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Lipase-Catalysed Enzymatic Kinetic Resolution of Aromatic Morita-Baylis-Hillman Derivatives by Hydrolysis and
Nompumelelo P Mathebula1, Roger A Sheldon1,2, Moira L Bode1
1Molecular Sciences Institute School of Chemistry, University of the Witwatersrand Private Bag X3, PO WITS, Johannesburg, 2050, South Africa.
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.
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