Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization

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.