A 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 degrees C and its co-factor was NADPH. This novel ADH efficiently mediated the reduction of 3-oxo esters with a high degree of ste-reoselectivity, 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.