Immobilization of catalase on chitosan and amino acid- modified chitosan beads

Abstract

Bovine liver catalase was covalently immobilized onto amino acid-modified chitosan beads. The beads were characterized with SEM, FTIR, TGA and the effects of immobilization on optimum pH and temperature, thermostability, reusability were evaluated. Immobilized catalase showed the maximal enzyme activity at pH 7.0 at 30°C. The kinetic parameters, K_m and V_max, for immobilized catalase on alanine–chitosan beads and lysine–chitosan beads were estimated to be 25.67 mM, 27 mM and 201.39 μmol H₂O₂/min, 197.50 μmol H₂O₂/min, respectively. The activity of the immobilized catalase on Ala–CB and Lys–CB retained 40% of its high initial activity after 100 times of reuse.

Keywords::

• Amino
• acid
• catalase
• chitosan
• immobilization
• modification

Declaration of interest The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.

This work was supported by Research Grants BAP 2010-106 from Celal Bayar University.