Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids

© 2015 Elsevier B.V.Lipase-based catalysts were tested for the ring-opening polymerization of d-, l- and d,l-lactide isomers, highlighting the different specificity of the enzyme toward these isomers. Free form of Candida antarctica lipase B (CALB) and its clay- and acrylic resin- immobilized forms...

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Published in:Journal of Molecular Catalysis B: Enzymatic
Main Authors: Düşkünkorur, H, Bégué, A, Pollet, Eric, Phalip, Vincent, Güvenilir, Y, Avérous, Luc
Other Authors: Laboratoire des Matériaux, Surfaces et Procédés pour la Catalyse (LMSPC), Institut de chimie et procédés pour l'énergie, l'environnement et la santé (ICPEES), Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE), Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE), Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS)-Centre National de la Recherche Scientifique (CNRS)
Format: Article in Journal/Newspaper
Language:English
Published: HAL CCSD 2015
Subjects:
Online Access:https://hal.archives-ouvertes.fr/hal-03112160
https://doi.org/10.1016/j.molcatb.2015.01.011
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language English
topic [CHIM.POLY]Chemical Sciences/Polymers
spellingShingle [CHIM.POLY]Chemical Sciences/Polymers
Düşkünkorur, H
Bégué, A
Pollet, Eric
Phalip, Vincent
Güvenilir, Y
Avérous, Luc
Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids
topic_facet [CHIM.POLY]Chemical Sciences/Polymers
description © 2015 Elsevier B.V.Lipase-based catalysts were tested for the ring-opening polymerization of d-, l- and d,l-lactide isomers, highlighting the different specificity of the enzyme toward these isomers. Free form of Candida antarctica lipase B (CALB) and its clay- and acrylic resin- immobilized forms were compared. For l- and d,l-lactide monomers only short oligomers were obtained. The acrylic resin immobilized form of CALB (NOVO-435) led to a complete conversion of d-lactide to PDLA with a Mn of 2600 g/mol, whereas the clay-immobilized and free forms of CALB exhibited slower kinetics and produced chains of lower Mn. Copolymerization reactions between ε-caprolactone and lactide isomers were performed using NOVO-435 as bio-catalyst. Random copolyesters were successfully synthesized by copolymerizing d-lactide with ε-caprolactone. Better results were obtained with a two-step reaction, starting from presynthesized polycaprolactone chains, compared with the one-pot copolymerization. Conducting this two-step copolymerization in the presence of organo-modified montmorillonite allowed the successful synthesis of copolymer/clay nanohybrids.
author2 Laboratoire des Matériaux, Surfaces et Procédés pour la Catalyse (LMSPC)
Institut de chimie et procédés pour l'énergie, l'environnement et la santé (ICPEES)
Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE)
Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE)
Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Biotechnologie et signalisation cellulaire (BSC)
Université de Strasbourg (UNISTRA)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS)-Centre National de la Recherche Scientifique (CNRS)
format Article in Journal/Newspaper
author Düşkünkorur, H
Bégué, A
Pollet, Eric
Phalip, Vincent
Güvenilir, Y
Avérous, Luc
author_facet Düşkünkorur, H
Bégué, A
Pollet, Eric
Phalip, Vincent
Güvenilir, Y
Avérous, Luc
author_sort Düşkünkorur, H
title Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids
title_short Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids
title_full Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids
title_fullStr Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids
title_full_unstemmed Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids
title_sort enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. toward the in situ synthesis of organic/inorganic nanohybrids
publisher HAL CCSD
publishDate 2015
url https://hal.archives-ouvertes.fr/hal-03112160
https://doi.org/10.1016/j.molcatb.2015.01.011
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Journal of Molecular Catalysis B: Enzymatic
https://hal.archives-ouvertes.fr/hal-03112160
Journal of Molecular Catalysis B: Enzymatic, 2015, 115, ⟨10.1016/j.molcatb.2015.01.011⟩
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container_title Journal of Molecular Catalysis B: Enzymatic
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spelling ftccsdartic:oai:HAL:hal-03112160v1 2023-05-15T13:47:30+02:00 Enzymatic ring-opening (co)polymerization of lactide stereoisomers catalyzed by lipases. Toward the in situ synthesis of organic/inorganic nanohybrids Düşkünkorur, H Bégué, A Pollet, Eric Phalip, Vincent Güvenilir, Y Avérous, Luc Laboratoire des Matériaux, Surfaces et Procédés pour la Catalyse (LMSPC) Institut de chimie et procédés pour l'énergie, l'environnement et la santé (ICPEES) Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE) Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Matériaux et nanosciences d'Alsace (FMNGE) Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS) Biotechnologie et signalisation cellulaire (BSC) Université de Strasbourg (UNISTRA)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS)-Centre National de la Recherche Scientifique (CNRS) 2015 https://hal.archives-ouvertes.fr/hal-03112160 https://doi.org/10.1016/j.molcatb.2015.01.011 en eng HAL CCSD info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2015.01.011 hal-03112160 https://hal.archives-ouvertes.fr/hal-03112160 doi:10.1016/j.molcatb.2015.01.011 Journal of Molecular Catalysis B: Enzymatic https://hal.archives-ouvertes.fr/hal-03112160 Journal of Molecular Catalysis B: Enzymatic, 2015, 115, ⟨10.1016/j.molcatb.2015.01.011⟩ ///C:/Users/averous/Documents/Mendeley Desktop/Journal of Molecular Catalysis Enzymatic Halle.pdf [CHIM.POLY]Chemical Sciences/Polymers info:eu-repo/semantics/article Journal articles 2015 ftccsdartic https://doi.org/10.1016/j.molcatb.2015.01.011 2021-12-12T00:50:48Z © 2015 Elsevier B.V.Lipase-based catalysts were tested for the ring-opening polymerization of d-, l- and d,l-lactide isomers, highlighting the different specificity of the enzyme toward these isomers. Free form of Candida antarctica lipase B (CALB) and its clay- and acrylic resin- immobilized forms were compared. For l- and d,l-lactide monomers only short oligomers were obtained. The acrylic resin immobilized form of CALB (NOVO-435) led to a complete conversion of d-lactide to PDLA with a Mn of 2600 g/mol, whereas the clay-immobilized and free forms of CALB exhibited slower kinetics and produced chains of lower Mn. Copolymerization reactions between ε-caprolactone and lactide isomers were performed using NOVO-435 as bio-catalyst. Random copolyesters were successfully synthesized by copolymerizing d-lactide with ε-caprolactone. Better results were obtained with a two-step reaction, starting from presynthesized polycaprolactone chains, compared with the one-pot copolymerization. Conducting this two-step copolymerization in the presence of organo-modified montmorillonite allowed the successful synthesis of copolymer/clay nanohybrids. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Journal of Molecular Catalysis B: Enzymatic 115 20 28