Catalytic activities of fungal oxidases in hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate-based microemulsion

Colloids Surf B Biointerfaces. 2008 Oct 1;66(1):146-9. doi: 10.1016/j.colsurfb.2008.05.016. Epub 2008 Jul 7.

Abstract

For hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF(6)]), an H(2)O-in-[BMIM][PF(6)] microemulsion could be formed in the presence of nonionic surfactant Triton X-100 (TX-100). In such a medium, both lignin peroxidase (LiP) and laccase could express their catalytic activity with the optimum molar ratio of H(2)O to TX-100 at 8.0 for LiP and >20 for laccase, and the optimum pH values at 3.2 for LiP and 4.2 for laccase, respectively. As compared with pure or water saturated [BMIM][PF(6)], in which the two oxidases had negligible catalytic activity due to the strong inactivating effect of [BMIM][PF(6)] on both enzymes, the use of the [BMIM][PF(6)]-based microemulsion had some advantages. Not only the catalytic activities of both fungal oxidases greatly enhanced, but also the apparent viscosity of the medium decreased.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Emulsions
  • Hydrophobic and Hydrophilic Interactions
  • Imidazoles / chemistry*
  • Laccase / metabolism*
  • Peroxidases / isolation & purification
  • Peroxidases / metabolism*
  • Phanerochaete / enzymology
  • Viscosity

Substances

  • 1-butyl-3-methylimidazolium hexafluorophosphate
  • Emulsions
  • Imidazoles
  • Laccase
  • Peroxidases
  • lignin peroxidase