期刊
BIOCHEMICAL ENGINEERING JOURNAL
卷 69, 期 -, 页码 28-31出版社
ELSEVIER
DOI: 10.1016/j.bej.2012.07.025
关键词
Immobilized enzymes; Affinity; Glucose; Graphene oxide; Glucose oxidase; Kinetic parameters
资金
- National Nature Science Foundation of China [21006020]
- Natural Science Foundation of Hebei Province [B2010000035, B2011202095]
- Science and Technology Research Key Project of Higher School in Hebei Province [ZD2010118]
- Application Basic Research Plan Key Basic Research Project of Hebei Province [11965150D]
The oriented immobilization of glucose oxidase (GOD) on a selective support composed of graphene oxide (GO) and concanavalin A (Con A) was prepared in this study. Specially, the amino groups of Con A were covalently attached to the carboxyl groups of pre-activated GO, and then GOD was oriented immobilized on the GO-Con A conjugate via strong biospecific affinity between the sugar residues of GOD and Con A. Compared with free GOD and randomly immobilized GOD (GO-GOD), the high-affinity of Con A and GOD endowed the oriented immobilized GOD (GO-Con A-GOD) with a wider pH stability range, a better thermal stability, a longer-term storage stability and a higher resistance ability toward the denaturing agents. The Michaelis constant (K-m) of GO-Con A-GOD was very close to that of free GOD. Hopefully, the GO-Con A-GOD may be further integrated into functional bioelectrodes for biosensor applications. (C) 2012 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