高等学校化学学报 ›› 1997, Vol. 18 ›› Issue (5): 786.

• 论文 • 上一篇    下一篇

微量热法研究漆酶和3,4,5-三羟基苯甲酸的反应

望天志1, 吴鼎泉1, 万洪文2, 屈松生1, 杜予民1   

  1. 1. 武汉大学化学系, 武汉, 430072;
    2. 华中师范大学化学系, 武汉, 430070
  • 收稿日期:1996-05-27 出版日期:1997-05-24 发布日期:1997-05-24
  • 通讯作者: 吴鼎泉.
  • 作者简介:望天志, 男, 28岁, 博士研究生.
  • 基金资助:

    国家自然科学基金

Studies on the Reaction Between Laccase and 3,4,5-Trihydroxybenzoic Acid by Microcalorimetry

WANG Tian-Zhi1, WU Ding-Quan1, WAN Hong-Went2, QU Song-Sheng1, DU Yu-Min1   

  1. 1. Department of Chemistry, Wuhan University, Wuhan, 430072;
    2. Department of Chemistry, Central China Normal Universityt, Wuhan, 430070
  • Received:1996-05-27 Online:1997-05-24 Published:1997-05-24

摘要: 用LKB-2107型微量热系统,在不同的温度(pH=7.4)条件下,测定了3,4,5-三羟基苯甲酸与漆酶反应的摩尔反应烙、米氏常数、反应速率常数、漆酶的活性并计算了结合能、活化自由能、活化能和活化烟等.在此基础上,应用过渡态理论,从能量变化的角度,对其催化过程进行了分析.由活化摘(△S≠T<0)得出酶-底物过渡态的结构较酶-底物复合物更为有序的结论.

关键词: 漆酶, 微量热法, 过渡态, 3, 4, 5-三羟基苯甲酸

Abstract: The reactions between laccase and 3,4,5-trihydroxybenzoic acid have been studied by LKB-2107 batch microcalorimetry system at different temperatures and pH = 7.4.The rnolar reaction enthalpy (ΔrHm), the Michaelis constant (Km), the rate constant (k2), the laccase activity (EA), the binding energy (ΔG0), the activation Gibbs free energy (ΔG≠T),the actlvation energy(Ea) and the activation entropy (ΔS≠T) have been determined.The results have been discussed from changes in free energy by using the transition state theory.The activation entropy (ΔS≠T < 0) indicated that enzyme-substrate/transition structure is bound more orderly than enzyme-substrate complex.

Key words: Laccase, Microcalorimetry, Transition state,3,4,5-Trihydroxybenzoic acid

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