[Trypsin immobilization on a mineral matrix].

G P Ivanova; L A Zaĭtseva; Mirgorodskaia; B V Moskvichev

PubMed · 31617

[Trypsin immobilization on a mineral matrix].

G P Ivanova·L A Zaĭtseva·Mirgorodskaia·B V Moskvichev

Abstract

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.

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Caseins Enzymes, Immobilized Hydrogen-Ion Concentration Silicon Dioxide Substrate Specificity Trypsin Trypsin Inhibitors English Abstract Journal Article

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G P Ivanova, L A Zaĭtseva, Mirgorodskaia, B V Moskvichev. [Trypsin immobilization on a mineral matrix].. https://pubmed.ncbi.nlm.nih.gov/31617/

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