Abstract

Summary The composition of buffalo milk casein and cow milk casein was almost identical in the numbers and in quantities of amino acids as estimated by paper chromatography. Pepsin hydrolysis was slower for buffalo milk casein than it was for cow milk casein, regardless of period of incubation, substrate concentration, and enzyme concentration. This was also true for trypsin, papain, and pancreatic digestion of the two types of caseins. A peptide isolated from peptic digestion of both caseins contained aspartic acid, glutamic acid, lysine, serine, glycine, arginine, threonine, tyrosine, valine, leucines, and phenylalanine.

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