豆豉纤溶酶的酶动力性质研究

广东工业大学学报 ›› 2006, Vol. 23 ›› Issue (3): 26-30.

豆豉纤溶酶的酶动力性质研究

华南理工大学生物科学与工程学院；华南农业大学测试中心；华南理工大学生物科学与工程学院广东广州510640；广东广州510640；

出版日期:2006-06-02 发布日期:2006-06-02

Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme

(1.School of Bioscience and Bioengineering,South China University of Technology,Guangzhou 510640,China;2.Instrumental Analysis and Research Center,South China Agricultural University,Guangzhou 510640,China)

Online:2006-06-02 Published:2006-06-02

摘要/Abstract

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.

关键词: 豆豉纤溶酶；酶动力学；研究；

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.

Key words: douchi fibrinolytic enzyme； catalysis kinetics； study；

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~1,HAN Shuang-yan~1,SHU Wei~2,GUO Yong~1. Study on Catalysis Kinetics of Douchi Fibrinolytic Enzyme[J]. Journal of Guangdong University of Technology, 2006, 23(3): 26-30.

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