论文部分内容阅读
从一株海洋假单胞菌中分离制备出一种具有纤溶活性的酶 ,对其酶学性质进行实验研究结果显示 :该酶的分子量是 2 1k D,等电点是 7.4～ 7.5 ;最适作用 p H是 8.0 ,最适作用温度是 5 0℃。该酶具有降解苯甲酰 - L -精氨酸乙酯盐酸盐 (BAEE)的活性 ,酶的动力学分析表明 :Km =0 .87mmol/ L,Vmax=1.80× 10 -3 mmol/ L s-1。
An enzyme with fibrinolytic activity was isolated from a marine Pseudomonas spp. and the enzymatic properties of the enzyme were studied. The results showed that the molecular weight of the enzyme was 21 kD and the isoelectric point was 7.4-7.5; The suitable effect p H is 8.0 and the optimum temperature is 50°C. The enzyme has the activity of degrading benzoyl-L-arginine ethyl ester hydrochloride (BAEE). Kinetic analysis of the enzyme showed that: Km = 0.87 mmol/L, Vmax = 1.80 × 10 -3 mmol/L s -1.