Abstract
In this study, the in vitro digestion process of green wheat protein (GWP) was explored by simulating the gastrointestinal digestion. The digestibility of GWP was 65.23%, and was mainly digested by trypsin. During the digestion process of GWP, large-size particles are digested by pepsin, and medium-sized particles are digested by trypsin into smaller particles; irregular large block structure with smooth surface was gradually turned into smaller blocks with porous surface; and the spatial conformation was loosened mainly by the unfolding of β-sheet structure. Gel electrophoresis demonstrated that HMW glutenin and ω-gliadins in GWP were completely digested, while LMW glutenin and α/β/γ-gliadins were partially digested. Additionally, the peptide lengths were relatively dispersed after pepsin digestion. Most of the peptides (76.5%) fell into the range 3-15 amino acid after pepsin and trypsin digestion. The molecular weight (MW) of most pepsin digestion products was above 2000 Da, whereas the MW of trypsin digestion products was mainly concentrated in 500-2000 Da. Besides, the sensitizing peptide sequence of wheat protein was detected in the final digestion products of GWP. This research provided a theoretical guidance for the development and application of GWP.