Arylpropionic Alcohols via Enzyme-Mediated Dynamic Kinetic Resolution

Significance

The authors report their preliminary studies on the reduction of two 2-arylpropionic aldehydes to enantioenriched alcohols via a dynamic kinetic resolution. The enzyme catalyst is commercially available horse liver alcohol dehydrogenase (HLADH), with NADH as a cofactor. Since the enzyme regenerates its cofactor in the presence of ethanol, substoichiometric amounts of NADH are sufficient. It was found that organic co-solvents tetrahydrofurane and acetonitrile, which increase the solubility of the starting material, are tolerated in up to 10 vol% with respect to the buffer solution. With a change in the protocol, almost pure hexane (up to 99 vol%) can also be tolerated as solvent.