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 overalll activity. The optimal reaction temperature and pH were determined to be $37^{circ}C$ 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.