基于大分子拥挤原理的介孔二氧化硅中青霉素酰化酶的共价组装

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基于大分子拥挤原理的介孔二氧化硅中青霉素酰化酶的共价组装

王安明^1,2; 周成¹; 王华¹; 沈树宝¹; 薛建跃²; 欧阳平凯¹

¹ College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, China
² Department of Chemistry, Chaohu College, Chaohu 238000, China

收稿日期:2006-12-26 修回日期:1900-01-01 出版日期:2007-12-28 发布日期:2007-12-28
通讯作者: 王安明

Covalent assembly of penicillin acylase in mesoporous silica based on macromolecular crowding theory

WANG Anming^a,b; ZHOU Cheng^a; WANG Hua^a; SHEN Shubao^a; XUE Jianyue^b; OUYANG Pingkai^a

¹ College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, China
² Department of Chemistry, Chaohu College, Chaohu 238000, China

Received:2006-12-26 Revised:1900-01-01 Online:2007-12-28 Published:2007-12-28
Contact: WANG Anming

摘要/Abstract

摘要： To improve the covalent immobilization of penicillin acylase (PA), macromolecular crowding theory was applied to its immobilization. Influence of mass ratio of enzyme to the silica, as well as, activation time with glutaraldehyde on the activity of assembled PA, was studied. In the mesopores, the effect of β-cyclodextrin (β-CD) on the immobilization of the enzyme was also investigated. It was remarkable that the coupled yield and relative activity reached 99.5% and 92.3%, respectively, when penicillin acylase assembled covalently in the mesopores. The results here indicate that mimicked macromolecule crowding could significantly ameliorate the performance of covalently immobilized PA.

关键词: enzyme immobilization;penicillin acylase;β-cyclodextrin;macromolecule crowding

Abstract: To improve the covalent immobilization of penicillin acylase (PA), macromolecular crowding theory was applied to its immobilization. Influence of mass ratio of enzyme to the silica, as well as, activation time with glutaraldehyde on the activity of assembled PA, was studied. In the mesopores, the effect of β-cyclodextrin (β-CD) on the immobilization of the enzyme was also investigated. It was remarkable that the coupled yield and relative activity reached 99.5% and 92.3%, respectively, when penicillin acylase assembled covalently in the mesopores. The results here indicate that mimicked macromolecule crowding could significantly ameliorate the performance of covalently immobilized PA.

Key words: enzyme immobilization, penicillin acylase, β-cyclodextrin, macromolecule crowding

王安明, 周成, 王华, 沈树宝, 薛建跃, 欧阳平凯. 基于大分子拥挤原理的介孔二氧化硅中青霉素酰化酶的共价组装[J]. CIESC Journal.

WANG Anming a,b , ZHOU Cheng a , WANG Hua a , SHEN Shubao a , XUE Jianyue b , OUYANG Pingkai a . Covalent assembly of penicillin acylase in mesoporous silica based on macromolecular crowding theory[J]. .

参考文献

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基于大分子拥挤原理的介孔二氧化硅中青霉素酰化酶的共价组装

Covalent assembly of penicillin acylase in mesoporous silica based on macromolecular crowding theory

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