Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme

CUI Tang-bing; HAN Shuang-yan; SHU Wei; GUO Yong

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Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme

更新时间：2026-05-27

- Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme
- Vol. 23, Issue 3, Pages: 26-30(2006)
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- Online First：02 June 2006，
  
  Published：2006
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崔堂兵, 韩双艳, 舒薇, 郭勇. 豆豉纤溶酶的酶动力性质研究[J]. 广东工业大学学报, 2006, 23(3): 26-30.

CUI Tang-bing, HAN Shuang-yan, SHU Wei, et al. Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme[J]. 2006, 23(3): 26-30.
崔堂兵, 韩双艳, 舒薇, 郭勇. 豆豉纤溶酶的酶动力性质研究[J]. 广东工业大学学报, 2006, 23(3): 26-30. DOI：

CUI Tang-bing, HAN Shuang-yan, SHU Wei, et al. Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme[J]. 2006, 23(3): 26-30. DOI：

摘要

对豆豉纤溶酶(DFE)的催化动力学性质进行了研究

结果表明:酶的相对分子量为41 970

是一种新的豆豉纤溶酶;酶最适用pH为7.0

酶活力在pH7~8范围内最稳定

在pH8~10范围内相对稳定

在pH4以下降为0;最适作用温度为41℃

在37~45℃范围内

酶活性均较高

在15℃时酶的保存稳定性最好;Hg2+大大降低了酶活性

Fe3+和L i+则能显著提高酶活性;以酪蛋白为底物时

纤溶酶催化的反应受到底物的抑制.

Abstract

Catalysis kinetics characterization of douchi fibrinolytic enzyme（DFE）is studied.The results show that:the relative molecular weight is 41 970

the optimal reaction pH is pH7.0

DFE’s activity is the stablest at the pH range of 78

relatively stable at the pH range of 8-10

0 under the pH 4;the optimal reaction comperature is 41 ℃

enzyme activity is higher at the comperature range of 37-45 ℃;the stability of conservation is best at 15 ℃;Hg2+could remarkably inhibit DFE’s activity

Fe3+and Li+ could enhance it.When casein is used as a substrate

the reaction catalyzed by DFE is inhibited by the substrate.

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