A novel R-specific carbonyl reductase capable of catalyzing asymmetric reduction of prochiral ketones to enantiopure (R)-alcohols was found in a new strain Acetobacter sp. CCTCC M209061, and purified to homogeneity by three steps. A 26-fold enrichment of the enzyme with an overall yield of 0.3% was obtained. During the purification process, it was necessary to add Mn2+ ions and keep low temperature (4�C) to prevent rapid deactivation. The enzyme was mainly dependent on NADPH, and still showed catalytic activity in the presence of NADH. The optimum pH and temperature for 4'-chloroacetophenone reduction were 6.0 and 25�C. The Km values were 2.28 mM (4'-chloroacetophenone) and 0.14 mM (NADPH). Addition of EDTA led to the enzyme's deactivation, indicating that the enzyme was essentially dependent on some mental ions. Besides, the enzyme was highly active and enantioselective for the bioreduction of a wide range of other prochiral ketones.

Novel <i>R</i>-specific carbonyl reductase from <i>Acetobacter sp</i>. CCTCC M209061: Purification and characterization

245th National Meeting (2013)

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Novel R-specific carbonyl reductase from Acetobacter sp. CCTCC M209061: Purification and characterization