文献类型：期刊文献

英文题名：Assembly of Graphene Oxide-Enzyme Conjugates through Hydrophobic Interaction

作者：Zhang, Yan[2];Zhang, Jingyan[1];Huang, Xuelei[1];Zhou, Xuejiao[2];Wu, Haixia[2];Guo, Shouwu[2]

机构：[1]E China Univ Sci & Technol, Sch Pharm, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Shanghai Jiao Tong Univ, Natl Key Lab Micro Nano Fabricat Technol, Res Inst Micro Nano Sci & Technol, Key Lab Thin Film & Microfabricat,Minist Educ, Shanghai 200240, Peoples R China

年份：2012

卷号：8

期号：1

起止页码：154

外文期刊名：SMALL

收录：;EI(收录号：20120214671231);WOS:【SCI-EXPANDED(收录号:WOS:000298788800020)】；

基金：This work was supported by the State Key Laboratory of Bioreactor Engineering (No. 2060204), 111 Project (B07023), and the National "973 Program" (2007CB936000, 2010CB933900).

语种：英文

外文关键词：enzyme adsorption; chemically reduced graphene oxide; hydrophobic interaction; horseradish peroxidase; oxalate oxidase

摘要：Biochemical and biomedical applications of graphene oxide (GO) critically rely on the interaction of biomolecules with it. It has been previously reported that the biological activity of the GOenzyme conjugate decreases due to electrostatic interaction between the enzymes and GO. Herein, the immobilization of horseradish peroxidase (HRP) and oxalate oxidase (OxOx) on chemically reduced graphene oxide (CRGO) are reported. The enzymes can be adsorbed onto CRGO directly with a tenfold higher enzyme loading than that on GO, and maximum enzyme loadings reach 1.3 and 12 mg mg-1 for HRP and OxOx, respectively. Significantly, the more CRGO is reduced, the higher the enzyme loading. The CRGOHRP conjugates also exhibit higher enzyme activity and stability than GOHRP. Excellent properties of the CRGOenzyme conjugates are attributed to hydrophobic interaction between the enzymes and the CRGO. The hydrophobic interaction mode of the CRGOenzyme conjugates can be applied to other hydrophobic proteins, and thus could dramatically improve the performance of immobilized proteins. The results indicate that CRGO is a potential substrate for efficient enzyme immobilization, and is an ideal candidate as a macromolecule carrier and biosensor.