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Biocatalytic polyester acrylation-process optimization and enzyme stability.

Hagström, Anna LU ; Nordblad, Mathias LU and Adlercreutz, Patrick LU (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
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
external identifiers
  • wos:000262598200005
  • pmid:18821636
  • scopus:60349099060
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
2008-11-25 18:17:44
date last changed
2017-03-05 03:29:14
@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},
  keyword      = {acrylation,lipase,enzyme stability,process optimization},
  language     = {eng},
  pages        = {693--699},
  publisher    = {John Wiley & Sons},
  series       = {Biotechnology and Bioengineering},
  title        = {Biocatalytic polyester acrylation-process optimization and enzyme stability.},
  url          = {http://dx.doi.org/10.1002/bit.22111},
  volume       = {102},
  year         = {2009},
}