Abstract
AbstractA yeast alcohol dehydrogenase (ADH) has been purified up to a purification factor value of 21,731‐fold from Kluyveromyces marxianus CBS 6556. The purification procedure consisted of two chromatographic steps (DEAE‐anion exchange and affinity chromatography). The optimal pH was 7, its optimal temperature was 40 °C and its co‐factor was NADPH. This novel ADH efficiently mediated the reduction of 3‐oxo esters with a high degree of stereoselectivity, providing chiral alcohols having the (S) absolute configuration at the newly formed stereogenic centre by delivering the hydride from the re‐face of the prochiral carbonyl compounds.
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