Lipase catalysed kinetic resolutions of 3-aryl alkanoic acids

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Lipase catalysed kinetic resolutions of 3-aryl alkanoic acids

Deasy, Rebecca E.; Brossat, Maude; Moody, Thomas S.; Maguire, Anita R.
Date: 2011-02-02
Copyright: 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
Related: http://www.sciencedirect.com/science/article/pii/S0957416610008608
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
Published Version: 10.1016/j.tetasy.2010.12.019

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.

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