Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols
Dynamic kinetic resolution (DKR) is one of the most attractive methods for enantioselective synthesis. In the reported studies, lipase B from Candida antarctica (CALB) immobilized on siliceous mesoporous cellular foams (MCF) functionalized with different hydrophobic groups, and two ruthenium complex...
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ftmdpi:oai:mdpi.com:/2073-4344/11/4/518/ 2023-08-20T04:02:25+02:00 Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols Dominika Stradomska Monika Heba Aleksandra Czernek Nikodem Kuźnik Danuta Gillner Katarzyna Maresz Wojciech Pudło Andrzej Jarzębski Katarzyna Szymańska 2021-04-20 application/pdf https://doi.org/10.3390/catal11040518 EN eng Multidisciplinary Digital Publishing Institute Biocatalysis https://dx.doi.org/10.3390/catal11040518 https://creativecommons.org/licenses/by/4.0/ Catalysts; Volume 11; Issue 4; Pages: 518 chiral secondary alcohols resolution of enantiomers dynamic kinetic resolution DKR synthesis of enantiomers bicatalytic tandem Text 2021 ftmdpi https://doi.org/10.3390/catal11040518 2023-08-01T01:32:37Z Dynamic kinetic resolution (DKR) is one of the most attractive methods for enantioselective synthesis. In the reported studies, lipase B from Candida antarctica (CALB) immobilized on siliceous mesoporous cellular foams (MCF) functionalized with different hydrophobic groups, and two ruthenium complexes with substituted cyclopentadienyl ligands were investigated as catalysts for the chemoenzymatic DKR of (rac)-1-phenylethanol, using Novozym 435 as a benchmark biocatalyst. Studies on the (rac)-1-phenylethanol transesterification reaction showed that CALB supported on MCFs grafted with methyl groups is a promising biocatalyst and isopropenyl acetate is a preferable acylation agent. Both Ru-complexes activated by K3PO4 or t-BuOK, proved to be effective catalysts of the racemization reaction. The final DKR experiments using all catalysts combinations singled out, gave 96% conversion, and (R)-1-phenylethyl acetate enantiomeric excess of 98% in 8 h using K3PO4 activator. Text Antarc* Antarctica MDPI Open Access Publishing Catalysts 11 4 518 |
institution |
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MDPI Open Access Publishing |
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ftmdpi |
language |
English |
topic |
chiral secondary alcohols resolution of enantiomers dynamic kinetic resolution DKR synthesis of enantiomers bicatalytic tandem |
spellingShingle |
chiral secondary alcohols resolution of enantiomers dynamic kinetic resolution DKR synthesis of enantiomers bicatalytic tandem Dominika Stradomska Monika Heba Aleksandra Czernek Nikodem Kuźnik Danuta Gillner Katarzyna Maresz Wojciech Pudło Andrzej Jarzębski Katarzyna Szymańska Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols |
topic_facet |
chiral secondary alcohols resolution of enantiomers dynamic kinetic resolution DKR synthesis of enantiomers bicatalytic tandem |
description |
Dynamic kinetic resolution (DKR) is one of the most attractive methods for enantioselective synthesis. In the reported studies, lipase B from Candida antarctica (CALB) immobilized on siliceous mesoporous cellular foams (MCF) functionalized with different hydrophobic groups, and two ruthenium complexes with substituted cyclopentadienyl ligands were investigated as catalysts for the chemoenzymatic DKR of (rac)-1-phenylethanol, using Novozym 435 as a benchmark biocatalyst. Studies on the (rac)-1-phenylethanol transesterification reaction showed that CALB supported on MCFs grafted with methyl groups is a promising biocatalyst and isopropenyl acetate is a preferable acylation agent. Both Ru-complexes activated by K3PO4 or t-BuOK, proved to be effective catalysts of the racemization reaction. The final DKR experiments using all catalysts combinations singled out, gave 96% conversion, and (R)-1-phenylethyl acetate enantiomeric excess of 98% in 8 h using K3PO4 activator. |
format |
Text |
author |
Dominika Stradomska Monika Heba Aleksandra Czernek Nikodem Kuźnik Danuta Gillner Katarzyna Maresz Wojciech Pudło Andrzej Jarzębski Katarzyna Szymańska |
author_facet |
Dominika Stradomska Monika Heba Aleksandra Czernek Nikodem Kuźnik Danuta Gillner Katarzyna Maresz Wojciech Pudło Andrzej Jarzębski Katarzyna Szymańska |
author_sort |
Dominika Stradomska |
title |
Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols |
title_short |
Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols |
title_full |
Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols |
title_fullStr |
Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols |
title_full_unstemmed |
Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols |
title_sort |
lipase immobilized on mcfs as biocatalysts for kinetic and dynamic kinetic resolution of sec-alcohols |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2021 |
url |
https://doi.org/10.3390/catal11040518 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Catalysts; Volume 11; Issue 4; Pages: 518 |
op_relation |
Biocatalysis https://dx.doi.org/10.3390/catal11040518 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/catal11040518 |
container_title |
Catalysts |
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11 |
container_issue |
4 |
container_start_page |
518 |
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1774712849348689920 |