食品科学 ›› 2009, Vol. 30 ›› Issue (21 ): 166-171.doi: 10.7506/spkx1002-6300-200921039

• 生物工程 • 上一篇    下一篇

胰蛋白酶有限酶解米渣蛋白的机理及动力学模型研究

李 湘1,2,彭地纬1,2,熊 华1,2,*,赵 强1,2,李 薇1,2   

  1. 1.南昌大学 食品科学与技术国家重点实验室 2. 南昌大学生命科学与食品工程学院
  • 收稿日期:2009-06-30 出版日期:2009-11-01 发布日期:2010-12-29
  • 通讯作者: 熊 华1,2,*, E-mail:huaxiong100@yahoo.com.cn
  • 基金资助:

    “十一五”国家科技支撑计划项目(2006BAD27B00);食品科学与技术国家重点实验室目标导向资助项目(SKLF-MB-200809);食品科学与技术国家重点实验室自由探索资助项目(SKLF-TS-200818);教育部“长江学者和创新团队发展计划”项目(IRT0540)

Mechanism and Kinetic Model for Limited Trypsin Digestion of Protein in Rice Dregs

LI Xiang1,2,PENG Di-wei1,2,XIONG Hua1,2,*,ZHAO Qiang1,2,LI Wei1,2   

  1. 1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China;
    2. College of Life Science and Food Engineering, Nanchang University, Nanchang 330047, China
  • Received:2009-06-30 Online:2009-11-01 Published:2010-12-29
  • Contact: XIONG Hua1,2,*, E-mail:huaxiong100@yahoo.com.cn

摘要:

运用实验研究结合数学推导的方法,采用胰蛋白酶在温度53℃、pH 7.6 条件下对酶解米渣蛋白的动力学机制进行研究。结果表明:在反应过程中底物存在着促进反应进行和抑制酶活性的双重作用,酶催化的水解速率随水解进程呈指数下降;并由实验数据推导出描述胰蛋白酶催化水解米渣蛋白的动力学方程及胰蛋白酶的失活常数,验证结果表明动力学模型与实验结果非常吻合。通过对酶与底物浓度之比、反应时间的调节可有效控制水解作用的程度,从而为利用米渣酶法制备米蛋白肽的产业化实践提供指导。

关键词: 米渣, 胰蛋白酶, 有限酶解, 动力学模型

Abstract:

Mechanisms and kinetic models of enzymatic hydrolysis of protein in rice dregs by trypsin at pH 7.6 and 53 ℃ were investigated using the combined method of experimental analysis and mathematic deduction. Results indicated that the overall rate of hydrolysis decreased exponentially during the hydrolysis process due to dual functions of the substrate for accelerating and inhibiting enzymatic activity. Based on experimental data, a kinetic model equation was deduced to demonstrate trypsin hydrolysis of protein in rice dregs and inactivation constant of trypsin. Therefore, hydrolysis degree can be effectively controlled through the adjustment of trypsin/substrate ratio, and reaction time, which can provide guidance to peptide industrialization from rice dregs by means of enzymatic technology.

Key words: rice dregs, trypsin, limited-hydrolysis, kinetic model

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