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

Int J Biol Macromol. 2018 Dec;120(Pt A):896-905. doi: 10.1016/j.ijbiomac.2018.08.097. Epub 2018 Aug 30.

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.

Keywords: Glucose oxidase; Immobilization; Iron oxide; Magnetic recovery; Porosity; Synergy.

MeSH terms

  • Aluminum Oxide / chemistry
  • Catalysis
  • Enzymes / chemistry*
  • Enzymes, Immobilized / chemistry*
  • Glucose / chemistry*
  • Glucose Oxidase / chemistry*
  • Hydrogen-Ion Concentration
  • Magnetic Phenomena
  • Oxidation-Reduction
  • Silicon Dioxide / chemistry

Substances

  • Enzymes
  • Enzymes, Immobilized
  • Silicon Dioxide
  • Glucose Oxidase
  • Glucose
  • Aluminum Oxide