Leandro Piovan, Monica D. Pasquini, L. Andrade
Sep 1, 2011
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0
Influential Citations
3
Citations
Journal
Molecules
Abstract
The enzymatic kinetic resolution of tert-butyl 2-(1-hydroxyethyl)phenylcarbamate via lipase-catalyzed transesterification reaction was studied. We investigated several reaction conditions and the carbamate was resolved by Candida antarctica lipase B (CAL-B), leading to the optically pure (R)- and (S)-enantiomers. The enzymatic process showed excellent enantioselectivity (E > 200). (R)- and (S)-tert-butyl 2-(1-hydroxyethyl)phenylcarbamate were easily transformed into the corresponding (R)- and (S)-1-(2-aminophenyl)ethanols.