Biocatalytic polyester acrylation—process optimization and enzyme stability
Abstract An OH‐functional polyester has been acrylated via transesterification of ethyl acrylate, catalyzed by Candida antarctica lipase B (CalB) in two different preparations: Novozym® 435 and immobilized on Accurel® MP1000. The batch process resulted in incomplete acrylation as well as severe degr...
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crwiley:10.1002/bit.22111 2024-06-02T07:57:37+00:00 Biocatalytic polyester acrylation—process optimization and enzyme stability Hagström, Anna E.V. Nordblad, Mathias Adlercreutz, Patrick 2008 http://dx.doi.org/10.1002/bit.22111 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbit.22111 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.22111 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology and Bioengineering volume 102, issue 3, page 693-699 ISSN 0006-3592 1097-0290 journal-article 2008 crwiley https://doi.org/10.1002/bit.22111 2024-05-03T11:00:49Z Abstract An OH‐functional polyester has been acrylated via transesterification of ethyl acrylate, catalyzed by Candida antarctica lipase B (CalB) in two different preparations: Novozym® 435 and immobilized on Accurel® MP1000. The batch process resulted in incomplete acrylation as well as severe degradation of the polyester. A high degree of acrylation was achieved by optimization through the application of low pressure (15 kPa), continuous inflow of ethyl acrylate and continuous distillation to evaporate the by‐product, ethanol. The enzyme preparations displayed good stability with half‐lives of 180 and 324 h for Novozym® 435 and CalB/MP1000, respectively. This translates into product yields of 3600 and 6200 times the weight of the catalyst, indicating that the enzyme will have a marginal impact on the total process cost. Biotechnol. Bioeng. 2009; 102: 693–699. © 2008 Wiley Periodicals, Inc. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology and Bioengineering 102 3 693 699 |
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English |
description |
Abstract An OH‐functional polyester has been acrylated via transesterification of ethyl acrylate, catalyzed by Candida antarctica lipase B (CalB) in two different preparations: Novozym® 435 and immobilized on Accurel® MP1000. The batch process resulted in incomplete acrylation as well as severe degradation of the polyester. A high degree of acrylation was achieved by optimization through the application of low pressure (15 kPa), continuous inflow of ethyl acrylate and continuous distillation to evaporate the by‐product, ethanol. The enzyme preparations displayed good stability with half‐lives of 180 and 324 h for Novozym® 435 and CalB/MP1000, respectively. This translates into product yields of 3600 and 6200 times the weight of the catalyst, indicating that the enzyme will have a marginal impact on the total process cost. Biotechnol. Bioeng. 2009; 102: 693–699. © 2008 Wiley Periodicals, Inc. |
format |
Article in Journal/Newspaper |
author |
Hagström, Anna E.V. Nordblad, Mathias Adlercreutz, Patrick |
spellingShingle |
Hagström, Anna E.V. Nordblad, Mathias Adlercreutz, Patrick Biocatalytic polyester acrylation—process optimization and enzyme stability |
author_facet |
Hagström, Anna E.V. Nordblad, Mathias Adlercreutz, Patrick |
author_sort |
Hagström, Anna E.V. |
title |
Biocatalytic polyester acrylation—process optimization and enzyme stability |
title_short |
Biocatalytic polyester acrylation—process optimization and enzyme stability |
title_full |
Biocatalytic polyester acrylation—process optimization and enzyme stability |
title_fullStr |
Biocatalytic polyester acrylation—process optimization and enzyme stability |
title_full_unstemmed |
Biocatalytic polyester acrylation—process optimization and enzyme stability |
title_sort |
biocatalytic polyester acrylation—process optimization and enzyme stability |
publisher |
Wiley |
publishDate |
2008 |
url |
http://dx.doi.org/10.1002/bit.22111 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbit.22111 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.22111 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology and Bioengineering volume 102, issue 3, page 693-699 ISSN 0006-3592 1097-0290 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bit.22111 |
container_title |
Biotechnology and Bioengineering |
container_volume |
102 |
container_issue |
3 |
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693 |
op_container_end_page |
699 |
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1800740809659645952 |