Ultrasonication improved myofibrillar protein-stabilized emulsions: Oil/ water interface adsorption behavior and rheological behavior

This study systematically investigated the ultrasonic enhancement of myofibrillar protein (MP)-stabilized emulsions, with emphasis on interfacial adsorption behavior and rheological properties. High-intensity ultrasonication (20 kHz, 500 W, 15 min) induced a 77.5 % reduction (p < 0.05) in MP particle size and a 61.0 % increase in solubility at pH 7.0, accompanied by the exposure of latent hydrophobic domains and free sulfhydryl groups. These structural modifications significantly enhanced the interfacial adsorption capacity of MPs. Actin was identified as the dominant interfacial-binding protein through SDS-PAGE analysis. Rheological characterization revealed pseudoplastic behavior in MP-stabilized emulsions, where 15-min ultrasonication markedly reinforced emulsion network structures. Intriguingly, while prolonged ultrasonication (15 min) exhibited the strongest correlation (p < 0.05) with emulsion stabilization efficacy, optimal functional performance was achieved at 10-min treatment. This study provides a robust theoretical basis and strong technical support for the application of ultrasonication in optimizing the emulsifying properties of proteins.