RESUMO

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.

Assuntos

Candida/enzimologia , Proteínas Fúngicas/química , Lipase/química , Compostos Organometálicos/síntese química , Compostos Organosselênicos/síntese química , Fenilcarbamatos/síntese química , Telúrio/química , Biocatálise , Esterificação , Cinética , Espectroscopia de Ressonância Magnética , Estrutura Molecular , Oxirredução , Fenilcarbamatos/química , Solventes , Estereoisomerismo