Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification
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 enantio...
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ftpubmed:oai:pubmedcentral.nih.gov:9828654 2023-05-15T13:40:01+02:00 Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification Mathebula, Nompumelelo P. Sheldon, Roger A. Bode, Moira L. 2022-09-29 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9828654/ http://www.ncbi.nlm.nih.gov/pubmed/36049111 https://doi.org/10.1002/cbic.202200435 en eng John Wiley and Sons Inc. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9828654/ http://www.ncbi.nlm.nih.gov/pubmed/36049111 http://dx.doi.org/10.1002/cbic.202200435 © 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. CC-BY-NC Chembiochem Research Articles Text 2022 ftpubmed https://doi.org/10.1002/cbic.202200435 2023-01-15T01:56:04Z 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. Text Antarc* Antarctica PubMed Central (PMC) ChemBioChem 23 21 |
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Research Articles |
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Research Articles Mathebula, Nompumelelo P. Sheldon, Roger A. Bode, Moira L. Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification |
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Research Articles |
description |
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. |
format |
Text |
author |
Mathebula, Nompumelelo P. Sheldon, Roger A. Bode, Moira L. |
author_facet |
Mathebula, Nompumelelo P. Sheldon, Roger A. Bode, Moira L. |
author_sort |
Mathebula, Nompumelelo P. |
title |
Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification |
title_short |
Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification |
title_full |
Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification |
title_fullStr |
Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification |
title_full_unstemmed |
Lipase‐Catalysed Enzymatic Kinetic Resolution of Aromatic Morita‐Baylis‐Hillman Derivatives by Hydrolysis and Transesterification |
title_sort |
lipase‐catalysed enzymatic kinetic resolution of aromatic morita‐baylis‐hillman derivatives by hydrolysis and transesterification |
publisher |
John Wiley and Sons Inc. |
publishDate |
2022 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9828654/ http://www.ncbi.nlm.nih.gov/pubmed/36049111 https://doi.org/10.1002/cbic.202200435 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Chembiochem |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9828654/ http://www.ncbi.nlm.nih.gov/pubmed/36049111 http://dx.doi.org/10.1002/cbic.202200435 |
op_rights |
© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
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CC-BY-NC |
op_doi |
https://doi.org/10.1002/cbic.202200435 |
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ChemBioChem |
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23 |
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21 |
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1766127017108963328 |