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

Abstract 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 instance...

Full description

Bibliographic Details
Published in:ChemBioChem
Main Authors: Mathebula, Nompumelelo P., Sheldon, Roger A., Bode, Moira L.
Other Authors: University of the Witwatersrand, Johannesburg
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2022
Subjects:
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.1002/cbic.202200435
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202200435
https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cbic.202200435
Description
Summary:Abstract 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.

Similar Items