文献类型：期刊文献

中文题名：青霉素酰化酶在含铁MCM-41介孔分子筛上的固定化研究

英文题名：Study on Immobilization of Penicillin Acylase on Mesoporous Fe-MCM-41 Molecular Sieve

作者：薛屏[1,2];卢冠忠[1];郭杨龙[1];王筠松[1];吴东方[1]

机构：[1]华东理工大学工业催化研究所;[2]宁夏大学化学与化工学院宁夏银川750021

年份：2003

卷号：66

期号：10

起止页码：681

中文期刊名：化学通报

外文期刊名：Chemistry

收录：CSTPCD;;Scopus;北大核心:【北大核心2000】；CSCD:【CSCD2011_2012】；

语种：中文

中文关键词：青霉素酰化酶;含铁MCM-41介孔分子筛;固定化;载体

外文关键词：Fe-MCM-41, Support, Penicillin acylase, Immobilization method

摘要：制备了具有长程有序结构、孔径分布狭窄的含铁MCM 4 1介孔分子筛 ,利用直接法和共价结合法将青霉素酰化酶固定在分子筛表面。结果表明 ,两种方法制备的固定化酶对青霉素G水解反应的表观活性分别为 782U g和 2 5 6U g ;经 6次连续操作使用 ,二者保持初始活性的 4 9.4 %和 81 .2 % ,后者的操作稳定性好于前者。共价结合法制备的固定化酶活性较低 ,是由于Fe MCM 4 1表面修饰后比表面积和孔径明显减小所致。
The mesoporous MCM-41 molecular sieve containing iron having well ordered long\|range structure and narrow pore size distribution was synthesized. The apparent activity of penicillin acylase immobilized on Fe-MCM-41 through direct immobilization or covalent coupling was 782U/g and 268U/g, respectively. The former remained about 49.4% of its initial activity, and the latter remained 81.2% of its initial activity after used in the consecutive hydrolysis of penicillin G for 6 times. The enzyme immobilized by covalent coupling had lower initial activity due to the decrease of the pore diameter and the specific surthce area after Fe-MCM-41 was modified.