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Composition of Undigested Peptide Fragments from Gluten with Regard to Bioavailability of Essential Amino Acids
Author(s) -
LANDMANN WENDELL A.,
PADMANABHAN DHANAKOTI,
YOUNG CHARLES R.
Publication year - 1985
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1985.tb13015.x
Subject(s) - chemistry , gluten , amino acid , bioavailability , methionine , wheat gluten , peptide , lysine , threonine , dansyl chloride , biochemistry , corn gluten meal , essential amino acid , serine , chromatography , biology , soybean meal , organic chemistry , enzyme , derivatization , high performance liquid chromatography , bioinformatics , raw material
Our purpose was to isolate and characterize the high molecular weight peptides resulting from the in vitro digestion of wheat gluten in a system simulating actual in vivo conditions, and to determine to what extent essential amino acids were included in these peptides. Large peptides were separated from the smaller products by CuSephadex G‐25, TLE and TLC, treated with dansyl chloride for end group determination, and redansylated to identify the remaining amino acids. Fifteen peptides, hexapeptides or larger, were isolated and were found to contain about 16.1% of the threonine, 15.2% of the methionine and 12.3% of the lysine originally present in wheat gluten.