Immobilization of glucose oxidase on Fe3O4/SiO2 magnetic nanoparticles

Biotechnol Lett. 2010 Jun;32(6):817-21. doi: 10.1007/s10529-010-0217-9. Epub 2010 Feb 14.

Abstract

Glucose oxidase (GOD) was covalently immobilized onto Fe(3)O(4)/SiO(2) magnetic nanoparticles (FSMNs) using glutaraldehyde (GA). Optimal immobilization was at pH 6 with 3-aminopropyltriethoxysilane at 2% (v/v), GA at 3% (v/v) and 0.143 g GOD per g carrier. The activity of immobilized GOD was 4,570 U/g at pH 7 and 50 degrees C. The immobilized GOD retained 80% of its initial activity after 6 h at 45 degrees C while free enzyme retained only 20% activity. The immobilized GOD maintained 60% of its initial activity after 6 cycles of repeated use and retained 75% of its initial activity after 1 month at 4 degrees C whereas free enzymes retained 62% of its activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biotechnology / methods*
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Ferrosoferric Oxide
  • Glucose Oxidase / chemistry
  • Glucose Oxidase / metabolism*
  • Hydrogen-Ion Concentration
  • Nanoparticles / chemistry*
  • Protein Binding
  • Silicon Dioxide
  • Temperature

Substances

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