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INACTIVATION OF FICIN PROTEOLYTIC ACTIVITY IN THE PRESENCE OF ASCORBIC ACID AND Cu2+‐IONS
Author(s) -
FUKAL LADISLAV,
KAS JAN,
SOVA ZDENEK,
RAUCH PAVEL
Publication year - 1986
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1986.tb00099.x
Subject(s) - chemistry , ascorbic acid , sephadex , chromatography , proteolytic enzymes , biochemistry , substrate (aquarium) , arginine , enzyme , amino acid , food science , biology , ecology
The simultaneous presence of ascorbic acid, Cu 2+ ions and oxygen causes irreversible ficin inactivation. The degree of inactivation is dependent on the concentration of inhibitors. Relatively higher decrease of ficin proteolytic activity was found with high molecular substrate, hide powder azure, than with a low molecular one, N‐benzoyl‐L‐arginine‐p‐nitroanilide. Gel chromatography on Sephadex G‐50 showed that ficin inactivation is not due to the destruction of its molecule resulting in the decrease of its molecular weight. Inactivation of ficin proteolytic activity was associated with a partial drop in ficin immunoreactivity.