Construction of Fe-aminoclay-glucose Oxidase Nanocomposite Catalyst and Its Multi-enzyme Cascade Analysis

被引:4
作者
Li, Liu [1 ]
Sun, Shiyong [1 ]
Lv, Rui [1 ]
Golubev, Yevgeny Aleksandrovich [2 ]
Wang, Ke [1 ]
Dong, Faqin [1 ]
Duan, Tao [3 ]
Kotova, Olga Borisovna [2 ]
Kotova, Elena Leonidovna [4 ]
机构
[1] Southwest Univ Sci & Technol, Sch Environm & Resource, Mianyang 621010, Sichuan, Peoples R China
[2] RAS, Ural Branch, Komi Sci Ctr, Yuskins Inst Geol, Syktyvkar 167982, Russia
[3] Southwest Univ Sci & Technol, Sch Natl Def Sci & Technol, Mianyang 621010, Sichuan, Peoples R China
[4] St Petersburg Min State Univ, St Petersburg 199106, Russia
来源
CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE | 2021年 / 42卷 / 03期
基金
俄罗斯基础研究基金会; 俄罗斯科学基金会; 中国国家自然科学基金;
关键词
Fe-aminoclay; Glucose oxidase; Immobilized enzyme; Cascade reaction; PEROXIDASE-LIKE ACTIVITY; MAGNETIC NANOPARTICLES; COLORIMETRIC DETECTION; MESOPOROUS SILICA; IMMOBILIZATION; PRECIPITATION; NANOMATERIALS; ADSORPTION; STABILITY; NANOZYMES;
D O I
10.7503/cjcu20200635
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Glucose oxidase (GO(x)) and Fe-aminoclay (FeAC) were combined to construct a mimic multi-enzyme system (FeAC-GO(x)) for cascade reaction. FeAC exhibit peroxidase-like activity which can catalyze H2O2 generated by GOx and trigger color reaction. The obtained FeAC-GO(x) was characterized by scanning electron microscope (SEM), X-ray diffraction (XRD), and fourier transform infrared spectroscopy (FTIR). The enzymatic kinetics, catalytic stability and reusability were evaluated. As a result, the immobilization efficiency of GO(x) could reach to 76.4%, and FeAC-GO(x) exhibited excellent cascade catalysis activity. Compared with the free enzyme, FeAC not only possessed a strong tolerance toward temperature and pH, but also presented excellent reusability. The catalytic activity of reused FeAC barely changed after six repetitions. This strategy may lay the foundation to the development of a new glucose biosensor, and provide a novel approach to design multi-enzyme cascade system.
引用
收藏
页码:803 / 810
页数:8
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