[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.
D002364:Caseins; D004800:Enzymes, Immobilized; D006863:Hydrogen-Ion Concentration; D012822:Silicon Dioxide; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors
D002364:Caseins; D004800:Enzymes, Immobilized; D014361:Trypsin Inhibitors; D012822:Silicon Dioxide; D014357:Trypsin
Immobilizatsiia tripsina na mineral'noĭ matritse.