This study aimed to produce fibrils from goat whey protein concentrate (FWPCC), characterize their properties, and compare them with bovine whey protein fibrils (FWPCB). Goat whey protein concentrate (WPC) was obtained from sweet goat whey by ultrafiltration and diafiltration, and subsequently converted into fibrils at pH 2. The physicochemical and emulsifying properties of both native WPC and its fibrils (FWPC) were systematically evaluated. Transmission electron microscopy (TEM) revealed distinct morphological differences: FWPCB formed long, linear fibrils without visible aggregates, whereas FWPCC fibrils were thinner and showed stronger inter-fibrillar interactions, assembling into rope-like or dense network structures. Zeta potential measurements indicated that fibrillation increased the positive charge of proteins, enhancing electrostatic repulsion and preventing visible aggregation. Fibril suspensions exhibited higher turbidity than native WPC, which decreased in the presence of SDS, highlighting the role of hydrophobic interactions in fibril stability. Electrophoretic analysis confirmed protein denaturation and fibril formation after heat treatment, while surface hydrophobicity remained unchanged. No significant differences were observed in the emulsifying activity index (EAI), although FWPCB showed a lower creaming index. Overall, despite morphological differences, goat whey proteins fibrils exhibited physicochemical and functional properties comparable to their bovine control, supporting their potential use as an alternative protein nanostructure.