Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols
This study shows the influence of the amount of Candida Antarctica-B lipase on reactivity and selectivity in lipase-catalyzed acylation of arylalkylcarbinols 1-8. For 1-indanol 1 and with isopropenyl acetate, the selectivity E increases from 60 to > 500 when the amount of the lipase decreases fro...
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ftunivlouvain:oai:dial.uclouvain.be:boreal:108408 2024-05-12T07:53:28+00:00 Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols Merabet-Khelassi, Mounia Bouzemi, Nassima Fiaud, Jean-Claude Riant, Olivier Aribi-Zouioueche, Louisa UCL - SST/IMCN/MOST - Molecules, Solids and Reactivity 2011 http://hdl.handle.net/2078.1/108408 https://doi.org/10.1016/j.crci.2011.07.005 eng eng Elsevier boreal:108408 http://hdl.handle.net/2078.1/108408 doi:10.1016/j.crci.2011.07.005 urn:ISSN:1631-0748 info:eu-repo/semantics/restrictedAccess Comptes rendus. Chimie, Vol. 14, no. 11, p. 978-986 (2011) Arylalkylcarbinols Enzymatic kinetic resolution Isopropenyl acetate Lipases Selectivity Succinic anhydride Vinyl acetate info:eu-repo/semantics/article 2011 ftunivlouvain https://doi.org/10.1016/j.crci.2011.07.005 2024-04-17T17:23:36Z This study shows the influence of the amount of Candida Antarctica-B lipase on reactivity and selectivity in lipase-catalyzed acylation of arylalkylcarbinols 1-8. For 1-indanol 1 and with isopropenyl acetate, the selectivity E increases from 60 to > 500 when the amount of the lipase decreases from 150 to 3 mg. For the 1,2,3,4-tetrahydronaphthalen-1-ol 4, in the presence of succinic anhydride, the decrease of the amount of Candida Antarctica-B from 150 to 20 mg brings an improvement of the selectivity from E = 50 to E = 140. For the acylation of α-hydroxyferrocene 8 with vinyl acetate, high selectivities are reached with the lipases of Candida Antarctica-B, C = 50% E > 500 and Pseudomonas cepacia, C = 42% E = 425. The reduction of the amount of CAL-B, in toluene, results in an increase of the selectivity of acylation of ferrocenylethanol 8, from E = 20 to E > 500. This effect is not displayed in di-isopropylether. © 2011 Académie des sciences. Published by Elsevier Masson SAS. All rights reserved. Article in Journal/Newspaper Antarc* Antarctica DIAL@UCLouvain (Université catholique de Louvain) Comptes Rendus Chimie 14 11 978 986 |
institution |
Open Polar |
collection |
DIAL@UCLouvain (Université catholique de Louvain) |
op_collection_id |
ftunivlouvain |
language |
English |
topic |
Arylalkylcarbinols Enzymatic kinetic resolution Isopropenyl acetate Lipases Selectivity Succinic anhydride Vinyl acetate |
spellingShingle |
Arylalkylcarbinols Enzymatic kinetic resolution Isopropenyl acetate Lipases Selectivity Succinic anhydride Vinyl acetate Merabet-Khelassi, Mounia Bouzemi, Nassima Fiaud, Jean-Claude Riant, Olivier Aribi-Zouioueche, Louisa Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
topic_facet |
Arylalkylcarbinols Enzymatic kinetic resolution Isopropenyl acetate Lipases Selectivity Succinic anhydride Vinyl acetate |
description |
This study shows the influence of the amount of Candida Antarctica-B lipase on reactivity and selectivity in lipase-catalyzed acylation of arylalkylcarbinols 1-8. For 1-indanol 1 and with isopropenyl acetate, the selectivity E increases from 60 to > 500 when the amount of the lipase decreases from 150 to 3 mg. For the 1,2,3,4-tetrahydronaphthalen-1-ol 4, in the presence of succinic anhydride, the decrease of the amount of Candida Antarctica-B from 150 to 20 mg brings an improvement of the selectivity from E = 50 to E = 140. For the acylation of α-hydroxyferrocene 8 with vinyl acetate, high selectivities are reached with the lipases of Candida Antarctica-B, C = 50% E > 500 and Pseudomonas cepacia, C = 42% E = 425. The reduction of the amount of CAL-B, in toluene, results in an increase of the selectivity of acylation of ferrocenylethanol 8, from E = 20 to E > 500. This effect is not displayed in di-isopropylether. © 2011 Académie des sciences. Published by Elsevier Masson SAS. All rights reserved. |
author2 |
UCL - SST/IMCN/MOST - Molecules, Solids and Reactivity |
format |
Article in Journal/Newspaper |
author |
Merabet-Khelassi, Mounia Bouzemi, Nassima Fiaud, Jean-Claude Riant, Olivier Aribi-Zouioueche, Louisa |
author_facet |
Merabet-Khelassi, Mounia Bouzemi, Nassima Fiaud, Jean-Claude Riant, Olivier Aribi-Zouioueche, Louisa |
author_sort |
Merabet-Khelassi, Mounia |
title |
Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
title_short |
Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
title_full |
Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
title_fullStr |
Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
title_full_unstemmed |
Effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
title_sort |
effect of the amount of lipase on enantioselectivity in the kinetic resolution by enzymatic acylation of arylalkylcarbinols |
publisher |
Elsevier |
publishDate |
2011 |
url |
http://hdl.handle.net/2078.1/108408 https://doi.org/10.1016/j.crci.2011.07.005 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Comptes rendus. Chimie, Vol. 14, no. 11, p. 978-986 (2011) |
op_relation |
boreal:108408 http://hdl.handle.net/2078.1/108408 doi:10.1016/j.crci.2011.07.005 urn:ISSN:1631-0748 |
op_rights |
info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1016/j.crci.2011.07.005 |
container_title |
Comptes Rendus Chimie |
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14 |
container_issue |
11 |
container_start_page |
978 |
op_container_end_page |
986 |
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1798842844174090240 |