Enzymic proteolysis

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Abstract
A study was made of the progressive liberation of ammonia and of amino-groups during the action of pepsin, trypsin, erepsin and of papain on 3 typical proteins, casein, edestin, and gliadin. It was shown that amide and peptide hydrolyses did not run parallel and that the ammonia formed was not directly connected with proteolytic action but arose from the decomposition of the primary products of protein cleavage. This secondary decomposition was not enzymic in nature but was brought about by the acidic or alkaline reactions of the digestion media. In papain digestion ammonia formation was an enzymic function. Papain either possessed deamidase activity itself or contained a component which had such activity.