Abstract
κ-Casein and crude λ-casein were separated from crude κ-casein (calcium soluble fraction of Warner's α-casein). Development of turbidity and liberation of non protein nitrogen (NPN) in crude κ-casein by rennin, as already reported, was assumed to be attributed to the change of κ-casein itself. Liberation of NPN from αR-casein (calcium insoluble fraction of Warner's α-casein) and purified κ-casein by pepsin and chymotrypsin was compared with that by rennin. It was demonstrated that pepsin, as well as rennin, liberated a definite amount of NPN from κ-casein and scarcely liberated it from αR;-casein, while chymotrypsin liberated NPN from both fractions increasingly with the increment of re-action time.
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