PGA在含环氧活性基的多孔高聚物载体上的固定化及修饰  

Immobilization of Penicillin G Acylase on the Porous Polymer with Oxirane Groups

作　　者：高克亮[1] 颜淑玮[1] 许伟钦[1] 魏东芝[1] 

机构地区：[1]华东理工大学生物反应器工程国家重点实验室鲁华生物技术研究所,上海200237

出　　处：《华东理工大学学报（自然科学版）》2007年第6期798-802,共5页Journal of East China University of Science and Technology

基　　金：上海市重点学科建设项目资助(B505)

摘　　要：研究了青霉素G酰化酶（PGA）在含环氧活性基的多孔高聚物载体上的固定化及修饰，优化固定化条件为1mol/L，pH8.0的磷酸钾缓冲体系，每克载体（湿重）投酶量为500～550U，30℃下150r/min固定化36～48h，得到的固定化酶表观酶活为每克载体（湿重）177U，表观酶活回收率35％。固定化酶经巯基乙醇修饰后提高了热稳定性。固定化酶水解青霉素G的最适pH为9.0，最适温度为47℃在pH4～9，40℃以下稳定。固定化酶的各项性能均优于游离酶。Penicillin G acy mercaptoethanol after immobil ase （PGA） was immobilized on a kind of oxirane carrier and modified by zation, which improved thermal stabilization of immobilized PGA（IPA）. The optimum condition of immobilization reaction was 1 mol/L phosphate potassium buffer of pH 8.0, addition enzyme on wel carrier between 500～550 U/g, and shaking gently （150 r/min） for 36～48 h at 30℃. The apparent activity of the immobilized enzyme on wet carrier prepared under these conditions was 177 U/g and the apparent activity recovery was 35% The optimal pH and temperature of immobilized PGA were 9.0 and 47℃ for hydrolysis of penicillin G respectively. The immobilized enzyme was stable in the range of pH 4～9 and at the temperature below 40℃. Compared with free PGA, IPA was eximious on most enzymatic characterizations.

关 键 词：青霉素G酰化酶 共价固定化 化学修饰 环氧树脂 

分 类 号：Q814.2[生物学—生物工程]