Immobilization and kinetics of catalase onto magnesium silicate

Tukel S. S. , Alptekin O.

PROCESS BIOCHEMISTRY, vol.39, no.12, pp.2149-2155, 2004 (Peer-Reviewed Journal) identifier identifier

  • Publication Type: Article / Article
  • Volume: 39 Issue: 12
  • Publication Date: 2004
  • Doi Number: 10.1016/j.procbio.2003.11.010
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.2149-2155
  • Keywords: catalase, magnesium silicate, covalent immobilization, glutaraldehyde, 3-aminopropionic acid, HYDROGEN-PEROXIDE, ENZYME ELECTRODE, BIOSENSOR, ADSORPTION, FILM, MEMBRANES


Bovine liver catalase was immobilized covalently with glutaraldehyde, or glutaraldehyde + 3-aminopropionic acid as a spacer, onto magnesium silicate. The coupling time was determined as 2 h for immobilization. The pH and temperature optima as well as the changes in the kinetics (K-m, V-max, E-a) of the immobilized catalase was observed and discussed. Immobilized catalase preparations showed higher storage stabilities than free catalase. The half-life of free catalase, catalase immobilized via glutaraldehyde and catalase immobilized via glutaraldehyde + spacer were calculated as 2, 55 and 10 days at room temperature and 4, 85 and 107 days at 5 degreesC, respectively. The operational stability of the catalase immobilized via glutaraldehyde was higher than the catalase immobilized via glutaraldehyde + spacer. The remaining activity of the catalase immobilized via glutaraldehyde was about 90% and that of the catalase immobilized via glutaraldeyde + spacer was about 30% after 20 cycles of batch operation. (C) 2003 Elsevier Ltd. All rights reserved.