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

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ID: 178283
2011
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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.
Reference Key
piovan2011moleculesenzymatic Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Leandro Piovan;Monica D. Pasquini;Leandro H. Andrade
Journal Journal of ethnopharmacology
Year 2011
DOI
10.3390/molecules16098098
URL
http://www.mdpi.com/1420-3049/16/9/8098/
Keywords
alcohols

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