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...
Published in: | ChemBioChem |
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Main Authors: | , , |
Other Authors: | |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2022
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Subjects: | |
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 |
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. |
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