4.7 Article

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

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 120, Issue -, Pages 896-905

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.08.097

Keywords

Immobilization; Glucose oxidase; Iron oxide; Magnetic recovery; Porosity; Synergy

Funding

  1. Russian Science Foundation [17-19-01408]
  2. Russian Foundation for Basic Research [18-08-00468, 18-38-00159]
  3. NSF [CHE-1048613]
  4. NSF MRI grant [NSF DMR 1126394]

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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 degrees 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 Bronsted 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. (C) 2018 Elsevier B.V. All rights reserved.

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