Synthesis of functional derivative peptides by enzymatic way
The present work consisted in studying the N and/or O-enzymatic acylation of amino alcohols and dipeptides. A preliminary study was firstly undertaken about the enzymatic acylation of a bifunctionnal model molecule, 6-amino-1-hexanol and demonstrated the ability of the lipase B of Candida antarctica...
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2008
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ftccsdartic:oai:HAL:tel-01753057v1 2023-05-15T13:49:11+02:00 Synthesis of functional derivative peptides by enzymatic way Synthèse de dérivés fonctionnels de petits peptides par voie enzymatique Husson, Eric Laboratoire des Sciences du Génie Chimique (LSGC) Institut National Polytechnique de Lorraine (INPL)-Centre National de la Recherche Scientifique (CNRS) Institut National Polytechnique de Lorraine Ivan Marc 2008-11-06 https://hal.univ-lorraine.fr/tel-01753057 https://hal.univ-lorraine.fr/tel-01753057/document https://hal.univ-lorraine.fr/tel-01753057/file/2008_HUSSON_E.pdf fr fre HAL CCSD NNT: 2008INPL061N tel-01753057 https://hal.univ-lorraine.fr/tel-01753057 https://hal.univ-lorraine.fr/tel-01753057/document https://hal.univ-lorraine.fr/tel-01753057/file/2008_HUSSON_E.pdf info:eu-repo/semantics/OpenAccess https://hal.univ-lorraine.fr/tel-01753057 Alimentation et Nutrition. Institut National Polytechnique de Lorraine, 2008. Français. ⟨NNT : 2008INPL061N⟩ N and/or O-acylation Supercritical carbon dioxyde Solvent- free system Acyl-transferase Dipeptides Lipase CAL B Ionic liquid Selectivity Organic solvent N et/ou O-acylation Sélectivité CO2 supercritique Liquide ionique Système sans solvant Solvant organique Acylation Peptides Polyphénols [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition [SPI.OTHER]Engineering Sciences [physics]/Other info:eu-repo/semantics/doctoralThesis Theses 2008 ftccsdartic 2021-02-28T01:05:37Z The present work consisted in studying the N and/or O-enzymatic acylation of amino alcohols and dipeptides. A preliminary study was firstly undertaken about the enzymatic acylation of a bifunctionnal model molecule, 6-amino-1-hexanol and demonstrated the ability of the lipase B of Candida antarctica to catalyze the acylation of this substrate in different reaction media. The reaction performed in organic solvents (hexane, 2-methyl-2-butanol) allowed to the synthesis of the diacylated product with a substrate conversion yield of 85 %, showing the absence of chimio-selectivity of the reaction. The use of a solvent-free system constituted of free fatty acid and the use of supercritical carbon dioxide permitted to orientate the selectivity of the reaction in favour of the O-acylation. Ionic liquids with imidazolium cation and few nucleophilic anions led to a substrate conversion of 99 % and to maintain the absence of chemo-selectivity observed in organic solvents. Then, the study focused on the acylation of model dipeptides like Lys-Ser, HCl and Ser-Leu. Results relative to the acylation of Lys-Ser, HCl catalyzed by the lipase B of Candida antarctica immobilized showed a selectivity in favour of the acylation of the e-amino function independently of the reaction medium. The Ser-Leu O-acylation permitted to demonstrate the influence of the molecular environment (electro-attractor C terminal carboxylic group) on the reactivity of the serine hydroxyl function. Finally, the enzymatic acylation of a bioactive dipeptide was catalyzed by the lipase B of Candida antarctica immobilized in organic solvent and by the acyl-transferase of Candida parapsilosis in lipid-aqueous biphasic medium. The acylation of carnosine allowed the N-oleyl carnosine synthesis. The acylation of carnosine did not affect its xanthine oxydase inhibition activity and seemed to improve its superoxyde anion scavenging property Ce travail a consisté à étudier la N et/ou O acylation enzymatique d'alcool aminés et de dipeptides.Une étude préliminaire ... Doctoral or Postdoctoral Thesis Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
institution |
Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
French |
topic |
N and/or O-acylation Supercritical carbon dioxyde Solvent- free system Acyl-transferase Dipeptides Lipase CAL B Ionic liquid Selectivity Organic solvent N et/ou O-acylation Sélectivité CO2 supercritique Liquide ionique Système sans solvant Solvant organique Acylation Peptides Polyphénols [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition [SPI.OTHER]Engineering Sciences [physics]/Other |
spellingShingle |
N and/or O-acylation Supercritical carbon dioxyde Solvent- free system Acyl-transferase Dipeptides Lipase CAL B Ionic liquid Selectivity Organic solvent N et/ou O-acylation Sélectivité CO2 supercritique Liquide ionique Système sans solvant Solvant organique Acylation Peptides Polyphénols [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition [SPI.OTHER]Engineering Sciences [physics]/Other Husson, Eric Synthesis of functional derivative peptides by enzymatic way |
topic_facet |
N and/or O-acylation Supercritical carbon dioxyde Solvent- free system Acyl-transferase Dipeptides Lipase CAL B Ionic liquid Selectivity Organic solvent N et/ou O-acylation Sélectivité CO2 supercritique Liquide ionique Système sans solvant Solvant organique Acylation Peptides Polyphénols [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition [SPI.OTHER]Engineering Sciences [physics]/Other |
description |
The present work consisted in studying the N and/or O-enzymatic acylation of amino alcohols and dipeptides. A preliminary study was firstly undertaken about the enzymatic acylation of a bifunctionnal model molecule, 6-amino-1-hexanol and demonstrated the ability of the lipase B of Candida antarctica to catalyze the acylation of this substrate in different reaction media. The reaction performed in organic solvents (hexane, 2-methyl-2-butanol) allowed to the synthesis of the diacylated product with a substrate conversion yield of 85 %, showing the absence of chimio-selectivity of the reaction. The use of a solvent-free system constituted of free fatty acid and the use of supercritical carbon dioxide permitted to orientate the selectivity of the reaction in favour of the O-acylation. Ionic liquids with imidazolium cation and few nucleophilic anions led to a substrate conversion of 99 % and to maintain the absence of chemo-selectivity observed in organic solvents. Then, the study focused on the acylation of model dipeptides like Lys-Ser, HCl and Ser-Leu. Results relative to the acylation of Lys-Ser, HCl catalyzed by the lipase B of Candida antarctica immobilized showed a selectivity in favour of the acylation of the e-amino function independently of the reaction medium. The Ser-Leu O-acylation permitted to demonstrate the influence of the molecular environment (electro-attractor C terminal carboxylic group) on the reactivity of the serine hydroxyl function. Finally, the enzymatic acylation of a bioactive dipeptide was catalyzed by the lipase B of Candida antarctica immobilized in organic solvent and by the acyl-transferase of Candida parapsilosis in lipid-aqueous biphasic medium. The acylation of carnosine allowed the N-oleyl carnosine synthesis. The acylation of carnosine did not affect its xanthine oxydase inhibition activity and seemed to improve its superoxyde anion scavenging property Ce travail a consisté à étudier la N et/ou O acylation enzymatique d'alcool aminés et de dipeptides.Une étude préliminaire ... |
author2 |
Laboratoire des Sciences du Génie Chimique (LSGC) Institut National Polytechnique de Lorraine (INPL)-Centre National de la Recherche Scientifique (CNRS) Institut National Polytechnique de Lorraine Ivan Marc |
format |
Doctoral or Postdoctoral Thesis |
author |
Husson, Eric |
author_facet |
Husson, Eric |
author_sort |
Husson, Eric |
title |
Synthesis of functional derivative peptides by enzymatic way |
title_short |
Synthesis of functional derivative peptides by enzymatic way |
title_full |
Synthesis of functional derivative peptides by enzymatic way |
title_fullStr |
Synthesis of functional derivative peptides by enzymatic way |
title_full_unstemmed |
Synthesis of functional derivative peptides by enzymatic way |
title_sort |
synthesis of functional derivative peptides by enzymatic way |
publisher |
HAL CCSD |
publishDate |
2008 |
url |
https://hal.univ-lorraine.fr/tel-01753057 https://hal.univ-lorraine.fr/tel-01753057/document https://hal.univ-lorraine.fr/tel-01753057/file/2008_HUSSON_E.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
https://hal.univ-lorraine.fr/tel-01753057 Alimentation et Nutrition. Institut National Polytechnique de Lorraine, 2008. Français. ⟨NNT : 2008INPL061N⟩ |
op_relation |
NNT: 2008INPL061N tel-01753057 https://hal.univ-lorraine.fr/tel-01753057 https://hal.univ-lorraine.fr/tel-01753057/document https://hal.univ-lorraine.fr/tel-01753057/file/2008_HUSSON_E.pdf |
op_rights |
info:eu-repo/semantics/OpenAccess |
_version_ |
1766250977924481024 |