Fibrillation of plant proteins is a promising approach to enhance their gel properties. In this study, black kidney bean protein isolate self-assembled into amyloid fibrils and subsequently formed hydrogels at a concentration of 2.0 wt% after thermal treatment at pH 2.0. Gel structure and rheological properties were modulated by regulating the acid-heat incubation time (0-72 h). With increased incubation time, the black kidney bean protein fibrils (BKPFs) transitioned through distinct states: sol state (8 h), gel state formed by fibril entanglement (12-20 h), and disrupted gel state by partial depolymerization of fibril aggregates (>
24 h). Rheological analysis revealed that the gels at 16 h had maximum storage modulus (159.9 Pa). Small-angle X-ray scattering indicated that BKPFs highly aggregated (R