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Purification and characterization of a recombinantCaulobacter crescentus epoxide hydrolase

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Abstract

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.

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Correspondence to Chayong Choi.

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Hwang, S., Hyun, H., Lee, B. et al. Purification and characterization of a recombinantCaulobacter crescentus epoxide hydrolase. Biotechnol. Bioprocess Eng. 11, 282–287 (2006). https://doi.org/10.1007/BF03026241

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  • DOI: https://doi.org/10.1007/BF03026241

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