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Merck

Biocatalytic polyester acrylation--process optimization and enzyme stability.

Biotechnology and bioengineering (2008-09-30)
Anna E V Hagström, Mathias Nordblad, Patrick Adlercreutz
RESUMEN

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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Sigma-Aldrich
Ethyl acrylate, contains 10-20 ppm MEHQ as inhibitor, 99%
Sigma-Aldrich
Ethyl acrylate, ≥99.5%, stabilized
Supelco
Ethyl acrylate, analytical standard
Sigma-Aldrich
Ethyl acrylate, SAJ first grade, ≥99.0%