文献类型：期刊文献

英文题名：Influence of preparation methods of copolymer supports containing oxirane groups on activity of immobilized penicillin acylase

作者：Xue, P; Lu, GZ; Guo, Y; 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, Ningxia 750021, Peoples R China

年份：2003

卷号：24

期号：10

起止页码：733

外文期刊名：CHINESE JOURNAL OF CATALYSIS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000186595800005)】；

语种：英文

外文关键词：oxirane group; copolymer support; immobilized penicillin acylase

摘要：The immobilized penicillin acylase has played an important role in the manufacture of semi-synthetic antibiotics. Much effort is being made to develop new types of carriers to improve the catalytic efficiency of the enzyme and reduce the cost of the supports. Oxirane groups of copolymer supports can couple to amino groups of enzymes under mild conditions so that the enzyme molecules can be immobilized on the surface of the supports. In this work, the immobilization of penicillin acylase on a copolymer support containing oxirane groups is reported. The macroporous beads of the copolymer support containing oxirane groups was synthesized by two methods with glycidyl methacrylate as the reactive monomer and N, N'-methylene-bis-acrylamide as the crosslinking agent. The support structure, specific surface area, and pore size distribution were characterized by Fourier transform infrared spectroscopy, scanning electron microscope, and N-2 adsorption. The results show that the effect of the preparation method on the properties of the copolymer is very great. The GM1 (60) copolymer, which was prepared using paraffin oil as the main polymerization medium and aqueous methanol as the pore-forming agent, has higher specific surface area, larger pore diameter, and better swelling capacity in water. The GM2(60) copolymer, which was prepared in a mixed solvent of n-heptane and using tetrachloroethylene as the suspending medium and formamide as the pore-generating agent, gives a lower capacity to couple enzyme. The activity of GM1 (60)-immobilized penicillin acylase and GM2 (60) -immobilized penicillin acylase is 537 and 426 U/g, respectively. The former decreases to 487 U/g and the latter decreases to 378 U/g after the immobilized enzymes are used for the consecutive hydrolysis of penicillin G at 37 degreesC for 10 times (10 min each time). Evidently, the GM1(60) copolymer is superior to GM2(60) as the support for immobilization of penicillin acylase. The GM1 (60) copolymer has higher capacity to couple penicillin acylase and the enzyme immobilized on GM1 (60) keeps higher activity during the operation than that on GM2(60).