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Molecules. 2011 Sep 20;16(9):8098-109. doi: 10.3390/molecules16098098.

Enzymatic kinetic resolution of tert-butyl 2-(1-hydroxyethyl)phenylcarbamate, a key intermediate to chiral organoselenanes and organotelluranes.

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1
Institute of Chemistry, University of São Paulo, Av. Prof. Lineu Prestes 748, SP 05508-900, São Paulo, Brazil.

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.

PMID:
21934647
DOI:
10.3390/molecules16098098
[Indexed for MEDLINE]
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