The authors acknowledge Colloid and Polymer Science (Springer) for allowing them to archive this paper. The original publication is available at http://www.springerlink.com/content/kl4387m7441567v3/?p=d9a2ecc0d7d8405f8bc8ea4a8d754922&pi=11
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[en] 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 either N-acryloyl-l,6-diamino-hexane (an amine promoter) or acrylic acid (a carboxylic acid promoter). The effect of the functions 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 of p-nitrophenyl-phosphate.
Research center :
Center for Education and Research on Macromolecules (CERM)
Disciplines :
Chemistry Materials science & engineering
Author, co-author :
Daubresse, Catherine; Université de Liège - ULiège > Department of Chemistry > Center for Education and Research on Macromolecules (CERM)
Grandfils, Christian ; Université de Liège - ULiège > Department of Chemistry > Center for Education and Research on Macromolecules (CERM)
Jérôme, Robert ; Université de Liège - ULiège > Department of Chemistry > Center for Education and Research on Macromolecules (CERM)
Teyssié, Philippe ; Université de Liège - ULiège > Department of Chemistry > Center for Education and Research on Macromolecules (CERM)
Language :
English
Title :
Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization
BELSPO - Politique scientifique fédérale [BE] Eurogentec IRSIA - Institut pour l'Encouragement de la Recherche Scientifique dans l'Industrie et l'Agriculture [BE]
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