The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols
International audience The selective acylation of multifunctional compounds exhibiting both alcohol and amino groups gives interesting products with many applications in food, cosmetic and pharmaceutical industries, but it is real challenge. The current work describes the different behavior shown by...
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ftunivrochelle:oai:HAL:hal-00789681v1 2024-02-11T09:58:28+01:00 The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols Le Joubioux, Florian Ben Henda, Yesmine Bridiau, Nicolas Achour, Oussama Graber, Marianne Maugard, Thierry LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) 2012-11-23 https://hal.science/hal-00789681 https://hal.science/hal-00789681/document https://hal.science/hal-00789681/file/publi_LeJoubioux-effet_substrat_HAL.pdf en eng HAL CCSD Elsevier hal-00789681 https://hal.science/hal-00789681 https://hal.science/hal-00789681/document https://hal.science/hal-00789681/file/publi_LeJoubioux-effet_substrat_HAL.pdf info:eu-repo/semantics/OpenAccess ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-00789681 Journal of Molecular Catalysis B: Enzymatic, 2012, 85-86, pp.193-199 [SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology info:eu-repo/semantics/article Journal articles 2012 ftunivrochelle 2024-01-23T23:33:48Z International audience The selective acylation of multifunctional compounds exhibiting both alcohol and amino groups gives interesting products with many applications in food, cosmetic and pharmaceutical industries, but it is real challenge. The current work describes the different behavior shown by Candida antarctica lipase B (Novozym 435) when catalyzing the O-acylation and N-acylation of bifunctional acyl acceptors. The acylation of three aminoalcohols (alaninol, 4-amino-1-pentanol and 6-amino-1-hexanol) was studied using myristic acid as an acyl donor. To achieve this, a structure-reactivity study was performed in tert-amyl alcohol as a solvent, comparing the three amino-alcohols as acyl acceptors and a series of structurally related amines, namely (R)-sec-butylamine, 1-methoxy-2-propylamine and 1,2- diaminopropane. These substrates were designed to investigate the effect of the group located in β-position of the amino group on the acyl acceptor: the more nucleophilic the group, the more the apparent maximal velocity (V max,app ) of N-acylation increases. Moreover, the crucial role of the carbon chain length between the alcohol and amino groups on the chemoselectivity was also demonstrated. The chemoselectivity for the N-acylation was improved when the carbon chain included two carbons (alaninol) whereas the chemoselectivity for the O- acylation was improved when the carbon chain included four carbons or more (4-amino-1- pentanol and 6-amino-1-hexanol). These results provided new insights for the selective synthesis of amides or esters produced from the acylation of bifunctional substrates. Article in Journal/Newspaper Antarc* Antarctica HAL - Université de La Rochelle |
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HAL - Université de La Rochelle |
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ftunivrochelle |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology Le Joubioux, Florian Ben Henda, Yesmine Bridiau, Nicolas Achour, Oussama Graber, Marianne Maugard, Thierry The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
description |
International audience The selective acylation of multifunctional compounds exhibiting both alcohol and amino groups gives interesting products with many applications in food, cosmetic and pharmaceutical industries, but it is real challenge. The current work describes the different behavior shown by Candida antarctica lipase B (Novozym 435) when catalyzing the O-acylation and N-acylation of bifunctional acyl acceptors. The acylation of three aminoalcohols (alaninol, 4-amino-1-pentanol and 6-amino-1-hexanol) was studied using myristic acid as an acyl donor. To achieve this, a structure-reactivity study was performed in tert-amyl alcohol as a solvent, comparing the three amino-alcohols as acyl acceptors and a series of structurally related amines, namely (R)-sec-butylamine, 1-methoxy-2-propylamine and 1,2- diaminopropane. These substrates were designed to investigate the effect of the group located in β-position of the amino group on the acyl acceptor: the more nucleophilic the group, the more the apparent maximal velocity (V max,app ) of N-acylation increases. Moreover, the crucial role of the carbon chain length between the alcohol and amino groups on the chemoselectivity was also demonstrated. The chemoselectivity for the N-acylation was improved when the carbon chain included two carbons (alaninol) whereas the chemoselectivity for the O- acylation was improved when the carbon chain included four carbons or more (4-amino-1- pentanol and 6-amino-1-hexanol). These results provided new insights for the selective synthesis of amides or esters produced from the acylation of bifunctional substrates. |
author2 |
LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
author |
Le Joubioux, Florian Ben Henda, Yesmine Bridiau, Nicolas Achour, Oussama Graber, Marianne Maugard, Thierry |
author_facet |
Le Joubioux, Florian Ben Henda, Yesmine Bridiau, Nicolas Achour, Oussama Graber, Marianne Maugard, Thierry |
author_sort |
Le Joubioux, Florian |
title |
The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols |
title_short |
The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols |
title_full |
The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols |
title_fullStr |
The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols |
title_full_unstemmed |
The effect of substrate structure on the chemoselectivity of Candida antarctica lipase B-catalyzed acylation of amino-alcohols |
title_sort |
effect of substrate structure on the chemoselectivity of candida antarctica lipase b-catalyzed acylation of amino-alcohols |
publisher |
HAL CCSD |
publishDate |
2012 |
url |
https://hal.science/hal-00789681 https://hal.science/hal-00789681/document https://hal.science/hal-00789681/file/publi_LeJoubioux-effet_substrat_HAL.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-00789681 Journal of Molecular Catalysis B: Enzymatic, 2012, 85-86, pp.193-199 |
op_relation |
hal-00789681 https://hal.science/hal-00789681 https://hal.science/hal-00789681/document https://hal.science/hal-00789681/file/publi_LeJoubioux-effet_substrat_HAL.pdf |
op_rights |
info:eu-repo/semantics/OpenAccess |
_version_ |
1790594114701492224 |