详细信息
Comparative Studies on Enzyme Activity of Immobilized Horseradish Peroxidase in Silica Nanomaterials with Three Different Shapes and Methoxychlor Degradation of Vesicle-Like Mesoporous SiO2 as Carrier ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:Comparative Studies on Enzyme Activity of Immobilized Horseradish Peroxidase in Silica Nanomaterials with Three Different Shapes and Methoxychlor Degradation of Vesicle-Like Mesoporous SiO2 as Carrier
作者:Yang, Yuxiang[1];Zhao, Min[1];Yao, Pingping[1];Huang, Yan[1];Dai, Zuocheng[1];Yuan, Hongming[3];Ni, Chaoying[2]
机构:[1]East China Univ Sci & Technol, Chem Dept, Shanghai 200237, Peoples R China;[2]Univ Delaware, Dept Mat Sci & Engn, Newark, DE 19716 USA;[3]Jilin Univ, Coll Chem, State Key Lab Inorgan Synth & Preparat Chem, Changchun 130012, Jilin, Peoples R China
年份:2018
卷号:18
期号:4
起止页码:2971
外文期刊名:JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY
收录:;EI(收录号:20180204625831);WOS:【SCI-EXPANDED(收录号:WOS:000426050500091)】;
基金:This work was supported by the National Natural Science Foundation of China (20577010 and 20971043) and the Fundamental Research Funds from the Central University.
语种:英文
外文关键词:VSL; Mesoporous Silica; HRP; Immobilization; MXC; Degradation
摘要:In the present work, three differently shaped mesoporous silica nanoparticles, spherical nano-SiO2, tubular mesoporous SiO2 and vesicle-like mesoporous SiO2 (VSL), were prepared and used to immobilize Horse radish peroxidase (HRP), and their enzyme's activity was also evaluated. It was found that the VSL immobilized HRP displayed higher specific activity than free enzyme and other two differently shaped silica immobilized HRP. After immobilization, the thermal stability, pH tolerance resistance and storage stability on vesicle-like SiO2 were studied as well. In addition, the kinetic constants K-m and V-max for HRP were significantly altered by immobilization. The affinity for HRP towards its substrate increased (with decreasing K-m), leading to enhanced catalytic efficiency (with increased V-max). Moreover, the reusability for degradation of methoxychlor (MXC) by VSL immobilized enzyme was studied and its degradation products were detected by GC-MS and NMR analysis.
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