Hagström Anna E V, Nordblad Mathias, Adlercreutz Patrick
Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
Biotechnol Bioeng. 2009 Feb 15;102(3):693-9. doi: 10.1002/bit.22111.
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.
一种含羟基的聚酯已通过丙烯酸乙酯的酯交换反应进行丙烯酸化，该反应由两种不同制剂中的南极假丝酵母脂肪酶B（CalB）催化：诺维信435以及固定在Accurel MP1000上的CalB。间歇过程导致丙烯酸化不完全以及聚酯严重降解。通过采用低压（15 kPa）、丙烯酸乙酯连续流入和连续蒸馏以蒸发副产物乙醇进行优化，实现了高度丙烯酸化。酶制剂表现出良好的稳定性，诺维信435和CalB/MP1000的半衰期分别为180小时和324小时。这转化为产物产率分别为催化剂重量的3600倍和6200倍，表明该酶对总工艺成本的影响很小。
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