Functional and Bioactive Properties of Wheat Protein Fractions: Impact of Digestive Enzymes on Antioxidant, α-Amylase, and Angiotensin-Converting Enzyme Inhibition Potential

This research aimed to determine the biofunctional properties of wheat flour (WF) protein fractions and modifications antioxidant, anti-α-amylase anti-angiotensin-I converting enzyme (ACE) activities induced by action digestive endopeptidases in vitro. A molecular characterization most abundant fractions, i.e., albumins, glutelins-1, glutelins-2 prolamins, showed that low- high-MW polypeptides rich cysteine, glutamic acid leucine were present albumins glutelins, whereas low-MW subunits with a high proportion polar amino acids prevailed prolamins. Prolamins exhibited second-highest water holding capacity (54%) after WF (84%), while provided superior foam stability (76%). Prolamins, glutenins-1 globulins demonstrated highest antioxidant activity (up 95%, 68% 59%, respectively) both before hydrolysis pepsin (P-H) or trypsin–chymotrypsin (TC-H). strongly inhibited α-amylase (>90%) TC-H, P-H (55–71%). Moreover, significantly increased inhibition from 53 74%. The strong ACE inhibitory (70–89%) included prolamins TC-H P-H, as well P-H. novel evidence indicates their peptide-enriched P TC hydrolysates are excellent sources multifunctional bioactives antihyperglycemic antihypertensive potential.