• Bulletin of the Korean Chemical Society
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• v.22 no.11
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• pp.1261-1263
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• 2001

• Bulletin of the Korean Chemical Society
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• v.20 no.12
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• pp.1437-1440
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• 1999

Ozonolysis reactions of indene 5 in the presence of carbonyl compounds 6 provided the corresponding indenemonoozonide 9 and cross-ozonides 10a-c and 11a-c. Further reactions of ozonides 10 and 11 with the independently prepared carbonyl oxide 13 gave diozonides of structure 14a-c and 15a-c.

• Biotechnology and Bioprocess Engineering:BBE
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• v.11 no.4
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• pp.282-287
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• 2006

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.

• Journal of Microbiology and Biotechnology
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• v.16 no.1
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• pp.32-36
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• 2006

The genome sequences from several microbes have led to the discovery of numerous open reading frames of unknown functionality. The putative bacterial epoxide hydrolase (EH) genes selected from the genome databases were examined for their activities toward various epoxides. Among the nine open reading frames (ORFs) from four microbial species, the ORF from Caulobacter crescentus showed an epoxide hydrolase activity. The kinetic resolution, using C. crescentus EH (CCEH) of the aryl epoxides such as styrene oxide, could be performed more efficiently than short aliphatic epoxides. The resolution of racemic indene oxide, which could previously be resolved only by fungal epoxide hydrolases, was effectively accomplished by CCEH.