The physicochemically characterized divalent cation-driven whey protein isolate (WPI) fibrils were assessed by interfacial viewpoint, then the corresponding ultrastable HIPPEs containing nutritional cations were characterized. The amyloids mediated the interfacial interactions with in-plane bending, producing a firm elastic temperature-independent structure. The multi-core microstructure of Fe2+-mediated fibrils with high bundling minimized the textural properties and complex viscosity (105–112 mPa.s) with reduced elastic portion. The Ca2+- and Mg2+-assisted fibrils less influenced by hydrophobic forces had the minimum oil loss (1.1, 0.59%). Multi-layered microstructure of Zn2+-driven fibrils reduced fibril-water interactions. The semi-flexible zigzagshaped interwined microstructure of Ca2+-driven fibrils greatly stabilized the HIPPE at high frequencies (100 Hz). The random coils reduced the fibril ability to hold water, reducing firmness. The oxygen permeation respectively increased and decreased by heavy components and polygonal shape of the oil droplets. Larger ionic radii increased electrophoretic mobility of fibrils, reducing the droplet size of HIPPEs by Coulomb repulsions.

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