Amyloid fibrils from black kidney bean protein self-assemble into hydrogels: Impact of heating time on gel structure and rheological properties

被引:0
作者
Wang, Shurui [1 ]
Liu, Peixuan [1 ]
Zang, Yiyu [1 ]
Wei, Jiaoyue [1 ]
Sun, Cuixia [1 ]
Li, Xiaoyang [1 ]
Zhao, Yiguo [1 ]
Cao, Yiping [1 ]
Lu, Wei [1 ]
Fang, Yapeng [1 ]
机构
[1] Shanghai Jiao Tong Univ, Sch Agr & Biol, Dept Food Sci & Technol, Shanghai 200240, Peoples R China
关键词
Black kidney bean protein isolate; Fibrillation; Gel properties; Incubation time; GLOBULAR-PROTEINS; PEA PROTEIN; KINETICS; POLYPHENOL; MECHANISM; GELATION; FORCES; FOOD;
D O I
10.1016/j.foodchem.2025.143406
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
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-g = 49.49 nm) with a more compact mass fractal structure (D-f = 2.0) at 16 h. Cryo-scanning electron microscopy images showed the formation of a homogeneous and dense three-dimensional gel network structure at 12 h.
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页数:13
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