详细信息
Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:Effect of substrate (ZnO) morphology on enzyme immobilization and its catalytic activity
作者:Zhang, Yan[1];Wu, Haixia[1];Huang, Xuelei[2];Zhang, Jingyan[2];Guo, Shouwu[1]
机构:[1]Shanghai Jiao Tong Univ, Res Inst Micro Nano Sci & Technol, Natl Key Lab Micro Nano Fabricat Technol, Key Lab Thin Film & Microfabricat,Minist Educ, Shanghai 200240, Peoples R China;[2]E China Univ Sci & Technol, Sch Pharm, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
年份:2011
卷号:6
外文期刊名:NANOSCALE RESEARCH LETTERS
收录:;WOS:【SCI-EXPANDED(收录号:WOS:000293647900001)】;
基金:This study was financially supported by the National "973" Program (Nos. 2007CB936000 and 2010CB933900), the NSFC (No. 20774029 and No. 20906055) of China, the State key laboratory of bioreactor engineering (No. 2060204), and China postdoctoral science foundation (No. 20100470131).
语种:英文
摘要:In this study, zinc oxide (ZnO) nanocrystals with different morphologies were synthesized and used as substrates for enzyme immobilization. The effects of morphology of ZnO nanocrystals on enzyme immobilization and their catalytic activities were investigated. The ZnO nanocrystals were prepared through a hydrothermal procedure using tetramethylammonium hydroxide as a mineralizing agent. The control on the morphology of ZnO nanocrystals was achieved by varying the ratio of CH(3)OH to H(2)O, which were used as solvents in the hydrothermal reaction system. The surface of as-prepared ZnO nanoparticles was functionalized with amino groups using 3-aminopropyltriethoxysilane and tetraethyl orthosilicate, and the amino groups on the surface were identified and calculated by FT-IR and the Kaiser assay. Horseradish peroxidase was immobilized on as-modified ZnO nanostructures with glutaraldehyde as a crosslinker. The results showed that three-dimensional nanomultipod is more appropriate for the immobilization of enzyme used further in catalytic reaction.
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