机构地区: 华南理工大学生物科学与工程学院
出 处: 《广东工业大学学报》 2006年第3期26-30,共5页
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41970,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;Hg^2+大大降低了酶活性,Fe^3+和Li^+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. 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 7 -8 ,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 ℃;Hg^2+ could remarkably inhibit DFE's activity ,Fe^3+ and Li ^+ could enhance it. When casein is used as a substrate,the reaction catalyzed by DFE is inhibited by the substrate.