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,...

Full description

Saved in:
Bibliographic Details
Published inBiotechnology and bioprocess engineering Vol. 11; no. 4; pp. 282 - 287
Main Authors Hwang, Seungha (Pohang University of Science and Technology, Pohang, Republic of Korea), Hyun, H.J. (Seoul National University, Seoul, Republic of Korea), Lee, B.J. (Seoul National University, Seoul, Republic of Korea), Park, Y.S. (Pohang University of Science and Technology, Pohang, Republic of Korea), Lee, E.Y. (Kyungsung University, Busan, Republic of Korea), Choi, C.Y. (Seoul National University, Seoul, Republic of Korea), E-mail: choicy@snu.ac.kr
Format Journal Article
LanguageEnglish
Published 한국생물공학회 01.08.2006
Subjects
Online AccessGet full text
ISSN1226-8372
1976-3816
DOI10.1007/BF03026241

Cover

More Information
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.
Bibliography:E21
2007001391
G704-000785.2006.11.4.001
ISSN:1226-8372
1976-3816
DOI:10.1007/BF03026241