Improvement of the stability and activity of immobilized glucose oxidase on modified iron oxide magnetic nanoparticles

被引：49

作者：

Abbasi, Mahboube ^{[1
]}

Amiri, Razieh ^{[1
]}

Bordbar, Abdol-Kalegh ^{[1
]}

Ranjbakhsh, Elnaz ^{[1
]}

Khosropour, Ahmad-Reza ^{[1
]}

机构：

[1] Univ Isfahan, Dept Chem, Esfahan 8174673441, Iran

来源：

APPLIED SURFACE SCIENCE | 2016年 / 364卷

关键词：

Enzymatic activity; Glucose oxidase; Immobilization; Iron oxide magnetic nanoparticles; Stability; ENZYME IMMOBILIZATION; GOLD NANOPARTICLES; LIPASE; WATER;

D O I：

10.1016/j.apsusc.2015.12.120

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Immobilized proteins and enzymes are widely investigated in the medical field as well as the food and environmental fields. In this study, glucose oxidase (GOX) was covalently immobilized on the surface of modified iron oxide magnetic nanoparticles (MIMNs) to produce a bioconjugate complex. Transmission electron microscopy (TEM) and X-ray diffraction (XRD) were used to the size, shape and structure characterization of the MIMNs. Binding of GOX to these MIMNs was confirmed by using FT-IR spectroscopy. The stability of the immobilized and free enzyme at different temperature and pH values was investigated by measuring the enzymatic activity. These studies reveal that the enzyme's stability is enhanced by immobilization. Further experiments showed that the storage stability of the enzyme is improved upon binding to the MIMNs. The results of kinetic measurements suggest that the effect of the immobilization process on substrate and product diffusion is small. Such bioconjugates can be considered as a catalytic nanodevice for accelerating the glucose oxidation reaction for biotechnological purposes. (C) 2016 Published by Elsevier B.V.

引用

页码：752 / 757

页数：6

共 38 条

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