ENZYME IMMOBILIZATION IN REACTIVE NANOPARTICLES PRODUCED BY INVERSE MICROEMULSION POLYMERIZATION

This paper deals with the immobilization of alkaline phosphatase by ph ysical entrapment within colloidal particles produced by inverse micro emulsion polymerization. Functionality has been imparted to the nanopa rticle surface by copolymerization of acrylamide (the main monomer), N ,N'-methylene-bisacrylamide (the cross-linking agent) with either N-ac ryloyl-1,6-diaminohexane (an amine promoter) or acrylic acid (a carbox ylic acid promoter). The effect of the functional comonomers on the si ze and zeta potential of the reactive latexes has been studied. Integr ity of the immobilized enzyme has been ascertained from its catalytic activity towards hydrolysis of p-nitrophenylphosphate.