Immobilization of chloroperoxidase on mesoporous materials for the oxidation of 4,6-dimethyldibenzothiophene, a recalcitrant organic sulfur compound present in petroleum fractions

Biotechnol Lett. 2008 Jan;30(1):173-9. doi: 10.1007/s10529-007-9512-5. Epub 2007 Sep 18.

Abstract

The catalytic potential of chloroperoxidase (CPO) immobilized on mesoporous materials was evaluated for the oxidation of 4,6-dimethyldibenzothiophene in water/acetonitrile mixtures. Two different types of materials were used for the immobilization: a metal containing Al-MCM-41 material with a pore size of 26 A and SBA-16 materials with three different pore sizes: 40, 90 and 117 A. The SBA-16 40 A did not retain any CPO. The nature and the pore size of the material affected the catalytic activity of the enzyme as well as its stability. Compared to the free enzyme, the thermal stability of CPO at 45 degrees C was two and three times higher than when immobilized on Al-MCM-41 and SBA-16 90 A, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ascomycota / enzymology*
  • Chloride Peroxidase / chemistry*
  • Enzyme Activation
  • Enzymes, Immobilized / chemistry
  • Organic Chemicals / chemistry
  • Oxidation-Reduction
  • Porosity
  • Sulfur Compounds / chemistry
  • Thiophenes / chemistry*

Substances

  • 4,6-dimethyldibenzothiophene
  • Enzymes, Immobilized
  • Organic Chemicals
  • Sulfur Compounds
  • Thiophenes
  • Chloride Peroxidase