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Proteases of the soyabean II. —Specificity of the active fractions
Author(s) -
Pinsky A.,
Grossman S.
Publication year - 1969
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740200612
Subject(s) - trypsin , proteases , hydrolysis , chemistry , fraction (chemistry) , proteolytic enzymes , chromatography , enzyme , biochemistry
Six proteolytic fractions of the soyabean differed in specificity on synthetic substrates. Their Michaelis constants on poly (L‐glutamic acid) differed one from the other. The optimum pH values of proteolytic action were slightly lower than that of the crude extract. The fractions did not autolyse, nor did one fraction hydrolyse any other. Finally, none of the fractions exhibited trypsin‐like activity, as characterised by ability to hydrolyse benzoylarginine ethyl ester, either at their optimum pH or at the pH optimum of trypsin.