The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols
International audience The current work describes the differential behaviour of Novozym® 435 (immobilized Candida antarctica lipase B) in O-acylation and N-acylation catalysis of bifunctional amino-alcohols acyl acceptors. We performed acylation experiments on three amino-alcohols (alaninol, 4-amino...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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ftanrparis:oai:HAL:hal-01070399v1 2024-09-15T17:42:44+00:00 The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols Le Joubioux, Florian Bridiau, Nicolas Ben Henda, Yesmine Achour, Oussama Graber, Marianne Maugard, Thierry LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) ANR Expenantio ANR-08-CP2D-0010,EXPENANTIO,Vers une voie durable pour la synthèse de molécules chirales: approches expérimentales et théoriques innovantes pour la compréhension des bases moléculaires de l'énantiosélectivité des lipases et des estérases - Towards green synthesis of chiral molecules(2008) 2013-06-13 https://hal.science/hal-01070399 https://hal.science/hal-01070399/document https://hal.science/hal-01070399/file/Florian3_HAL.pdf https://doi.org/10.1016/j.molcatb.2013.06.002 en eng HAL CCSD Elsevier [1995, vol. 1, iss. 1-2016, vol. 134] info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2013.06.002 hal-01070399 https://hal.science/hal-01070399 https://hal.science/hal-01070399/document https://hal.science/hal-01070399/file/Florian3_HAL.pdf doi:10.1016/j.molcatb.2013.06.002 info:eu-repo/semantics/OpenAccess ISSN: 1381-1177 EISSN: 1873-3158 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-01070399 Journal of Molecular Catalysis B: Enzymatic, 2013, 95, pp.99-110. ⟨10.1016/j.molcatb.2013.06.002⟩ [SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology info:eu-repo/semantics/article Journal articles 2013 ftanrparis https://doi.org/10.1016/j.molcatb.2013.06.002 2024-07-12T11:39:01Z International audience The current work describes the differential behaviour of Novozym® 435 (immobilized Candida antarctica lipase B) in O-acylation and N-acylation catalysis of bifunctional amino-alcohols acyl acceptors. We performed acylation experiments on three amino-alcohols (alaninol, 4-amino-1-pentanol and 6-amino- 1-hexanol) using myristic acid as an acyl donor. Two organic solvents (tert-amyl alcohol and n-hexane) and one ionic liquid (1-butyl-3-methylimidazolium hexafluorophosphate: Bmim [PF6]) were used to determine the effect of the solvent. The influence of the amino-alcohol carbon chain length between the alcohol and amino groups on chemoselectivity C (kcat,app O-acylation/kcat,app N-acylation) was highlighted. N-acylation is improved using alaninol, a short chain amino-alcohol (no mono-O-acylation in tert-amyl alcohol and C = 0.12 in n-hexane) whereas O-acylation is improved using 4-amino-1-pentanol and 6- amino-1-hexanol which are amino-alcohols with longer chain (C = 10.5 in tert-amyl alcohol and C = 539 in n-hexane). On the other hand, the production of the acylated amino-alcohols after 96 h of reaction was shown to be strongly affected by the solvent nature and the amino-alcohol structure: starting from alaninol as an acyl acceptor, the yield of amide synthesis reaches up to 98% in tert-amyl alcohol using 0.7 equivalents of myristic acid while the yield of amido-ester synthesis reaches up to 88% in Bmim [PF6] using 1.75 equivalents of myristic acid. Article in Journal/Newspaper Antarc* Antarctica Portail HAL-ANR (Agence Nationale de la Recherche) Journal of Molecular Catalysis B: Enzymatic 95 99 110 |
institution |
Open Polar |
collection |
Portail HAL-ANR (Agence Nationale de la Recherche) |
op_collection_id |
ftanrparis |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
spellingShingle |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology Le Joubioux, Florian Bridiau, Nicolas Ben Henda, Yesmine Achour, Oussama Graber, Marianne Maugard, Thierry The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
description |
International audience The current work describes the differential behaviour of Novozym® 435 (immobilized Candida antarctica lipase B) in O-acylation and N-acylation catalysis of bifunctional amino-alcohols acyl acceptors. We performed acylation experiments on three amino-alcohols (alaninol, 4-amino-1-pentanol and 6-amino- 1-hexanol) using myristic acid as an acyl donor. Two organic solvents (tert-amyl alcohol and n-hexane) and one ionic liquid (1-butyl-3-methylimidazolium hexafluorophosphate: Bmim [PF6]) were used to determine the effect of the solvent. The influence of the amino-alcohol carbon chain length between the alcohol and amino groups on chemoselectivity C (kcat,app O-acylation/kcat,app N-acylation) was highlighted. N-acylation is improved using alaninol, a short chain amino-alcohol (no mono-O-acylation in tert-amyl alcohol and C = 0.12 in n-hexane) whereas O-acylation is improved using 4-amino-1-pentanol and 6- amino-1-hexanol which are amino-alcohols with longer chain (C = 10.5 in tert-amyl alcohol and C = 539 in n-hexane). On the other hand, the production of the acylated amino-alcohols after 96 h of reaction was shown to be strongly affected by the solvent nature and the amino-alcohol structure: starting from alaninol as an acyl acceptor, the yield of amide synthesis reaches up to 98% in tert-amyl alcohol using 0.7 equivalents of myristic acid while the yield of amido-ester synthesis reaches up to 88% in Bmim [PF6] using 1.75 equivalents of myristic acid. |
author2 |
LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) ANR Expenantio ANR-08-CP2D-0010,EXPENANTIO,Vers une voie durable pour la synthèse de molécules chirales: approches expérimentales et théoriques innovantes pour la compréhension des bases moléculaires de l'énantiosélectivité des lipases et des estérases - Towards green synthesis of chiral molecules(2008) |
format |
Article in Journal/Newspaper |
author |
Le Joubioux, Florian Bridiau, Nicolas Ben Henda, Yesmine Achour, Oussama Graber, Marianne Maugard, Thierry |
author_facet |
Le Joubioux, Florian Bridiau, Nicolas Ben Henda, Yesmine Achour, Oussama Graber, Marianne Maugard, Thierry |
author_sort |
Le Joubioux, Florian |
title |
The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
title_short |
The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
title_full |
The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
title_fullStr |
The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
title_full_unstemmed |
The control of Novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
title_sort |
control of novozym® 435 chemoselectivity and specificity by the solvents in acylation reactions of amino-alcohols |
publisher |
HAL CCSD |
publishDate |
2013 |
url |
https://hal.science/hal-01070399 https://hal.science/hal-01070399/document https://hal.science/hal-01070399/file/Florian3_HAL.pdf https://doi.org/10.1016/j.molcatb.2013.06.002 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1381-1177 EISSN: 1873-3158 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-01070399 Journal of Molecular Catalysis B: Enzymatic, 2013, 95, pp.99-110. ⟨10.1016/j.molcatb.2013.06.002⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2013.06.002 hal-01070399 https://hal.science/hal-01070399 https://hal.science/hal-01070399/document https://hal.science/hal-01070399/file/Florian3_HAL.pdf doi:10.1016/j.molcatb.2013.06.002 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.molcatb.2013.06.002 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
95 |
container_start_page |
99 |
op_container_end_page |
110 |
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1810489459228016640 |