The results of a reduction of a wide range of ketones using 31 commercially available isolated ketoreductases (KREDs) are presented. All enzymes accepted a wide substrate range. The stereo selectivity of each enzyme was measured for the reduction of benzoyl-hydroxyacetone and ethyl-3-oxobutanoate, and in each case, enzymes which produce enantiomerically pure (R)- and (S)-alcohols were found. The preparative scale reactions were investigated using two ketones with different hydrophobicities (benzoyl-hydroxyacetone and alpha-tetralone) and using enzymes with varying specific activities for their reduction. Regardless of the hydrophobicity of the substrate, high titers of ketone (0.75-1.4 M) were reduced in high yield using catalytic amounts of enzyme (1-7% g/g relative to substrate) and cofactor (0.1-0.2% equiv. relative to ketone) within 4-24 h. The cofactor was efficiently regenerated in situ via the oxidation of glucose by glucose dehydrogenase, an enzyme that has also been cloned and over-expressed. These results show that isolated ketoreductases can be quickly and easily screened against target ketones, and the reactions can be scaled to produce preparative amounts of chiral alcohols. Ketoreductase enzymes should become a standard addition to the organic chemists toolbox of asymmetric catalysts for stereoselective ketone reduction. (c) 2005 Elsevier Ltd. All rights reserved.