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

• 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

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