Impact of mixed β-conglycinin and hydrolysates of glycinin on the thermal transition and polymerization behavior of gluten

Selectively hydrolyzed soy protein can enhance wheat-based product quality by modulating gluten thermal polymerization. This study examined the effects of β-conglycinin (7S) and glycinin hydrolysate (GH) on gluten rheological and thermal properties, particle size, Raman spectra, and microstructure during heating. Both 7S and GH improved gluten viscoelasticity, with their combined addition (7S/GH) showing the strongest effect. 7S/GH increased the denaturation temperature by 4.94 °C and enthalpy by 43.84 %, while the D50 at 95 °C was 97.99 % higher than the control. These enhancements were linked to reinforced glutenin–gliadin crosslinking and a strengthened gluten network. 7S and GH synergistically promoted disulfide bond formation, buried tryptophan and tyrosine residues, and induced a more compact gluten conformation. Confocal laser scanning microscopy and micro-computed tomography confirmed a denser gluten network after heating. Overall, 7S and GH act synergistically to improve gluten stability, offering theoretical insights for soy protein hydrolysates in wheat-based product quality improvement.