Biocatalytic resolution of glycidyl aryl ethers by Trichosporon loubierii : cell/substrate ratio influences the optical purity of (R) - epoxides

Biotechnol Lett. 2004 Aug;26(15):1217-21. doi: 10.1023/B:BILE.0000036598.35494.de.

Abstract

Glycidyl aryl ethers were resolved by using lyophilized cells of Trichosporon loubierii ECU1040 having epoxide hydrolase activity. The activity and enantioselectivity depended on the structure of the aryl group. Different cell/substrate ratios also influenced the optical purity of remaining substrate. An additional stability test of the whole-cell enzyme suggests that rapid deactivation of the epoxide hydrolase was the potential reason. (R)-Epoxides were prepared in gram amounts with optical purity of 87% - 99% ee.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Cell Count
  • Cell Culture Techniques / methods*
  • Cell Proliferation
  • Enzyme Activation
  • Enzyme Stability
  • Epoxide Hydrolases / analysis
  • Epoxide Hydrolases / chemistry*
  • Epoxide Hydrolases / metabolism*
  • Epoxy Compounds / isolation & purification
  • Epoxy Compounds / metabolism*
  • Kinetics
  • Stereoisomerism
  • Trichosporon / enzymology*
  • Trichosporon / growth & development*

Substances

  • Epoxy Compounds
  • glycidyl ethers
  • Epoxide Hydrolases