THE COMPOSITIONS OF SOME PEPTIDES PRODUCED BY AN ENZYMIC HYDROLYSIS OF WHEAT GLIADIN

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Abstract
Wheat gliadin was hydrolyzed extensively by treatment with pepsin and then by trypsin. A large number of peptides were produced as well as small amounts of some amino acids, thus indicating a substantial amount of hydrolysis of gliadin by the enzymes. Five peptides were obtained crystalline and two of these constitute 11.5% and 1.2% of gliadin, respectively. Their structures have been partly determined. The results indicate that wheat gliadin contains (Asp. Asp) bonds and at least 1.9% of the glutamic acid is present as glutamylglutamic acid.