Immobilization of Thermoanaerobium brockii alcohol dehydrogenase on SBA-15

Bioprocess Biosyst Eng. 2011 Feb;34(2):247-51. doi: 10.1007/s00449-010-0480-0. Epub 2010 Nov 3.

Abstract

The activity of Thermoanaerobium brockii alcohol dehydrogenase (TBADH) adsorbed on mesoporous silica SBA-15 was compared with that of the free enzyme in water and in biphasic system (water phase up to 50% v/v water). TBADH was active at a water concentration ≥10% v/v. In the reduction reaction of sulcatone to sulcatol carried out in biphasic systems, the yield obtained with SBA-15-adsorbed TBADH was up to 5.5-fold higher than that with the free enzyme, which suggests a higher stability of the immobilized enzyme toward the organic solvent. The nature of the organic solvent substantially influenced the degree of conversion that, for example, was 7.4% in toluene and 31.6% in petroleum ether.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Dehydrogenase / chemistry*
  • Alkanes / chemistry
  • Bacterial Proteins / chemistry*
  • Enzymes, Immobilized / chemistry*
  • Gram-Positive Endospore-Forming Rods / enzymology*
  • Octanols / chemistry
  • Oxidation-Reduction
  • Silicon Dioxide / chemistry*
  • Toluene / chemistry

Substances

  • Alkanes
  • Bacterial Proteins
  • Enzymes, Immobilized
  • Octanols
  • SBA-15
  • sulcatol
  • Toluene
  • Silicon Dioxide
  • Alcohol Dehydrogenase
  • naphtha