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Isoelectric fractionation and some properties of a protease from soyabean seeds
Author(s) -
Catsimpoolas N.,
Funk S. K.,
Wang J.,
Kenney J.
Publication year - 1971
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.2740220209
Subject(s) - protease , isoelectric point , isoelectric focusing , trypsin , chemistry , enzyme , substrate (aquarium) , chromatography , fractionation , arginine , germination , biochemistry , amino acid , biology , botany , ecology
A protease, capable of hydrolysing benzoyl DL ‐arginine p ‐nitroanilide(BAPA), and L ‐amino acid β‐naphthylamide derivatives, was purified, by isoelectric focusing in the region pH 3–6, from dormant and 6‐day germinated soyabean seeds. The enzyme was focused at pH 4·80. The K m value using BAPA as substrate was found to be 5·03 × 10 −4 M . Maximum activity of the enzyme towards BAPA was obtained in the pH 8·2–8–5 region. Slight activation was observed in the presence of 0·05 M concentration of Ca 2+ and Mg 2+ ions. The protease lacked caseinolytic activity, and was not inhibited by Kunitz soyabean trypsin inhibitor.