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PARTIAL PURIFICATION AND CHARACTERIZATION OF POLYPHENOL OXIDASE FROM FRESH‐CUT CHINESE WATER CHESTNUT
Author(s) -
LU SHENGMIN,
TONG GANGPING,
LONG YING,
FENG HAO
Publication year - 2006
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.1745-4514.2006.00059.x
Subject(s) - polyphenol oxidase , browning , catechol , chemistry , sephadex , catechol oxidase , food science , substrate (aquarium) , yield (engineering) , chromatography , polyphenol , enzyme , botany , horticulture , biochemistry , biology , antioxidant , peroxidase , ecology , materials science , metallurgy
The characteristics of polyphenol oxidase (PPO) from Chinese water chestnut (CWC) and its potential inhibitors for browning reactions were investigated. PPO was isolated from fresh‐cut CWC and was purified on a Sephadex G‐100 column, with a yield of total activity close to 10%. The molecular weight, Michaelis constant ( K m ), substrate specificity, optimal pH and temperature of CWC PPO were examined. Kinetic studies indicated that the K m and V max values of CWC PPO for catechol were 10.32 mmol/L and 6.452 × 10 4 U/min, respectively. The optimal pH and temperature for CWC PPO was 6.5 and 40C, respectively. Among the browning inhibitors tested, 4‐hexylresorcinol, at a concentration of 0.3 mmol/L, showed the strongest inhibition (70%) against the PPO activity of CWC, followed by 3.0 mmol/L N‐acetyl‐L‐cysteine with an inhibition of 53%.