期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 134, 期 -, 页码 507-515出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2019.05.066
关键词
Graphene oxide; Magnetic Ni0.5Zn0.5Fe2O4@SiO2 nanocomposite; Penicillin G acylase
资金
- Jiangsu Provincial Postgraduate Scientific Practice and Innovation Project [SJCX18_0753]
Magnetic Ni0.5Zn0.5Fe2O4@SiO2 nanocomposite was prepared via the rapid combustion process, and its surface was modified to obtain amino-functionalized magnetic Ni0.5Zn0.5Fe2O4@SiO2-NH2 nanocomposite. The modified nanocomposite was loaded on graphene oxide (GO), on which penicillin G acylase (PGA) was covalently immobilized. The structure for docking was visualized between PGA and penicillin G using the PyMol program, which revealed the configuration of the active site. Selections of immobilization conditions including immobilization concentration and time of fixation, were explored. The catalytic performance of the immobilized PGA was characterized. The immobilized and free PGA had the highest activity at pH 8.0 and 45 degrees C. Compared with the activity of the free PGA, the activity of the immobilized PGA was affected less by pH and temperature. The immobilized PGA exhibited the high-effective activity and good stability. V-max and K-m of immobilized PGA were 0.8123 mol.min(-1) and 0.0399 mol.L-1, respectively. Free PGA's V-max and K-m were 0.6854 mol.min(-1) and 0.0328 mol.L-1. Immobilized PGA remained >70% in relative activity after 9 successive cycles. (C) 2019 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据