文献类型：期刊文献

英文题名：Synthesis and properties of the hydrophilic copolymer support containing oxirane for immobilized penicillin acylase

作者：Xue, P; Lu, GZ; Guo, YL; Wang, YS

机构：[1]E China Univ Sci & Technol, Res Inst Ind Catalysis, Shanghai 200237, Peoples R China;[2]Ningxia Univ, Sch Chem & Chem Engn, Yinchuan, Peoples R China

年份：2004

卷号：25

期号：2

起止页码：361

外文期刊名：CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000189187400043)】；

语种：英文

外文关键词：oxirane; hydrophilic support; inverse suspension polymerization; penicillin acylase; immobilization

摘要：\Oxirane groups can react with the amino groups of enzyme under mild conditions so that the enzyme molecules are immobilized on the copolymer support containing oxirane. A series of macroporous hydrophilic copolymers(GNM) containing oxirane were synthesized by inverse suspension polymerization with glycidyl methacrylate (GMA) as the reactive monomer, N-vinyl-2-pyrrolidone (NVP) as the hydrophilic comonomer, N,N'-methylene-bis-acrylamide(MBAA) as the crosslinking agent, and methanol and water as the porogenic agent and used as the support for the immobilization of penicillin G acylase (PA). The effects of the amount of the crosslinking agent on the structure properties and the apparent activity of immobilized enzyme were investigated. The specific surface area of, GNM copolymer increased, its average pore diameter and pore volume decreased, and swelling degree in water increased and then decreased with increasing the amount of the crosslinking agent. The apparent activity of 625 U/g (dry weight) was obtained when the enzyme immobilized on GNM polymer [m(NVP)/m(GMA)=1/5, w(MABB)=40%] with a mean pore diameter of 16.5 nm, an oxirane group content of 0.906 mmol/g and swelling degree of 203% in water. The optimal pH value and temperature of the hydrolysis of penicillin G over the immobilized enzyme was 8.0 and 50 degreesC, respectively. The immobilized enzyme was kept at 4 degreesC for 40 d, the change of the activity was not observed. The apparent activity of the immobilized enzyme reached a relatively steady value(about 601 U/g) after the immobilized enzyme was used for the hydrolysis of penicillin G for 3 times at 37 degreesC. It was used continuously and repeatedly for 12 times, the activity was hardly changed.