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

• 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

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.