Stabilization of Nocardia EH1 epoxide hydrolase by immobilization

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 nonio...

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Bibliographic Details
Published in:Biotechnology letters 1998-04, Vol.20 (4), p.373-377
Main Authors: KROUTIL, W, ORRU, R. V. A, FABER, K
Format: Article
Language:English
Subjects:
Binding sites
Biological and medical sciences
Biotechnology
Cellulose
Fundamental and applied biological sciences. Psychology
Immobilization of enzymes and other molecules
Immobilization techniques
Ions
Methods. Procedures. Technologies
Nocardia
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Summary: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[PUBLICATION ABSTRACT]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005379314104