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Synfacts 2007(11): 1203-1203
DOI: 10.1055/s-2007-991243
DOI: 10.1055/s-2007-991243
Organo- and Biocatalysis
© Georg Thieme Verlag Stuttgart · New York
Arylpropionic Alcohols via Enzyme-Mediated Dynamic Kinetic Resolution
D. Giacomini*, P. Galletti, A. Quintavalla, G. Gucciardo, F. Paradisi
University of Bologna, Italy and University College Dublin, Ireland
Further Information
Publication History
Publication Date:
23 October 2007 (online)
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.