Abstract

In the presence of substrate, the milk-clotting enzyme preparation of Penicillium citrinum showed a good stability against heat and p H changes. A linear relationship was observed between the amount of the enzyme and the reciprocal of clotting time. The rate of milk-clotting depended on a certain ratio between the enzyme and the substrate. Citrate-phosphate buffer of different p H values was unsuitable for electrophoretic separation of the enzyme components. Successful electrophoretic separation of the fungal enzyme preparation into 4 components was achieved with 0.01 M or 0.02 M acetate buffer of p H 3.42. Acetate buffers of higher p H values and those of higher concentrations were unsuitable. The rennin-like fractions constituted 2/3 of the enzyme preparation, and comprised 93% of the total milk-clotting activity.

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