FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (21): 275-278.doi: 10.7506/spkx1002-6630-201021062

• Bioengineering • Previous Articles     Next Articles

Enzymatic Properties of Polyphenol Oxidase from Kuerle Pear

ZHU Lu-ying1,WU Wei-wei1,2,SUN Jie1,DU Ting-ting1   

  1. 1. College of Life Sciences, Ludong University, Yantai 264025, China;
    2. College of Animal Science and Technology, Agricultural University of Hebei, Baoding 071001, China
  • Received:2010-03-15 Online:2010-11-15 Published:2010-12-29
  • Contact: ZHU Lu-ying E-mail:lyzhu@126.com

Abstract:

Enzymological characterization of the polyphenol oxidase (PPO) from Kuerle pear towards catechol as a substrate was conducted using spectrophotometry method. The results showed that the optimal pH and temperature for this enzyme was 5.7 and 42 ℃. High temperature treatment could inhibit PPO activity. The kinetics of PPO reaction was in accord with the Michaelis-Menten equation, with Km and Vmax values of 0.152 mol/L and 169.49 U/min, respectively. Ascorbic acid exhibited stronger inhibition effect on PPO activity than citric acid, NaCl and EDTA-2Na.

Key words: Kuerle pear, polyphenol oxidase, enzymatic properties, inhibition effect

CLC Number: