Purification and Characterization of a Recombinant Caulobacter crescentus Epoxide Hydrolase
A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH protein was purified 7.3-fold with a 22.9% yield in overall activity. The optimal reaction temperature and pH were determined to be 37℃ and pH 8.0,...
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Published in | Biotechnology and bioprocess engineering Vol. 11; no. 4; pp. 282 - 287 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
한국생물공학회
01.08.2006
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Subjects | |
Online Access | Get full text |
ISSN | 1226-8372 1976-3816 |
DOI | 10.1007/BF03026241 |
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Summary: | A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH protein was purified 7.3-fold with a 22.9% yield in overall activity. The optimal reaction temperature and pH were determined to be 37℃ and pH 8.0, respectively. The addition of 10% (v/v) dimethylsulfoxide as a cosolvent improved the enantioselectivity of CCEH for a batch kinetic resolution of racemic indene oxide. |
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Bibliography: | E21 2007001391 G704-000785.2006.11.4.001 |
ISSN: | 1226-8372 1976-3816 |
DOI: | 10.1007/BF03026241 |