Molecules 2011, 16(9), 8098-8109; https://doi.org/10.3390/molecules16098098
Enzymatic Kinetic Resolution of tert-Butyl 2-(1-Hydroxyethyl)phenylcarbamate, A Key Intermediate to Chiral Organoselenanes and Organotelluranes
Institute of Chemistry, University of São Paulo, Av. Prof. Lineu Prestes 748, SP 05508-900, São Paulo, Brazil
*
Author to whom correspondence should be addressed.
Received: 19 August 2011 / Revised: 14 September 2011 / Accepted: 15 September 2011 / Published: 20 September 2011
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions)
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. View Full-TextKeywords:
alcohols; carbamates; lipases; kinetic resolution; enatiopure
▼
Figures
Graphical abstract
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
Share & Cite This Article
MDPI and ACS Style
Piovan, L.; Pasquini, M.D.; Andrade, L.H. Enzymatic Kinetic Resolution of tert-Butyl 2-(1-Hydroxyethyl)phenylcarbamate, A Key Intermediate to Chiral Organoselenanes and Organotelluranes. Molecules 2011, 16, 8098-8109.
Related Articles
Article Metrics
Comments
[Return to top]
Molecules
EISSN 1420-3049
Published by MDPI AG, Basel, Switzerland
RSS
E-Mail Table of Contents Alert