The application of soy protein amyloid fibrils (SAFs) to food industrialization field has received focused attention because of their advantages such as ordered supramolecular structure and anti-proteolytic properties. However, the comparatively weak gelation properties of SAFs make it difficult to form self-supporting hydrogels, limiting its potential for future applications. Additionally, the extremely acidic environment (pH 2) of SAFs hinders their practical application in the food pH range (4–7). To address this issue, a dialysis strategy was utilized to enhance the gel structure of SAFs in this paper. The SAFs were dialyzed by deionized water and zinc ions solutions with four different pHs (2, 4, 7, and 9), and the impact of various dialysates on rheological properties, water distribution, and microstructure was investigated. The results demonstrated the method significantly improved gelation properties and modified the extremely acidic environment of SAFs. Various samples were continuously deacidified during dialysis in solutions of different pHs (4, 7, and 9), transforming from pH 2 to a higher pH value. Visual images exhibited that self-supporting hydrogels can be formed by SAFs just at a low concentration of 3% (wt). SAFs-Zn2+-9 hydrogel exhibited the highest storage modulus with a 500-fold compared to SAFs-2. Notably, the SAFs-H2O hydrogels were fabricated without any exogenous substances, in which the storage modulus of SAFs-H2O-9 increased by over 300 times. AFM images demonstrated that the shift from long rigid fibrils to short flexible fibrils induced tightly entanglement among fibrils, which improved gelation performance. Moreover, the transform in pH and the incorporation of ions caused the hydrogels to show dense network structure and strong water retention capacity. The ingenious insights were provided for improving the gelation performance of SAFs and modifying the polar acidic environment in the study, fully exploiting the potential of SAFs as edible ingredients for food applications.
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