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...
| Published in: | Biotechnology and Bioengineering |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2008
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| Subjects: | |
| Online Access: | 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 |
| Summary: | 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. |
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