Immobilized glucose oxidase on magnetic silica and alumina: Beyond magnetic separation

Abstract

Here we report immobilization of glucose oxidase (GOx) on magnetic silica (Fe3O4-SiO2) and alumina (Fe3O4-Al2O3) functionalized with amino groups using glutaraldehyde as a linker. Magnetic support based biocatalysts demonstrate high catalytic activity in d-glucose oxidation to D-gluconic acid at pH 5–7.5 and temperature of 30–50 °C with the best activities of 95% and 91% for magnetic silica and alumina, respectively. A comparison of magnetic and non-magnetic alumina and silica shows a significant enhancement of the relative catalytic activity for magnetic supports, while the silica based biocatalysts show a higher activity than the biocatalysts based on alumina. A noticeably higher activity of GOx immobilized on magnetic supports is explained by synergy of the GOx inherent activity and enzyme-like activity of iron oxide nanoparticles, while the enhancement with silica based catalysts is most likely due to a larger pore size and stronger Brønsted acid sites. Excellent relative activity of Fe3O4-SiO2-GOx (95% of native GOx) in a tolerant pH and temperature range as well as high stability in a repeated use (6% relative activity loss after five catalytic cycles) makes this catalyst promising for practical applications.

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Table of Contents

Description

This record is for a(n) postprint of an article published in International Journal of Biological Macromolecules on 2018-12-01; the version of record is available at https://doi.org/10.1016/j.ijbiomac.2018.08.097.

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Citation

Jaquish, Rigel, et al. "Immobilized glucose oxidase on magnetic silica and alumina: Beyond magnetic separation." International Journal of Biological Macromolecules, vol. 120, pp. 896-905, 2018-12-01, https://doi.org/10.1016/j.ijbiomac.2018.08.097.

Journal

International Journal of Biological Macromolecules

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This work may be protected by copyright unless otherwise stated.

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