FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (23 ): 229-232.doi: 10.7506/spkx1002-6300-200923051

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Screening and Characterization of Polyphenol Oxidase Source for Protein Cross-linking

WU Jin-ju1,2，GUO Xiao-ying3，CHEN Hong-bing1,2，GAO Jin-yan1,4,*   

  1. 1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China；2. Sino-German Joint
    Research Institute, Nanchang University, Nachang 330047, China；3. Nanchang Agri-food and Safety Inspection Center, Nanchang
    330009, China；4. School of Life Science and Food Engineering, Nanchang University, Nanchang 330047, China
  • Received:2009-06-25 Online:2009-12-01 Published:2010-12-29
  • Contact: GAO Jin-yan E-mail:gjy1967@yahoo.com.cn

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Abstract:

The plants and fungus with high polyphenol oxidase (PPO) activity were selected to apply to protein cross-linking, and biochemical nature of this enzyme was characterized. PPOs from Agaricus bisporus and eggplant were observed to be the highest, 11004 U/g and 9376 U/g. The optimum temperature and pH for these two kinds of PPO were found to be 20 ℃ and 7.0, while PPO from A. bisporus showed lower heat stability than that from eggplant at high temperature. Metal ions like Zn2+, Mn2+ and Ag+ showed obvious inhibition on PPOs while Cu2+ was able to promote the PPO activity from A. bisporus (140.9%) and inhibit PPO activity from 23.4%. The Km and Vmax values of PPOs from A. bisporus and eggplant were 5.5 mmol/L and 1666.7 U, 8.75 mmol/L and 2500 U, respectively.

Key words: cross-linking, polyphenol oxidase(PPO), Agaricus bisporus, eggplant

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