Biotechnology Letters

, Volume 17, Issue 9, pp 893–898

Isolation of a highly enantioselective epoxide hydrolase from Rhodococcus sp. NCIMB 11216

Authors

  • Martin Mischitz
    • Institute of Organic Chemistry, Graz University of Technology
  • Kurt Faber
    • Institute of Organic Chemistry, Graz University of Technology
  • Andrew Willetts
    • Department of Biological SciencesExeter University
Article

DOI: 10.1007/BF00127422

Cite this article as:
Mischitz, M., Faber, K. & Willetts, A. Biotechnol Lett (1995) 17: 893. doi:10.1007/BF00127422

Summary

Whole cells of Rhodococcus sp. NCIMB 11216 catalyze the asymmetric hydrolysis of racemic epoxides giving access to chiral epoxides and diols, which are important chiral building blocks for the synthesis of bioactive compounds. Employing a four-step purification procedure, the epoxide hydrolase responsible for the reaction was isolated and characterized to be a cofactor-independent, soluble monomeric protein of ~35kDa, exhibiting an isoelectric point of 4.7.

Copyright information

© Chapman & Hall 1995