Abstract
The aggregate of an amphiphilic block copolymer consisting of poly[(N-acetylimino)ethylene] and poly[(N-pentanoylimino)ethylene] was prepared and its host properties for hydrophobic molecules in aqueous solution were studied by gel-filtration and a fluorescent probe. The aggregate showed strong guest-binding ability for 8-anilino-1-naphthalenesulfonic acid (ANS) and pyrene compared with its monomeric form. The interactions of three enzymes, horseradish peroxidase (HRP), Lipase OF, and Lipase P, to the aggregate were investigated by ultrafiltration and gel filtration analyses. The hydrolysis activities of Lipase OF and Lipase P in aqueous solution increased about 30% in the presence of the aggregate. The polymer-lipase P aggregate showed remarkably enhanced activity in comparison with the native enzyme in water-saturated organic solvent.
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Naka, K., Kubo, Y., Ohki, A. et al. Aggregate of Amphiphilic Block Copolymer Derived from Poly [(N-acylimino)ethylene]s and Guest-Binding Properties for 8-Anilino-1-naphthalenesulfonic Acid, Pyrene, and Enzymes. Polym J 26, 243–249 (1994). https://doi.org/10.1295/polymj.26.243
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DOI: https://doi.org/10.1295/polymj.26.243
