Literature DB >> 18821636

Biocatalytic polyester acrylation--process optimization and enzyme stability.

Anna E V Hagström1, Mathias Nordblad, Patrick Adlercreutz.   

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.

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Year:  2009        PMID: 18821636     DOI: 10.1002/bit.22111

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  1 in total

1.  Effects of Regioselectivity and Lipid Class Specificity of Lipases on Transesterification, Exemplified by Biodiesel Production.

Authors:  Dovilė Sinkūnienė; Patrick Adlercreutz
Journal:  J Am Oil Chem Soc       Date:  2014-04-26       Impact factor: 1.849

  1 in total

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