Purification and characterization of a recombinantCaulobacter crescentus epoxide hydrolase
ACaulobacter crescentus epoxide hydrolase (CCEH) from a recombinantEscherichia 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°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.
Keywordschiral styrene oxide chiral indene oxide Caulobacter crescentus epoxid hydrolase enzyme purification
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