![]() |
|
|
Division of Protein Chemistry, The Squibb Institute for Medical Research, New Brunswick, N. J.
Casein was digested by Protease 15 and Rhozyme P-11 under conditions which minimized any change from the original amino acid composition of casein either by the removal or destruction of amino acids or by the addition of any significant amounts of amino acids from the enzymes. When fed to rats and dogs, the 2 hydrolysates prepared by the digestion of casein in neutral medium were found to yield the same nitrogen balance indexes and protein efficiencies as the whole protein.
These results suggest that neither the degree of digestion up to 40% nor the mode of attack necessarily affect the nutritive values of casein hydrolysates, so long as essential amino acids and perhaps the growth factors in casein are not destroyed.
Manuscript received 18 March 1948.