[Trypsin immobilization on a mineral matrix].

Trypsin immobilization on the mineral matrix--silochrome was studied. The effect of the matrix electrochemical nature on the process was examined. pH-optima for trypsin binding with different silochromes and pH-optimum of action of the immobilized enzyme on casein were determined. The effect on the trypsin-silochrome binding of different supplements--inhibitors (benzamidine), stabilizers (Ca2+) and substrates (casein, benzoyl argininamide hydrochloride) was demonstrated.