Isoelectric fractionation and some properties of a protease from soyabean seeds |
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Authors: | N Catsimpoolas S K Funk J Wang J Kenney |
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Affiliation: | Laboratory of Protein Chemistry, Central Soya Research Center, Chicago, Illinois 60639, U.S.A. |
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Abstract: | 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 Km value using BAPA as substrate was found to be 5·03 × 10?4M . 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 Ca2+ and Mg2+ ions. The protease lacked caseinolytic activity, and was not inhibited by Kunitz soyabean trypsin inhibitor. |
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