ABSTRACT The 11S globulin in quinoa protein isolate (QPI) reduces its water solubility, thereby impairing its emulsifying stability and restricting its application in the food industry. To address this challenge, this study aims to enhance the interfacial functionality of QPI by constructing ordered amyloid‐like fibrils and to elucidate the structure–function relationship governing their emulsifying performance. Quinoa amyloid‐like fibrils (QAFs) are fabricated via acid‐heating treatment for varying durations (0–8 h), and the effects of heating time on their structural evolution, interfacial behavior, and emulsifying properties are systematically evaluated. The results show that QAFs obtained after 4 h of heating exhibit the highest thioflavin T fluorescence intensity, a β‐sheet content of 48.81%, a disulfide bond content of 3.17 µmol/g, and intermediate wettability (contact angle of 74.50°). These structural characteristics correspond to optimal emulsifying activity and stability. Pickering emulsions stabilized with these QAFs (2 wt%) at a 40% oil phase display the smallest droplet size ( d 3 , 2 = 7.24 µm) and the highest interfacial protein adsorption (adsorbed protein content = 89%, surface load = 0.551 ± 0.01 mg/m 2 ), along with improved rheological behavior and storage stability (creaming index < 0.05). Correlation analysis further reveals significant positive correlations between the structural parameters of QAFs, including ThT fluorescence intensity, β‐sheet content, contact angle, ζ‐potential, and disulfide bond content, and their emulsifying performance ( R 2 = 0.70–0.97). These findings clarify the stabilization mechanism of QAFs for Pickering emulsions and provide novel insights into developing amyloid‐like plant proteins as sustainable emulsion stabilizers.
Gu et al. (2026) studied this question.