Abstract
The substrate range of a novel recombinant ( S)-alcohol dehydrogenase from Rhodococcus erythropolis is described. In addition, an enzyme-compatible biphasic reaction medium for the asymmetric biocatalytic reduction of ketones with in situ-cofactor regeneration has been developed. Thus, reductions of poorly water soluble ketones in the presence of the alcohol dehydrogenase from R. erythropolis and a formate dehydrogenase from Candida boidinii can be carried out at higher substrate concentrations of 10–200 mM. The resulting ( S)-alcohols were formed with moderate to good conversion rates, and with up to >99% ee.
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