详细信息

含环氧基团的聚合物载体合成方法的改进及其固定化青霉素酰化酶  ( SCI-EXPANDED收录)  

Improvement of the Preparation Method for Polymer Support with Epoxy Groups and Immobilization of Penicillin G Acylase

文献类型:期刊文献

中文题名:含环氧基团的聚合物载体合成方法的改进及其固定化青霉素酰化酶

英文题名:Improvement of the Preparation Method for Polymer Support with Epoxy Groups and Immobilization of Penicillin G Acylase

作者:吴东亮[1];赵巧玲[1];郭杨龙[1];王莹[1];王筠松[1];詹望成[1];卢冠忠[1]

机构:[1]华东理工大学结构可控先进功能材料及其制备教育部重点实验室,工业催化研究所,上海200237

年份:2010

卷号:31

期号:5

起止页码:586

中文期刊名:催化学报

外文期刊名:CHINESE JOURNAL OF CATALYSIS

收录:CSTPCD;;Scopus;WOS:【SCI-EXPANDED(收录号:WOS:000278399400017)】;北大核心:【北大核心2008】;CSCD:【CSCD2011_2012】;

基金:高等学校博士学科点专项科研基金(20070251016)

语种:中文

中文关键词:聚合物载体;环氧基团;青霉素酰化酶;固定化;反相悬浮聚合

外文关键词:polymer support; epoxy group; penicillin G acylase; immobilization; inverse suspension polymerization

摘要:以Span-60和Tween-20为复合分散剂,以N,N′-亚甲基双丙烯酰胺为交联剂,以甲基丙烯酸缩水甘油酯和烯丙基缩水甘油醚为功能性单体,用反相悬浮聚合技术成功制备了含环氧基团的聚合物载体,并用红外光谱和低温氮吸附对聚合物载体进行了表征.以Span-60和Tween-20为复合分散剂,替代原有的Span-60和硬脂酸钙复合分散剂,大幅度减少了后处理过程中所需的时间和溶剂用量,使固定化青霉素酰化酶的活性从215U/g提高到320U/g.与游离酶相比,该固定化酶具有较好的操作稳定性,在pH=5~11和不高于50oC的环境中具有较好的稳定性.固定化酶的水解反应动力学过程与游离酶相同,均遵循米氏反应动力学,而且活性与底物浓度密切相关.当底物浓度为6.5%时,固定化酶的活性最高,达到353U/g.
A polymer support with epoxy groups was synthesized by inverse suspension polymerization,using Span-60 and Tween-20 as the complex dispersant,N,N'-methylene-bis(acrylamide) as the crosslinking reagent,and glycidyl methacrylate and allyl glycidyl ether as reactive monomers,and it was characterized by infrared spectroscopy and nitrogen adsorption.The use of Span-60 and Tween-20 as the complex dispersant instead of Span-60 and calcium stearate greatly decreased the post-treatment time and the amount of used solvent and increased the activity of immobilized penicillin G acylase from 215 U/g up to 320 U/g.Compared with free enzyme,the immobilized penicillin G acylase had better operational stability,better stability in the pH range of 5-11,and better thermostability below 50 oC.The kinetic process of hydrolysis reaction over the immobilized penicillin G acylase obeyed Michaelis-Menten kinetics,which was the same as free enzyme.The activity of the immobilized penicillin G acylase had close relationship with the substrate concentration.When the substrate concentration was 6.5 %,the highest activity of 353 U/g was achieved.

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