PAPER CHROMATOGRAPHY OF CASEIN AND RENNIN

Abstract

Purified rennins of very high activity were prepared. The amino acid com position of the hydrolyzates of these preparations was studied by paper chromato graphy. Several fractions were obtained from the purified rennins by paper chromatography showing strong enzyme activity which was comparable to the density of their color development with a benzidine reagent. Whether these fractions represent distinct molecular species is not known as yet. The active enzyme was separated from the inert material of a crude commercial rennet powder by chromatography. The action of rennin on milk and casein was also studied by chromatographic techniques. It would appear that rennin causes an unfolding and breaking of the alpha casein molecule with the appearance of several large polypeptides. No free amino acids were detected after rennin action on casein.