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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Published in:Biotechnology and Bioengineering
Main Authors: Hagström, Anna E.V., Nordblad, Mathias, Adlercreutz, Patrick
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2008
Subjects:
Online Access:http://dx.doi.org/10.1002/bit.22111
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spelling 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
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language 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
container_start_page 693
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