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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
引用本文: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].中国化学工程学报,2007,15(6):788-790.
作者姓名:王安明  周成  王华  沈树宝  薛建跃  欧阳平凯
作者单位:[1]College of Life Science and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210009, China [2]Department of Chemistry, Chaohu College, Chaohu 238000, China
基金项目:国家高技术研究发展计划(863计划),国家自然科学基金,江苏省自然科学基金,Scientific Research Foundation for Young Teachers in the Higher Education Institutions of Anhui Province of China,Foundation of Jiangsu Province of China for College Postgraduate Students in Inno vation Engineering 
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 fl-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:酶固定化  青霉素酰基转移酶  β-环糊精  高分子聚合理论
收稿时间:2006-12-26
修稿时间:2007-04-02

Covalent Assembly of Penicillin Acylase in Mesoporous Silica Based on Macromolecular Crowding Theory
Anming WANG, Cheng ZHOU, Hua WANG, Shubao SHEN, Jianyue XUE,Pingkai OUYANG.Covalent Assembly of Penicillin Acylase in Mesoporous Silica Based on Macromolecular Crowding Theory[J].Chinese Journal of Chemical Engineering,2007,15(6):788-790.
Authors:Anming WANG  Cheng ZHOU  Hua WANG  Shubao SHEN  Jianyue XUE  Pingkai OUYANG
Affiliation:College of Life Science and Pharmaceutical Engineering,Nanjing University of Technology,Nanjing 210009,China;Department of Chemistry,Chaohu College,Chaohu 238000,China;College of Life Science and Pharmaceutical Engineering,Nanjing University of Technology,Nanjing 210009,China;Department of Chemistry,Chaohu College,Chaohu 238000,China
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.
Keywords:enzyme immobilization  penicillin acylase  β-cyclodextrin  macromolecule crowding
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