Abstract
The preceding paper described that the digestibility of casein, defined by the measurement of liberated nitrogen and freed 18 amino acid patterns, increased slightly by heat treatment, and it was superior to that of rice glutelin throughout the varying digesting time periods by both enzymes, pancreatin and pronase.
The present paper reports on the results of the liberation of eighteen kinds of amino acid from wheat gluten and soybean glycinine (with and without heating) through the above described enzymes. As shown in Tables 1 and 2, the digestibility of heated glycinine thus measured was superior to that of wheat gluten, although the measures of both substrates were inferior to that of casein. The manner of increase of the amount of each amino acid according to the digesting time period was not always identical on the kind of amino acid, substrate conducted and the test enzyme used.
