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ENZYMATIC DEGRADATION OF ANTHOCYANINS: THE ROLE OF SWEET CHERRY POLYPHENOL OXIDASE
Author(s) -
Pifferi P. G.,
Cultrera R.
Publication year - 1974
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1974.tb17980.x
Subject(s) - anthocyanin , polyphenol oxidase , chemistry , chlorogenic acid , phenols , ascorbic acid , polyphenol , cyanidin , pigment , phenol , enzyme , tyrosinase , catechol oxidase , biochemistry , cellulose , food science , organic chemistry , antioxidant , peroxidase
An enzymatic system capable of degrading cyanidin‐3‐glucoside in the absence of phenols is present in the skin of sweet cherries; contrarily, the pulp homogenate degraded the anthocyanin only in the presence of phenols. The degradation of this pigment as a function of pH was studied for two polyphenol oxidases isolated from the fruit pulp on DEAE‐cellulose with chlorogenic acid, D (+) catechine and pyrocatechol substrates. The decoloration was influenced by the anthocyanin structure at different pH and by the nature of the quinone obtained by enzymatic oxidation. The anhydrobase appeared to be the form of the anthocyanin most susceptible to oxidation. The degradation occurred according to the oxidation kinetics of the phenol substrate and was inhibited by ascorbic acid, indicating that the quinone's degradation of the anthocyanin occurred by a consecutive‐type mechanism.