Composition and Structural Sequence Analysis of Hydrolyzed Wheat Protein Peptides

Abstract:

Hydrolyzed wheat protein was analyzed by basic physicochemical components, relative molecular mass distribution, and amino acid composition. The peptide composition and sequence were identified by LC-MS/MS. The results showed that the total protein mass fraction of hydrolyzed wheat protein was (80.53±8.06)%, with the relative molecular mass mainly below 2 000 and a mass fraction of essential amino acids approximately 52.4%. Eight peptides were identified by Q3 scanning, PIS scanning, and MRM quantification, including leucyl-glutamine(LQ), valanyl- glutamine(VQ), isoleucyl-isoleucine(II), leucyl-leucine(LL), alanyl-isoleucine(AI), valanyl-leucine(VL), leucyl-methionine(LM) and isoleucyl-methionine(IM), with mass fractions of 385.0, 32.5, 30.0, 122.8, 8.9, 5.9, 134.9, 147.0 μg/g, respectively. These peptides may exhibit functional activities in vivo and serve as the material foundation for the application of hydrolyzed wheat protein in nutritional health food.