Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification

Acylated Morita‐Baylis‐Hillman (MBH) adducts were synthesised and subjected to enzymatic kinetic resolution (EKR) by hydrolysis employing various lipase enzymes: from P. fluorescens, P. cepacia (PCL), C. antarctica A (CAL−A), C. antarctica B (CAL−B) and Novozyme 435. In a number of instances enantio...

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Bibliographic Details
Published in:ChemBioChem
Main Authors: Mathebula, Nompumelelo P., Sheldon, Roger A., Bode, Moira L.
Format: Text
Language:English
Published: John Wiley and Sons Inc. 2022
Subjects:
Research Articles
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9828654/
http://www.ncbi.nlm.nih.gov/pubmed/36049111
https://doi.org/10.1002/cbic.202200435
Description
Summary:Acylated Morita‐Baylis‐Hillman (MBH) adducts were synthesised and subjected to enzymatic kinetic resolution (EKR) by hydrolysis employing various lipase enzymes: from P. fluorescens, P. cepacia (PCL), C. antarctica A (CAL−A), C. antarctica B (CAL−B) and Novozyme 435. In a number of instances enantiopure Morita‐Baylis‐Hillman acetates or butyrates and their corresponding hydrolysed MBH adducts were obtained with ee values of >90 %, at ca. 50 % conversion, corresponding to enantiomeric ratio (E) values of >200. Enantioselective transesterification reactions on MBH adducts was achieved using acyl anhydrides in THF or the greener organic solvent 2‐MeTHF in the presence of CAL−A. This is the first report of successful lipase‐catalysed EKR of aromatic MBH adducts by transesterification in organic medium.

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