Synergistic gelation mechanisms in β-conglycinin/glycinin/Patatin ternary systems: Tuning multi-scale structure by...

This study investigated the gelation mechanism among soybean β-conglycinin (7S), glycinin (11S) and potato patatin by systematically constructing ternary composite gels with varying 7S/11S ratios. Compared with soybean protein isolate (SPI) alone, the incorporation of patatin significantly improved network continuity and uniformity. Within these patatin-containing gels, further tuning the 7S/11S ratio revealed that as 7S/11S decreased from 1/0 to 0/1, gel hardness, disulfide bond content and free water increased. Water holding capacity (WHC), hydrophobic interactions and protein area fraction initially increased but then declined at the 0/1 ratio. This trend reflects the delicate balance between 7S-driven flexibility and 11S-mediated cross-linking. Correspondingly, the 2/1 ratio exhibited the highest β-sheet content and storage modulus (G'), the lowest β-turn, random coil and average pore diameter, thereby forming the most favorable gel network structure among ternary composite gels. Thus, optimizing the 7S/11S ratio together with patatin provides a practical strategy to tailor gel network architecture in plant-based protein systems.