Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources

Bio-based commercially available succinate, itaconate and 1,4-butanediol are enzymatically co-polymerized in solution via a two-stage method, using Candida antarctica Lipase B (CALB, in immobilized form as Novozyme® 435) as the biocatalyst. The chemical structures of the obtained products, poly(buty...

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Published in:Biomolecules
Main Authors: Jiang, Yi, Woortman, Albert J J, van Ekenstein, Gert O R Alberda, Loos, Katja
Format: Article in Journal/Newspaper
Language:English
Published: 2013
Subjects:
Online Access:https://hdl.handle.net/11370/af577dfc-6160-4d3b-b397-abbf22fc188d
https://research.rug.nl/en/publications/af577dfc-6160-4d3b-b397-abbf22fc188d
https://doi.org/10.3390/biom3030461
https://pure.rug.nl/ws/files/54022396/biomolecules_03_00461.pdf
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spelling ftunigroningenpu:oai:pure.rug.nl:publications/af577dfc-6160-4d3b-b397-abbf22fc188d 2024-06-02T07:56:00+00:00 Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources Jiang, Yi Woortman, Albert J J van Ekenstein, Gert O R Alberda Loos, Katja 2013-08-12 application/pdf https://hdl.handle.net/11370/af577dfc-6160-4d3b-b397-abbf22fc188d https://research.rug.nl/en/publications/af577dfc-6160-4d3b-b397-abbf22fc188d https://doi.org/10.3390/biom3030461 https://pure.rug.nl/ws/files/54022396/biomolecules_03_00461.pdf eng eng https://research.rug.nl/en/publications/af577dfc-6160-4d3b-b397-abbf22fc188d info:eu-repo/semantics/openAccess Jiang , Y , Woortman , A J J , van Ekenstein , G O R A & Loos , K 2013 , ' Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources ' , Biomolecules , vol. 3 , no. 3 , pp. 461-80 . https://doi.org/10.3390/biom3030461 article 2013 ftunigroningenpu https://doi.org/10.3390/biom3030461 2024-05-07T19:40:19Z Bio-based commercially available succinate, itaconate and 1,4-butanediol are enzymatically co-polymerized in solution via a two-stage method, using Candida antarctica Lipase B (CALB, in immobilized form as Novozyme® 435) as the biocatalyst. The chemical structures of the obtained products, poly(butylene succinate) (PBS) and poly(butylene succinate-co-itaconate) (PBSI), are confirmed by 1H- and 13C-NMR. The effects of the reaction conditions on the CALB-catalyzed synthesis of PBSI are fully investigated, and the optimal polymerization conditions are obtained. With the established method, PBSI with tunable compositions and satisfying reaction yields is produced. The 1H-NMR results confirm that carbon-carbon double bonds are well preserved in PBSI. The differential scanning calorimetry (DSC) and thermal gravimetric analysis (TGA) results indicate that the amount of itaconate in the co-polyesters has no obvious effects on the glass-transition temperature and the thermal stability of PBS and PBSI, but has significant effects on the melting temperature. Article in Journal/Newspaper Antarc* Antarctica University of Groningen research database Biomolecules 3 4 461 480
institution Open Polar
collection University of Groningen research database
op_collection_id ftunigroningenpu
language English
description Bio-based commercially available succinate, itaconate and 1,4-butanediol are enzymatically co-polymerized in solution via a two-stage method, using Candida antarctica Lipase B (CALB, in immobilized form as Novozyme® 435) as the biocatalyst. The chemical structures of the obtained products, poly(butylene succinate) (PBS) and poly(butylene succinate-co-itaconate) (PBSI), are confirmed by 1H- and 13C-NMR. The effects of the reaction conditions on the CALB-catalyzed synthesis of PBSI are fully investigated, and the optimal polymerization conditions are obtained. With the established method, PBSI with tunable compositions and satisfying reaction yields is produced. The 1H-NMR results confirm that carbon-carbon double bonds are well preserved in PBSI. The differential scanning calorimetry (DSC) and thermal gravimetric analysis (TGA) results indicate that the amount of itaconate in the co-polyesters has no obvious effects on the glass-transition temperature and the thermal stability of PBS and PBSI, but has significant effects on the melting temperature.
format Article in Journal/Newspaper
author Jiang, Yi
Woortman, Albert J J
van Ekenstein, Gert O R Alberda
Loos, Katja
spellingShingle Jiang, Yi
Woortman, Albert J J
van Ekenstein, Gert O R Alberda
Loos, Katja
Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
author_facet Jiang, Yi
Woortman, Albert J J
van Ekenstein, Gert O R Alberda
Loos, Katja
author_sort Jiang, Yi
title Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
title_short Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
title_full Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
title_fullStr Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
title_full_unstemmed Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
title_sort enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources
publishDate 2013
url https://hdl.handle.net/11370/af577dfc-6160-4d3b-b397-abbf22fc188d
https://research.rug.nl/en/publications/af577dfc-6160-4d3b-b397-abbf22fc188d
https://doi.org/10.3390/biom3030461
https://pure.rug.nl/ws/files/54022396/biomolecules_03_00461.pdf
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Jiang , Y , Woortman , A J J , van Ekenstein , G O R A & Loos , K 2013 , ' Enzyme-catalyzed synthesis of unsaturated aliphatic polyesters based on green monomers from renewable resources ' , Biomolecules , vol. 3 , no. 3 , pp. 461-80 . https://doi.org/10.3390/biom3030461
op_relation https://research.rug.nl/en/publications/af577dfc-6160-4d3b-b397-abbf22fc188d
op_rights info:eu-repo/semantics/openAccess
op_doi https://doi.org/10.3390/biom3030461
container_title Biomolecules
container_volume 3
container_issue 4
container_start_page 461
op_container_end_page 480
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