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Biocatalytic polyester acrylation-process optimization and enzyme stability.

Hagström, Anna LU ; Nordblad, Mathias LU and Adlercreutz, Patrick LU orcid (2009) In Biotechnology and Bioengineering 102. p.693-699
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(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,... (More)
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. (Less)
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
acrylation, lipase, enzyme stability, process optimization
in
Biotechnology and Bioengineering
volume
102
pages
693 - 699
publisher
John Wiley & Sons Inc.
external identifiers
  • wos:000262598200005
  • pmid:18821636
  • scopus:60349099060
  • pmid:18821636
ISSN
1097-0290
DOI
10.1002/bit.22111
language
English
LU publication?
yes
id
df3565c3-b72a-485f-8c1f-47bf07ff00d2 (old id 1262766)
date added to LUP
2016-04-01 11:55:12
date last changed
2025-10-14 10:59:31
@article{df3565c3-b72a-485f-8c1f-47bf07ff00d2,
  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(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.}},
  author       = {{Hagström, Anna and Nordblad, Mathias and Adlercreutz, Patrick}},
  issn         = {{1097-0290}},
  keywords     = {{acrylation; lipase; enzyme stability; process optimization}},
  language     = {{eng}},
  pages        = {{693--699}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Biotechnology and Bioengineering}},
  title        = {{Biocatalytic polyester acrylation-process optimization and enzyme stability.}},
  url          = {{http://dx.doi.org/10.1002/bit.22111}},
  doi          = {{10.1002/bit.22111}},
  volume       = {{102}},
  year         = {{2009}},
}