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. (author), Sheldon, R.A. (author), Bode, Moira L. (author)
Format: Article in Journal/Newspaper
Language:English
Published: 2022
Subjects:
enzymatic kinetic resolution
lipases
molecular modelling
Morita-Baylis-Hillman
Mosher derivatives
PCL
Antarc*
Antarctica
Online Access:http://resolver.tudelft.nl/uuid:756f3c13-e52c-42c2-a423-6ca2ee9666bf
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. BT/Biocatalysis

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