[Cooxidation of phenol and 4-aminoantipyrin, catalyzed by polymers and copolymers of horseradish root peroxidase and Penicillium funiculosum 46.1 glucose oxidase].
Polymers and copolymers of horseradish root peroxidase (HRP) and Penicillium funiculosum 46.1 glucose oxidase (GO) have been synthesized and their catalytic properties have been characterized (free and immobilized forms of each enzyme were studied). The cooxidation reaction of phenol and 4-aminoantipyrin (4-AAP), performed in an aqueous medium in the presence of equimolar amounts of GO and HRP, was characterized by effective K(M) and k(cat) of 0.58 mM and 20.9 s(-1) (for phenol), and 14.6 mM and 18.4 s(-1) (glucose), respectively. The catalytic efficiency of polymerization products (PPs) of GO (GO-PPs) depended on the extent of their aggregation. The combinations GO + HRP-PP and HRP + GO-PP, as well as the copolymer HRP*-GO-PP, proved promising as reagents for enzyme-based analytical systems. When adsorbed on aluminum hydroxide gels, GO-PPs exhibited higher catalytic activity than the non-polymeric enzyme. Maximum retention of GO-PP activity on the inorganic carrier was observed in the case of GO-PP copolymers with an activated HRP. Polymerization of HRP in the presence of a zinc hydroxide gel, paralleled by HRP-PP immobilization onto the gel, increased both the activity of the enzyme and its operational stability.
Eremin
A N
AN
Semashko
T V
TV
Mikhaĭlova
R V
RV
D000675:Ampyrone / Q000737:chemistry*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D005949:Glucose Oxidase / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry; D010084:Oxidation-Reduction; D010407:Penicillium / Q000201:enzymology*; D019800:Phenol / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011108:Polymers; D000675:Ampyrone; D019800:Phenol; D005949:Glucose Oxidase; D006735:Horseradish Peroxidase