Enzymatic Kinetic Resolution of tert-Butyl 2-(1-Hydroxyethyl)phenylcarbamate, A Key Intermediate to Chiral Organoselenanes and Organotelluranes

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...

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Bibliographic Details
Published in:Molecules
Main Authors: Piovan, Leandro, Pasquini, Monica D., Andrade, Leandro H.
Format: Text
Language:English
Published: MDPI 2011
Subjects:
Article
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264364/
http://www.ncbi.nlm.nih.gov/pubmed/21934647
https://doi.org/10.3390/molecules16098098
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Summary: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.

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