Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization |
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Authors: | C. Daubresse Ch. Grandfils R. Jérome Ph. Teyssié |
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Affiliation: | (1) Center for Education and Research on Macromolecules (CERM), University of Liège Chemistry Institute, B6, 4000 Liège (Sart-Tilman), Belgium |
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Abstract: | This paper deals with the immobilization of alkaline phosphatase by physical entrapment within colloidal particles produced by inverse microemulsion polymerization. Functionality has been imparted to the nanoparticle surface by copolymerization of acrylamide (the main monomer),N,N-methylene-bis-acrylamide (the cross-linking agent) with eitherN-acryloyl-1,6-diaminohexane (an amine promoter) or acrylic acid (a carboxylic acid promoter). The effect of the functional comonomers on the size and zeta potential of the reactive latexes has been studied. Integrity of the immobilized enzyme has been ascertained from its catalytic activity towards hydrolysis ofp-nitrophenylphosphate. |
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Keywords: | Inverse microemulsion polymerization microemulsion protein immobilization latex surface modification |
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