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...
Published in: | Biomolecules |
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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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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 |
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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 |
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3 |
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4 |
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461 |
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480 |
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1800752650094903296 |