[Stabilization of modified glucose oxidase from Penicillium vitale incorporated into the polymeric chains of gels]

Glucose oxidase from Penicillium vitale was modified by unsaturated compounds, e.g. acrolein, allylisothiocyanate, acryloyl chloride and maleic anhydride. The degree of modification for the respective agents made up to 27.2, 8.3, 11.1 and 35.0% of the amine residues; the enzymatic activity was thereby retained by 98, 100, 0.03 and 58%, respectively. The thermal stability of modified enzymes was decreased 2-7 times. The modified preparations were copolymerized with acrylamide or 2-hydroxyethyl methacrylate, spatially cross-linked by N,N'-methylenebisacrylamide or ethyleneglycol dimethacrylate, respectively. The rate constants for thermal inactivation of immobilized glucose oxidase were 2-31 times lower as compared to the inactivation constants of the unmodified enzyme, incorporated into the same matrices.