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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Published in:Biotechnology and Bioengineering
Main Authors: Hagström, Anna, Nordblad, Mathias, Adlercreutz, Patrick
Format: Article in Journal/Newspaper
Language:English
Published: John Wiley & Sons Inc. 2009
Subjects:
Online Access:https://lup.lub.lu.se/record/1262766
https://doi.org/10.1002/bit.22111
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spelling 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
container_issue 3
container_start_page 693
op_container_end_page 699
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