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Browning in processed yams: peroxidase or polyphenol oxidase?
Author(s) -
Chilaka Ferdinand C,
Eze Sabinus,
Anyadiegwu Clement,
Uvere Peter O
Publication year - 2002
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1119
Subject(s) - peroxidase , polyphenol oxidase , chemistry , browning , catechol oxidase , biochemistry , polyphenol , oxidase test , enzyme , antioxidant
Polyphenol oxidase and peroxidase were purified from white yam ( Dioscorea rotundata ) using DEAE‐cellulose ionexchange chromatography. Thermoinactivation curves for polyphenol oxidase showed monophasic kinetics, while those for peroxidase were biphasic. Urea partially stabilised peroxidase against irreversible thermoinactivation, but did not do so in the case of polyphenol oxidase. Only peroxidase was capable of regenerating activity after thermoinactivation. The results showed that thermoinactivation of peroxidase was mainly due to conformational changes, while that of polyphenol oxidase was probably due to covalent damage. Peroxidase reactivation might play an important role in the browning of processed yam. © 2002 Society of Chemical Industry