Enantioselective biocatalytic conversions of epoxides

This thesis describes the biocatalyic scope and limitations of an epoxide hydrolase and a haloalcohol dehalogenase. These enzymes, obtained from Agrobucterium radiobacter AD1, were tested for their suitability to prepare optically pure epoxides and derivatives thereof. These compounds can be used for the synthesis of various biologically active agents such as pharmaceuticals. The gram-negative bacterium A. rudiobacter AD1 was isolated from polluted freshwater sediment. Its epoxide hydrolase (EchA) and haloalcohol dehalogenase (HheC) are involved in the degradation of epichlorohydrin and dichloropropanols, enabling the organism to grow on these compounds. The 34 kD epoxide hydrolase was purified and the corresponding gene was cloned by means of PCR. The recombinant EchA can be produced at up to 40% of the total protein content in Escherichia coli, enabling the isolation of 200 to 300 mg of pure protein from a one-liter culture. This makes the enzyme available in sufficient quantities for applications in (synthetic) organic chemistry. In 1997, it was the first microbial epoxide hydrolase gene to be cloned. Until then, all conversions with microbial epoxide hydrolases were perfomred with whole cell suspensions or small quantities of (partially) purified enzyme

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