Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability

被引：143
作者：
Li, Dongxiang
He, Qiang
Cui, Yue
Duan, Li
Li, Junbai [1 ]
机构：
[1] Chinese Acad Sci, Inst Chem, BNLMS, Key Lab Colloid & Interface Sci, Beijing 100080, Peoples R China
[2] Max Planck Inst Colloids & Interfaces, D-14476 Golm, Germany
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 355卷 / 02期
基金：
中国国家自然科学基金;
关键词：
immobilization; glucose oxidase; gold nanoparticles; bioconjugate; enzyme activity; SURFACE MODIFICATION; COVALENT ATTACHMENT; STABILITY; DNA; MONOLAYERS; PROTEINS; SENSOR; ESTER; TIME;
D O I：
10.1016/j.bbrc.2007.01.183
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
immobilized proteins and enzymes were widely investigated in medical field as well as in food and environmental fields. In this paper, glucose oxidase (GOD) monolayer was covalently immobilized on the surface of gold nanoparticles (AuNPs) to fabricate bioconjugate complex. The citrate-stabilized AuNPs were first functionalized by a carboxyl-terminated alkanethiol and the terminal carboxyl groups were subsequently bonded with side-chain amino groups of protein surface through EDC/NHS coupling reaction. The enzyme activity assays of the obtained bioconjugates display an enhanced thermostability and similar pH-dependence behavior in contrast with that of free enzyme. Such GOD/AuNPs bioconjugates can be considered as a catalytic nanodevice to construct nanoreactor based on glucose oxidation reaction for biotechnological purpose. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码：488 / 493
页数：6
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