The weak gluten paradox: Post-hydrolysis protein reaggregation and glutenin ratio synergistically retard starch digestion.

While intact gluten networks modulate starch digestion, the multiscale regulatory mechanisms of gluten hydrolysates remain elusive. This study explored how gluten hydrolysates, varying in strength and glutenin-to-gliadin ratio, modulate starch digestibility through protein network reconstruction and molecular interactions. We identified a reversal of the strength-dependent pattern: weak-gluten hydrolysates retard starch digestion more effectively than their strong-gluten counterparts. Hydrolysis of weak gluten appears to enhance subsequent protein reaggregation during hydrothermal processing, consistent with a compact protein-starch matrix. Increasing the glutenin ratio raised unextractable polymeric protein from 5.78% to 26.33%. Conversely, elevating the gliadin ratio impaired the structural barrier in weak gluten while altering hydrophobic assemblies in strong systems. These findings support a dual-mechanism framework in which reconstructed protein networks and interfacial protein-starch and protein-enzyme interactions jointly regulate starch digestion, pointing to protein-mediated strategies in wheat-based foods.