摘要
将巨大芽孢杆菌胞外青霉素酰化酶通过共价键连接到醋酸纤维素载体上,制成的固定化青霉素酰化酶的表观活力达2000 u/g左右(PDAB 法)。水解10%(W/V)的青霉素 G 钾盐溶液,使用30批,保留活力70%以上。6-氨基青霉烷酸(6-APA)总收率平均达88.37%。固定化青霉素酰化酶水解青霉素 G 的最适 pH 为9.95,最适温度为55℃,表观米氏常数为1.093×10^(-2)mol/L,在 pH 5.8—10.7,温度45℃以下酶的活力稳定。
The extracellular penicillin acylase from Bacillus megaterium was immobilized by coup-ling on cellulose acetate fibres.The apparent activity of the immobilized penicillin acylase wasabout 2000μ/g(by PDAB method).It was used to hydrolyze 10% penicillin G solution in 0.05mol/L phosphate buffer pH8.0.The remained activity was over 70% after operating 30 times,andthe average yield of 6-APA was 88.37%.The properties of immobilized penicillin acyllase were studied.The optimal pH and tempe-rature for hydrolytic reaction of penicillin G was pH 9.95 and 55℃ respectively.The immobi-lized enzyme was stable in the pH range of 5.8—10.7,and at temprature below 45℃.The ap-parent Michaelis constant(Ka)for the penicillin G was 1.093×10^(-2)mol/L.
出处
《微生物学报》
CAS
CSCD
北大核心
1992年第3期212-217,共6页
Acta Microbiologica Sinica
基金
本课题为“七五”攻关项目
关键词
青霉素酰化酶
固定化酶
Penicillin acylase
Immobilized enzyme