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Amyloid-like fibrils from food proteins possess unique functional properties for food and many other uses. This study reports the effect of hydrolytic heating (pH 2.0, 85 °C, 0-24 h) and incubation times (0-7 days) on the formation and physicochemical properties of amyloid fibrils based on soy protein isolates (SPI). The SPI hydrolysates and fibrils were characterized through AFM, Thioflavin T (ThT) fluorescence, SDS-PAGE, FTIR, solubility, particle size, and DSC. Stable amyloid-like protein fibrils were formed with 8-10 h of hydrolytic he
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