Journal
BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
Volume 11, Issue 4, Pages 282-287Publisher
KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
DOI: 10.1007/BF03026241
Keywords
chiral styrene oxide; chiral indene oxide; Caulobacter crescentus; epoxide hydrolase; enzyme purification
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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 degrees C 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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