ORBi: Daubresse Catherine - Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization

Reference : Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polyme...


	Document type :	Scientific journals : Article
	Discipline(s) :	Engineering, computing & technology : Materials science & engineering Physical, chemical, mathematical & earth Sciences : Chemistry
	To cite this reference:	http://hdl.handle.net/2268/15554

Title :	Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization
Language :	English
Author, co-author :	Daubresse, Catherine [University of Liège (ULg) > Department of Chemistry > Center for Education and Research on Macromolecules (CERM) > >]
	Grandfils, Christian [University of Liège (ULg) > Department of Chemistry > Center for Education and Research on Macromolecules (CERM) > >]
	Jérôme, Robert [University of Liège (ULg) > Department of Chemistry > Center for Education and Research on Macromolecules (CERM) > >]
	Teyssié, Philippe [University of Liège (ULg) > Department of Chemistry > Center for Education and Research on Macromolecules (CERM) > >]
Publication date :	May-1996
Journal title :	Colloid and Polymer Science
Publisher :	Springer
Volume :	274
Issue/season :	5
Pages :	482-489
Audience :	International
ISSN :	0303-402X
Keywords :	[en] microemulsion polymerization
Abstract :	[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 units :	Center for Education and Research on Macromolecules (CERM)
Funders :	Politique Scientifique Fédérale (Belgique) = Belgian Federal Science Policy ; Eurogentec ; The “Institut pour l’Encouragement de la Recherche Scientifique dans l’Indiustrie et l’Agriculture” (IRSIA)
Target :	Researchers
Permalink :	http://hdl.handle.net/2268/15554
DOI :	10.1007/BF00652472
Other URL :	http://www.springerlink.com/content/kl4387m7441567v3/fulltext.pdf
Mentions required by the publisher for OA :	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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