Composition and Structural Sequence Analysis of Hydrolyzed Wheat Protein Peptides
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.