Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone
International audience Copolymers of g-butyrolactone (g-BL) and 3-caprolactone (3-CL) were successfully synthesized by ring-opening polymerization using Novozyme-435 (immobilized lipase B from Candida antartica) as catalyst. Copolymers with different compositions were obtained and characterized by 1...
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ftunimontpellier:oai:HAL:hal-00417160v1 2024-05-12T07:56:52+00:00 Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone Li, Suming Institut des Biomolécules Max Mousseron Pôle Chimie Balard (IBMM) Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) PRA E01-03 2005 https://hal.science/hal-00417160 https://doi.org/10.1016/j.polymer.2005.10.121 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.polymer.2005.10.121 hal-00417160 https://hal.science/hal-00417160 doi:10.1016/j.polymer.2005.10.121 ISSN: 0032-3861 Polymer https://hal.science/hal-00417160 Polymer, 2005, 46, pp.12682-12688. ⟨10.1016/j.polymer.2005.10.121⟩ Enzymatic copolymerization Enzymatic degradation PCL/PBL copolymer [CHIM.POLY]Chemical Sciences/Polymers info:eu-repo/semantics/article Journal articles 2005 ftunimontpellier https://doi.org/10.1016/j.polymer.2005.10.121 2024-04-17T15:29:07Z International audience Copolymers of g-butyrolactone (g-BL) and 3-caprolactone (3-CL) were successfully synthesized by ring-opening polymerization using Novozyme-435 (immobilized lipase B from Candida antartica) as catalyst. Copolymers with different compositions were obtained and characterized by 1H NMR, 13C NMR, GPC, DSC and X-ray diffraction. Increasing the [BL]/[CL] feed ratio resulted in decreases of molecular weight (Mn) of copolymers and reaction yield. Moreover, the BL contents in the copolymers varied according to the feed ratio. The Tm of the copolymers decreased from 58 to 49 8C with increase in BL content from 0 to 14%. The resulting copolymers were all semicrystalline with a PCLtype crystalline structure. Solution cast films were allowed to degrade in a pH 7.0 phosphate buffer solution containing Pseudomonas lipase. Weight loss data showed that the degradation rate of copolymers in the presence of Pseudomonas lipase decreased with the increase of BL contents. Article in Journal/Newspaper antartic* Université de Montpellier: HAL Polymer 46 26 12682 12688 |
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Open Polar |
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Université de Montpellier: HAL |
op_collection_id |
ftunimontpellier |
language |
English |
topic |
Enzymatic copolymerization Enzymatic degradation PCL/PBL copolymer [CHIM.POLY]Chemical Sciences/Polymers |
spellingShingle |
Enzymatic copolymerization Enzymatic degradation PCL/PBL copolymer [CHIM.POLY]Chemical Sciences/Polymers Li, Suming Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
topic_facet |
Enzymatic copolymerization Enzymatic degradation PCL/PBL copolymer [CHIM.POLY]Chemical Sciences/Polymers |
description |
International audience Copolymers of g-butyrolactone (g-BL) and 3-caprolactone (3-CL) were successfully synthesized by ring-opening polymerization using Novozyme-435 (immobilized lipase B from Candida antartica) as catalyst. Copolymers with different compositions were obtained and characterized by 1H NMR, 13C NMR, GPC, DSC and X-ray diffraction. Increasing the [BL]/[CL] feed ratio resulted in decreases of molecular weight (Mn) of copolymers and reaction yield. Moreover, the BL contents in the copolymers varied according to the feed ratio. The Tm of the copolymers decreased from 58 to 49 8C with increase in BL content from 0 to 14%. The resulting copolymers were all semicrystalline with a PCLtype crystalline structure. Solution cast films were allowed to degrade in a pH 7.0 phosphate buffer solution containing Pseudomonas lipase. Weight loss data showed that the degradation rate of copolymers in the presence of Pseudomonas lipase decreased with the increase of BL contents. |
author2 |
Institut des Biomolécules Max Mousseron Pôle Chimie Balard (IBMM) Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) PRA E01-03 |
format |
Article in Journal/Newspaper |
author |
Li, Suming |
author_facet |
Li, Suming |
author_sort |
Li, Suming |
title |
Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
title_short |
Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
title_full |
Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
title_fullStr |
Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
title_full_unstemmed |
Enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
title_sort |
enzyme-catalysed polymerization and degradation of copolyesters of e-caprolactone and g-butyrolactone |
publisher |
HAL CCSD |
publishDate |
2005 |
url |
https://hal.science/hal-00417160 https://doi.org/10.1016/j.polymer.2005.10.121 |
genre |
antartic* |
genre_facet |
antartic* |
op_source |
ISSN: 0032-3861 Polymer https://hal.science/hal-00417160 Polymer, 2005, 46, pp.12682-12688. ⟨10.1016/j.polymer.2005.10.121⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.polymer.2005.10.121 hal-00417160 https://hal.science/hal-00417160 doi:10.1016/j.polymer.2005.10.121 |
op_doi |
https://doi.org/10.1016/j.polymer.2005.10.121 |
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Polymer |
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46 |
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26 |
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12682 |
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12688 |
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