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Biotechnology Letters

, Volume 20, Issue 4, pp 373–377 | Cite as

Stabilization of Nocardia EH1 epoxide hydrolase by immobilization

  • Wolfgang Kroutil
  • Romano V. A. Orru
  • Kurt Faber
Article

Abstract

A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. This biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonionic detergent Triton X-100 during the immobilization further enhanced the stability as indicated by a dramatic shift in the temperature optimum from 35 to 45°C. The stabilized immobilized biocatalyst could be successfully employed in repeated batch reactions (residual activity of 55% after five cycles), which was not the case for whole cell reactions (residual activity ≤10 %). © Rapid Science Ltd. 1998

Keywords

Enzyme Organic Chemistry Immobilization Epoxide Hydrolase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Kluwer Academic Publishers 1998

Authors and Affiliations

  • Wolfgang Kroutil
    • 1
  • Romano V. A. Orru
    • 1
  • Kurt Faber
    • 1
  1. 1.Institute of Organic ChemistryGraz University of TechnologyStremayrgasse GrazAustria

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