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Purification of Protease from the Fungus Endothia parasitica

Department of Food Science and Technology, University of California, Davis

ABSTRACT

The protease from the fungus Endothia parasitica has been purified, by two methods, one leading to crystalline enzyme. The first method involved ammonium sulfate fractionation, gel filtration on Sephdex G-100, and chromatography twice on DEAE-cellulose at pH 4.60. The second method involved ammonium sulfate fractionation, acetone fractionation, charcoal treatment, gel filtration on Sephadex G-100, and crystallization from water-isopropanol. The crystallized material had only one-half the specific activity of the material purified by the first method. Chromatography of the crystallized enzyme on DEAE-cellulose gave a fraction with the same specific activity as that obtained by the first method. The enzyme is maximally stable at pH 4 to 5, but quite unstable at pH 7. It has a molecular weight of 37,500 by gel filtration on Sephadex G-100. The activity of the enzyme is not affected by iodoacetamide, N-ethylmaleimide, p-chloromercuribenzoate, sodium tetrathionate, and mercuric chloride, or by a-N-tosyl-L-phenylalanine chloromethyl ketone or a-N-tosyl-L-lysine chloromethyl ketone. Its isoelectric point is below pH 4.6.

¹ Jastro Scholarship recipient, 1967.