食品科学 ›› 2011, Vol. 32 ›› Issue (17): 269-272.doi: 10.7506/spkx1002-6630-201117056

• 生物工程 • 上一篇    下一篇

菜豆豆荚多酚氧化酶酶学特性研究

李雯妮,赵秀文,田维娜*,曹建康,姜微波   

  1. 中国农业大学食品科学与营养工程学院
  • 发布日期:2011-08-30
  • 基金资助:
    国家“863”计划项目(2008AA100803);中央高校基本科研业务费专项基金项目(2010JS075)

Enzymatic Properties of Polyphenol Oxidase from Kidney Bean Pods

LI Wen-ni,ZHAO Xiu-wen,TIAN Wei-na*,CAO Jian-kang,JIANG Wei-bo   

  1. (College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China)
  • Published:2011-08-30

摘要: 目的:了解菜豆豆荚多酚氧化酶(polyphenol Oxidase,PPO)的酶学特性。方法:采用聚丙烯酰氨凝胶电泳(polyacrylamide gel electrophoresis,PAGE)法对菜豆豆荚PPO 的最适pH值、最适温度、底物专一性、激活剂及抑制剂进行研究。结果:菜豆豆荚PPO 最适pH值为6.0;最适温度为30℃,且温度为30℃时,该酶具有较强的热稳定性,80℃可使其完全失活;该酶对不同酚类物质表现出不同的底物专一性,邻苯二酚为该酶的最适底物;抗坏血酸、L-半胱氨酸、β-巯基乙醇、甘氨酸均能抑制该酶的活性,而1.0mmol/L β-巯基乙醇或抗坏血酸可完全抑制其活性;氯化铜、尿素对该酶均有激活作用,其中氯化铜的激活作用明显。结论:高温、偏碱性环境、β-巯基乙醇或抗坏血酸处理均可有效抑制菜豆豆荚PPO 活性。

关键词: 多酚氧化酶, 酶学特性, 聚丙烯酰胺凝胶电泳, 菜豆豆荚

Abstract: Objective: To explore enzymatic properties of polyphenol oxidase (PPO) from kidney bean pods (Phaseolus vulgaris L. cv. Shuangqing). Methods: The optimal pH, temperature, substrate specificity and inhibitors of PPO were evaluated by polyacrylamide gel electrophoresis (PAGE). Results: The optima pH for PPO activity was 6.0. The PPO was relatively stable at 30 ℃ and inactivated at 80 ℃. Catechol was the optimal substrate for the enzyme. Its activity was inhibited by ascorbic acid, β-mercaptoethanol, glycine or L-cysteine. Moreover, the PPO activity was inhibited completely by 1.0 mmol/L β-mercaptoethanol or ascorbic acid; however, it was activated by copper dichloride and carbamide. Conclusion: High temperature, high pH and β-mercaptoethanol or ascorbic acid can inhibit the activity of the PPO enzyme.

Key words: polyphenol oxidase, polyphenol property, polyacrylamide gel electrophoresis (PAGE) , kidney bean pod

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