
    • 84985204884 scopus 로고
    • Changes in soluble and bound peroxidase-IAA oxidase during tomato fruit development
    • R.L. Thomas, J.J. Jen, C.V. Morr, Changes in soluble and bound peroxidase-IAA oxidase during tomato fruit development, J. Food Sci. 47 (1981) 158-161.
    • (1981) J. Food Sci , vol.47 , pp. 158-161
    • Thomas, R.L.1    Jen, J.J.2    Morr, C.V.3
  • 26
    • 0000361037 scopus 로고
    • The effect of heat on cabbage and Brussels sprout peroxidase enzymes
    • K.M. McLellan, D.S. Robinson, The effect of heat on cabbage and Brussels sprout peroxidase enzymes, Food Chem. 7 (1981) 257-266.
    • (1981) Food Chem , vol.7 , pp. 257-266
    • McLellan, K.M.1    Robinson, D.S.2
  • 28
    • 34248194075 scopus 로고    scopus 로고
    • Characterization and partial purification of peroxidase from artichoke leaves
    • A. Cardinali, D. Di Venere, L. Sergio, V. Linsalata, Characterization and partial purification of peroxidase from artichoke leaves, Acta Hort. 681 (2005) 445-452.
    • (2005) Acta Hort , vol.681 , pp. 445-452
    • Cardinali, A.1    Di Venere, D.2    Sergio, L.3    Linsalata, V.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the hand of bacteriophage
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the hand of bacteriophage, Nature, 22 (1970) 680-685.
    • (1970) Nature , vol.22 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0028861444 scopus 로고
    • Peroxidase isozyme polymorphism as a potential marker for detection of field resistance in Cucumis sativus to cucumber downy mildew (Pseudoperonospora cubensis (Berk, et Curt.) Rostov.)
    • A. Lebeda, K. Dolezal, Peroxidase isozyme polymorphism as a potential marker for detection of field resistance in Cucumis sativus to cucumber downy mildew (Pseudoperonospora cubensis (Berk, et Curt.) Rostov.), J. Plant Dis. Prot. 102 (1995) 467-471.
    • (1995) J. Plant Dis. Prot , vol.102 , pp. 467-471
    • Lebeda, A.1    Dolezal, K.2
  • 32
    • 34248187341 scopus 로고
    • Alteration of oxidative enzymes in potato tuber tissue by infection with Phytophthora infestans
    • K. Tomiyama, M.A. Stahmann, Alteration of oxidative enzymes in potato tuber tissue by infection with Phytophthora infestans, Plant Physiol. 39 (1964) 483-490.
    • (1964) Plant Physiol , vol.39 , pp. 483-490
    • Tomiyama, K.1    Stahmann, M.A.2
  • 33
    • 0037010672 scopus 로고    scopus 로고
    • Inactivation and reactivation kinetics of horseradish peroxidase in phosphate buffer and buffer-dimethylformamide solutions
    • M.F. Machado, J. Saraiva, Inactivation and reactivation kinetics of horseradish peroxidase in phosphate buffer and buffer-dimethylformamide solutions, J. Mol. Catal. B-Enzym. 19-20 (2002) 451-457.
    • (2002) J. Mol. Catal. B-Enzym , vol.19-20 , pp. 451-457
    • Machado, M.F.1    Saraiva, J.2
  • 34
    • 0021471834 scopus 로고
    • A mathematical analysis of enzyme stabilization by a series-type mechanism: Influence of chemical modifiers
    • J.P. Henley, A. Sadana, A mathematical analysis of enzyme stabilization by a series-type mechanism: Influence of chemical modifiers, Biotechnol. Bioeng. 26 (1984) 959-969.
    • (1984) Biotechnol. Bioeng , vol.26 , pp. 959-969
    • Henley, J.P.1    Sadana, A.2
  • 35
    • 21444460535 scopus 로고    scopus 로고
    • Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength
    • J. Saraiva, J.C. Oliveira, A. Lemos, M. Hendrickx, Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength, Int. J. Food Sci. Technol. 31 (1996) 223-231.
    • (1996) Int. J. Food Sci. Technol , vol.31 , pp. 223-231
    • Saraiva, J.1    Oliveira, J.C.2    Lemos, A.3    Hendrickx, M.4
  • 36
    • 0041478901 scopus 로고
    • Cabbage and Brussels sprout peroxidase isoenzymes separated by isoelectric focusing
    • K.M. McLellan, D.S. Robinson, Cabbage and Brussels sprout peroxidase isoenzymes separated by isoelectric focusing, Phytochemistry, 22 (1983) 645-647.
    • (1983) Phytochemistry , vol.22 , pp. 645-647
    • McLellan, K.M.1    Robinson, D.S.2


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