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PARTIAL CHARACTERIZATION OF A PEPTIDE FROM HONEY THAT INHIBITS MUSHROOM POLYPHENOL OXIDASE
Author(s) -
ATES SELMA,
PEKYARDIMCI SULE,
COKMUS CUMHUR
Publication year - 2001
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2001.tb00729.x
Subject(s) - polyphenol oxidase , mushroom , catechol , chemistry , sephadex , catechol oxidase , polyphenol , food science , oxidase test , peptide , enzyme , biochemistry , browning , chromatography , antioxidant , peroxidase
Mushroom polyphenol oxidase (PPO) was inhibited by one type of honey, in a model system. Honey was a noncompetitive inhibitor of PPO catalyzed oxidation of catechol. The Anhenius activation energy (Ea) of thermal inactivation of mushroom PPO differed in the presence and absence of honey. The Ea value in the presence of honey was 27.71 kJ/mol; whereas, Ea of the control was 83.14 kJ/rnol. Thus, the temperature coefficient of PPO inactivation was lower in the presence of honey. Characterization of the inhibitor was carried out by gel electrophoresis (SDS‐PAGE and NativePAGE). An inhibitory peptide fraction was obtained after native PAGE. The molecular weight was determined to be 0.6 kDa by Sephadex G‐15 column chromatography.