Biocatalytic polyester acrylation-process optimization and enzyme stability.
An OH-functional polyester has been acrylated via transesterification of ethyl acrylate, catalyzed by Candida antarctica lipase B (CalB) in two different preparations: Novozym(R) 435 and immobilized on Accurel(R) MP1000. The batch process resulted in incomplete acrylation as well as severe degradati...
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John Wiley & Sons Inc.
2009
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Online Access: | https://lup.lub.lu.se/record/1262766 https://doi.org/10.1002/bit.22111 |
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ftulundlup:oai:lup.lub.lu.se:df3565c3-b72a-485f-8c1f-47bf07ff00d2 2023-05-15T13:50:27+02:00 Biocatalytic polyester acrylation-process optimization and enzyme stability. Hagström, Anna Nordblad, Mathias Adlercreutz, Patrick 2009 https://lup.lub.lu.se/record/1262766 https://doi.org/10.1002/bit.22111 eng eng John Wiley & Sons Inc. https://lup.lub.lu.se/record/1262766 http://dx.doi.org/10.1002/bit.22111 wos:000262598200005 pmid:18821636 scopus:60349099060 Biotechnology and Bioengineering; 102, pp 693-699 (2009) ISSN: 1097-0290 Industrial Biotechnology acrylation lipase enzyme stability process optimization contributiontojournal/article info:eu-repo/semantics/article text 2009 ftulundlup https://doi.org/10.1002/bit.22111 2023-02-01T23:28:42Z An OH-functional polyester has been acrylated via transesterification of ethyl acrylate, catalyzed by Candida antarctica lipase B (CalB) in two different preparations: Novozym(R) 435 and immobilized on Accurel(R) 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(R) 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. 2008. (c) 2008 Wiley Periodicals, Inc. Article in Journal/Newspaper Antarc* Antarctica Lund University Publications (LUP) Biotechnology and Bioengineering 102 3 693 699 |
institution |
Open Polar |
collection |
Lund University Publications (LUP) |
op_collection_id |
ftulundlup |
language |
English |
topic |
Industrial Biotechnology acrylation lipase enzyme stability process optimization |
spellingShingle |
Industrial Biotechnology acrylation lipase enzyme stability process optimization Hagström, Anna Nordblad, Mathias Adlercreutz, Patrick Biocatalytic polyester acrylation-process optimization and enzyme stability. |
topic_facet |
Industrial Biotechnology acrylation lipase enzyme stability process optimization |
description |
An OH-functional polyester has been acrylated via transesterification of ethyl acrylate, catalyzed by Candida antarctica lipase B (CalB) in two different preparations: Novozym(R) 435 and immobilized on Accurel(R) 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(R) 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. 2008. (c) 2008 Wiley Periodicals, Inc. |
format |
Article in Journal/Newspaper |
author |
Hagström, Anna Nordblad, Mathias Adlercreutz, Patrick |
author_facet |
Hagström, Anna Nordblad, Mathias Adlercreutz, Patrick |
author_sort |
Hagström, Anna |
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 |
John Wiley & Sons Inc. |
publishDate |
2009 |
url |
https://lup.lub.lu.se/record/1262766 https://doi.org/10.1002/bit.22111 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology and Bioengineering; 102, pp 693-699 (2009) ISSN: 1097-0290 |
op_relation |
https://lup.lub.lu.se/record/1262766 http://dx.doi.org/10.1002/bit.22111 wos:000262598200005 pmid:18821636 scopus:60349099060 |
op_doi |
https://doi.org/10.1002/bit.22111 |
container_title |
Biotechnology and Bioengineering |
container_volume |
102 |
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3 |
container_start_page |
693 |
op_container_end_page |
699 |
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1766253509342134272 |