Reductive enzymatic dynamic kinetic resolution affording 115 g/L (S)-2-phenylpropanol.

Background: Published biocatalytic routes for accessing enantiopure 2-phenylpropanol using oxidoreductases afforded maximal product titers of only 80 mM. Enzyme deactivation was identified as the major limitation and was attributed to adduct formation of the aldehyde substrate with amino acid residues of the reductase.

Results: A single point mutant of Candida tenuis xylose reductase (CtXR D51A) with very high catalytic efficiency (43·10 s M) for (S)-2-phenylpropanal was found.