[Production and properties of trypsin immobilized on a polyurethane matrix].

Two methods were used to immobilize trypsin on the polyurethane carrier on the basis of toluylenediisocyanatepolyoxypropylene glycol due to interaction between the lyzine free amino groups and the enzyme arginine guanidine group and the prepolymer isocyanate group. The amount of the enzyme chemically bound by the two methods is about 50 and more than 70%, respectively. The substrate specificity of the initial and washed samples of the immobilized trypsin was studied with respect to three highly molecular substrates with different molecular weight and different charges--protamine, casein, hemoglobin. It is shown that independently of the method of binding the activity of the immobilized trypsin is the highest with respect to hemoglobin and is the lowest with respect to protamine. The samples of trypsin immobilized on the polyurethane carrier may be used in biology and medicine when creating the prolonged forms of the enzymic preparations.