Biocatalytic polyester acrylation-process optimization and enzyme stability.

Research output: Contribution to journalArticle

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.

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Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Industrial Biotechnology

Keywords

  • acrylation, lipase, enzyme stability, process optimization
Original languageEnglish
Pages (from-to)693-699
JournalBiotechnology and Bioengineering
Volume102
Publication statusPublished - 2009
Publication categoryResearch
Peer-reviewedYes