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...
| Published in: | Biotechnology and Bioengineering |
|---|---|
| Main Authors: | , , |
| 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 |
| Summary: | 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. |
|---|