Large-scale ruthenium- and enzyme-catalyzed dynamic kinetic resolution of (rac)-1-phenylethanol.

ABSTRACT: The scale-up of the ruthenium- and enzyme-catalyzed dynamic kinetic resolution (DKR) of (rac)-1-phenylethanol (2) is addressed. The immobilized lipase Candida antarctica lipase B (CALB) was employed for the resolution, which shows high enantioselectivity in the transesterification. The ruthenium catalyst used, (eta 5-C5Ph5)RuCl(CO)2 1, was shown to possess very high reactivity in the "in situ" redox racemization of 1-phenylethanol (2) in the presence of the immobilized enzyme, and could be used in 0.05 mol% with high efficiency. Commercially available isopropenyl acetate was employed as acylating agent in the lipase-catalyzed transesterifications, which makes the purification of the product very easy. In a successful large-scale DKR of 2, with 0.05 mol% of 1, (R)-1-phenylethanol acetate (3

SUBMITTER: Bogar K 

PROVIDER: S-EPMC2200671 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature