FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (1): 172-176.doi: 10.7506/spkx1002-6630-201001040

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Biochemical Characteristics of Phenoloxidase from Portunus trituberculatus

ZHENG Dan1,DUAN Qing-yuan2,*,ZHU Li-hua1,ZHONG Hui-ying1,YANG Jia-feng1,WANG Jie1   

  1. 1. Ningbo Inspection and Monitor Centre for Product Quality and Fishery Environment, Ningbo 315012, China ;
    2. Ningbo Academy of Ocean and Fishery, Ningbo 315012, China
  • Received:2009-03-17 Online:2010-01-01 Published:2014-05-19
  • Contact: ZHENG Dan1 E-mail:sustzhd@yahoo.com.cn

Abstract:

Crude phenoloxidase (PO) was extracted from Portunus trituberculatus and characterized biochemically. This enzyme exhibited an optimal pH of 8.2 and temperature of 55 ℃ for catalyzing the oxidation of pyrocatechol as a substrate. Optimal enzyme stability was observed in the ranges of pH 7.8-8.4 and 25-40 ℃. Browning reaction catalyzed by this enzyme obeyed the Michaelis-Menten equation. The values of Km and Vmax at 30 ℃ and pH 7.2 were calculated to be 0.531 mol/L and 0.049 A530nm/min, respectively. Twelve inhibitors tested all had a certain inhibitory effect against this enzyme, among which phytic acid was the strongest inhibitor, followed in turn by sodium metabisulfite, L-cysteine, oxalic acid and ascorbic acid.

Key words: Portunus trituberculatus, phenoloxidase, melanin

CLC Number: