FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (1): 161-164.doi: 10.7506/spkx1002-6630-201001038

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Enzymological Characterization of Polyphenol Oxidase from Chayote Fruits

ZHANG Fu-ping,ZHANG Xi-chun   

  1. (Department of Biology, Hanshan Normal University, Chaozhou 521041, China
  • Received:2009-04-14 Revised:2009-08-21 Online:2010-01-01 Published:2014-05-19
  • Contact: ZHANG Fu-ping E-mail:hsfpzh@126.com

Abstract:

Freshly-prepared crude polyphenol oxidase (PPO) from chayote was enzymologically characterized in the present study. Results showed that the optimal reaction pH and temperature for this enzyme were 7.5 and 30 ℃, respectively, and substrate concentration was positively correlated with enzyme activity. This enzyme could quickly catalyze the oxidation of pyrogallic acid as a substrate, but exhibited relatively low catalysis activity towards catechol, hydroquinone and resorcinol. The activity of this enzyme was inhibited by vitamin C, citric acid, sodium tetraborate, magnesium chloride and EDTA-2Na in decreasing order. With increasing concentration, there was an increase in inhibitory effects of vitamin C and citric acid against enzyme activity.

Key words: chayote fruits, polyphenol oxidase (PPO), relative activity, inhibitor

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