Sequential ultrasound treatment enhances aggregation modulation, network structuring, and gel performance of low-salt...

This study investigated the regulation of multiscale structural transitions, aggregation behavior, and gel properties of low-salt myofibrillar protein (MP)-soy protein isolate (SPI)-potato protein (PP) composite systems by the ultrasonic treatment sequence. Results showed that the introduction of SPI/PP promoted MP unfolding and the formation of small molecule aggregates. The ultrasonic sequence regulated intermolecular forces and protein interaction modes. Specifically, ultrasonic pretreatment of SPI-PP (U(SPI-PP)-MP) significantly reduced particle size, maximized solubility and Zeta potential, and formed a uniform, compact gel network, leading to superior structural integrity and enhanced overall gel performance. Conversely, other ultrasonic sequences caused decreased gel performance and presented rough and non-uniform structures. These findings emphasize the critical role of ultrasonic treatment sequence in the assembly and function of animal-plant protein gels. This study provides important theoretical basis and technical pathways for designing and optimizing the microstructure and functional properties of low-sodium protein products based on ultrasonic technology.