Abstract
Partial purification of milk-clotting and caseinase enzymes, produced by Penicillium oxalicum, was achieved by fractional precipitation with acetone, ethanol and methanol. Of the fractions obtained by three precipitants, the 60–70% ethanol fraction was the most promising enzyme fraction and possessed the highest milk-clotting activity, which reached about ninefold that of the culture filtrate. Purification of the milk-clotting enzyme by DEAE-cellulose column chromatography afforded a rennin-like enzyme component that showed no proteolytic activity. The enzyme activity was maximum at pH 4.0–5.0 and 65°C. In absence of substrate and up to 50°C, the enzyme showed good stability and retained 80% of its original activity after 20 min. Cu 2+, Co 2+ and Mg 2+ had stimulating effects on enzyme activity. Ascorbic acid, sodium lauryl sulphate, cysteine hydrochloride, cystine and EDTA had partial inhibitory effects on the enzyme.
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