Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes

Biotechnol Lett. 2009 Aug;31(8):1269-72. doi: 10.1007/s10529-009-0009-2. Epub 2009 Apr 29.

Abstract

Chloroperoxidase (CPO) from Caldariomyces fumago was optimally covalently immobilized on chitosan membranes pretreated with 0.8 M glutaraldehyde at pH 3.5 to give 3.18 mg CPO g(-1) support. Using monochlorodimedone (MCD) as assay substrate, the immobilized-CPO retained 40% activity at 50 degrees C after 40 min whereas free CPO retained only 0.02%. The residual activity for immobilized-CPO was 99 and 58% compared with 68 and 43% for free CPO in the presence of 1.5 M urea and 300 microM H(2)O(2), respectively, after 20 h.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ascomycota / enzymology*
  • Chitosan / metabolism*
  • Chloride Peroxidase / chemistry
  • Chloride Peroxidase / isolation & purification
  • Chloride Peroxidase / metabolism*
  • Cyclohexanones / metabolism
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Hot Temperature
  • Membranes / enzymology*
  • Time Factors

Substances

  • Cyclohexanones
  • Enzymes, Immobilized
  • chlorodimedone
  • Chitosan
  • Chloride Peroxidase