食品科学

• 基础研究 • 上一篇    下一篇

没食子酸对猪胰α-淀粉酶和蛋白酶的抑制作用

秦 昱,邵元元,熊 硕,滕 杰,丰金玉,肖文军   

  1. 湖南农业大学 国家植物功能成分利用工程技术研究中心,湖南 长沙 410128
  • 出版日期:2015-02-15 发布日期:2015-02-10

Inhibitory Effect of Gallic Acid on Pancreatic α-Amylase and Trypsin

QIN Yu, SHAO Yuanyuan, XIONG Shuo, TENG Jie, FENG Jinyu, XIAO Wenjun   

  1. National Research Center of Engineering Technology for Utilization of Botanical Functional Ingredients,
    Hunan Agricultural University, Changsha 410128, China
  • Online:2015-02-15 Published:2015-02-10

摘要:

以没食子酸为材料,通过考察酶质量浓度、反应体系中底物和酶及没食子酸添加顺序、不同反应时间、不同没食子酸质量浓度对猪胰α-淀粉酶、蛋白酶的活性影响,研究没食子酸对两种酶的抑制作用。结果表明,在底物质量浓度为1 g/100 mL、体系添加顺序为酶液与抑制剂没食子酸溶液37 ℃预温5 min后加入底物溶液的条件下,没食子酸抑制猪胰α-淀粉酶活性最优条件为:α-淀粉酶质量浓度0.64 mg/mL,反应时间15 min,没食子酸对α-淀粉酶的最大抑制率为95.52%;在体系添加顺序为酶液与抑制剂没食子酸溶液40 ℃预温5 min后加入底物溶液的条件下,没食子酸抑制猪胰蛋白酶活性的最优条件为:胰蛋白酶质量浓度0.63 mg/mL,反应时间30 min,没食子酸对胰蛋白酶的最大抑制率为99.24%。没食子酸对两种酶的抑制效果均随没食子酸质量浓度的增大而增强。

关键词: 没食子酸, 猪胰&alpha, -淀粉酶, 猪胰蛋白酶, 抑制作用

Abstract:

The inhibitory effect of gallic acid on the activities of pancreatic α-amylase and trypsin was studied by varying
enzyme concentration, the sequence of adding substrate, enzyme and gallic acid in reaction systems, reaction time and gallic
acid concentration. Results showed that the maximum inhibition rate (95.52%) of pancreatic α-amylase was achieved by
prewarming the enzyme at a concentration of 0.64 mg/mL in the presence of gallic acid at 37 ℃ for 5 min before addition
of 1 g/100 mL starch and allowing the reaction to proceed for 15 min. Gallic acid exhibited the strongest inhibition on
pancreatic trypsin (by 99.24%) by prewarming their mixture at 40 ℃ for 5 min followed by addition of 1 g/100 mL casein
as the substrate and permitting the reaction to take place for 30 min. The inhibitory effect of gallic acid on both enzyme
activities was positively associated with its concentration.

Key words: gallic acid, pancreatic α-amylase, pancreatic trypsin, inhibitory effect

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