Biocatalytic polyester acrylation-process optimization and enzyme stability.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1262766
- author
- Hagström, Anna LU ; Nordblad, Mathias LU and Adlercreutz, Patrick LU
- organization
- publishing date
- 2009
- 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
- 2022-01-26 20:10:36
@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}}, }