[Catalytic properties and thermostability of horseradish peroxidase covalently bound with Sepharose by carbohydrate residues of the enzyme].

A procedure for isolation of stabilized preparations of peroxidase, covalently bound with AH-Sepharose 4B by the enzyme carbohydrate residues, which had been previously oxidized by iodine acid, is proposed. The catalytic properties and thermostability of soluble oxidized and immobilized peroxidase has been studied and a comparison of these properties with those of the native enzyme has been made. It has been demonstrated that the oxidation of the carbohydrate residues dose not affect eh Km value for soluble oxidized peroxidase, but leads to a decrease in the kcat approximately two times for the reaction of peroxidase exidation of o-dianizidine. In case of immobilized peroxidase the Km value for H2O2 does not change, whereas the Km value for o-dianizidine is decreased approximately 20 times. It is demostrated that the chemical structure of the matrix surface and in case of the same matrix used--the degree and type of modification of the functional groups of protein, have a strong effect on the stability of the immobilized enzyme.