title: 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 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.
authors.affiliation: Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden. anna.hagstrom@biotek.lu.se
authors.forename: Anna E V
authors.initials: AE
authors.lastname: Hagström
authors.forename: Mathias
authors.initials: M
authors.lastname: Nordblad
authors.forename: Patrick
authors.initials: P
authors.lastname: Adlercreutz
mesh_terms: D000179:Acrylates / Q000378:metabolism*; D055162:Biocatalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism; D004951:Esterification; D005656:Fungal Proteins; D008049:Lipase / Q000378:metabolism*; D011091:Polyesters / Q000378:metabolism*
chemical_list: D000179:Acrylates; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011091:Polyesters; C040833:ethyl acrylate; D008049:Lipase; C431349:lipase B, Candida antarctica