Reaction between glycidylmethacrylate and enzymes and copolymerization of the products obtained

Abstract

Abstract The reaction between glycidylmethacrylate and proteins (enzymes) leads to products which were separated by gel filtration into different fractions, which were examined by means of various analytical techniques. Spectroscopic analysis gives evidence of a perturbation of the chromophore groups of the protein as a consequence of a strong interaction with the bifunctional monomer. This perturbation is caused by reaction under formation of a covalent bond as verified especially by electrophoretic and amino acid analysis and secondarily by IR and NMR spectra. The competitive reactivity of epoxy ring and double bond of the monomer can be established by the comparative reaction between monofunctional monomers, as methylacrylate and methylmethacrylate, and the protein. The effect of the reaction with glycidylmethacrylate on the stability of the enzymes is a decrease of the specific activity from 5 to 30% for reaction periods ranging from 12 to 120 h. The copolymerization of the reaction products produces materials having activities dependent on the degree of substitution of the fractions, and recoveries of activity higher than 50%.