Lipase catalysed kinetic resolutions of 3-aryl alkanoic acids

cbnd
Thumbnail Image
Files
RED_LipaseAV2011.pdf(1.29 MB)
Accepted Version
Date
2011-02-02
Authors
Deasy, Rebecca E.
Brossat, Maude
Moody, Thomas S.
Maguire, Anita R.
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Published Version
10.1016/j.tetasy.2010.12.019
Research Projects
Organizational Units
Journal Issue
Abstract
Hydrolase catalysed kinetic resolutions leading to a series of 3-aryl alkanoic acids (≥94% ee) is described. Hydrolysis of the ethyl esters with a series of hydrolases was undertaken to identify biocatalysts that yield the corresponding acids with excellent enantiopurity in each case. Steric and electronic effects on the efficiency and enantioselectivity of the biocatalytic transformation was also explored.
Description
Keywords
3-aryl , Alkanoic acid , Hydrolase catalysed , Enantiopurity
Citation
DEASY, R. E., BROSSAT, M., MOODY, T. S. & MAGUIRE, A. R. 2011. Lipase catalysed kinetic resolutions of 3-aryl alkanoic acids. Tetrahedron: Asymmetry, 22, 47-61. doi: 10.1016/j.tetasy.2010.12.019
Link to publisher’s version
http://www.sciencedirect.com/science/article/pii/S0957416610008608
URI
https://hdl.handle.net/10468/575
Collections
Chemistry - Journal Articles
Analytical & Biological Chemistry Research Facility - Journal Articles
Pharmacy - Journal Articles
Copyright
© 2011 Elsevier Ltd. All rights reserved. NOTICE: this is the author’s version of a work that was accepted for publication in Tetrahedron: Asymmetry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Tetrahedron: Asymmetry, [22, 1,(02/02/2011)] 10.1016/j.tetasy.2010.12.019