Sono-processing treatments enhanced the stability and digestive properties of soy-myofibrillar dual-protein systems.

This study systematically investigated the effects of sono-processing treatment on the stability and digestive characteristics of soy protein isolate (SPI) and myofibrillar protein (MPN) mixed systems. The sono-processing intensity in the SPI-MPN4 group reached 37.58%, which was approximately 4.12 times higher than that of the SPI-MPN2 system (9.12%), indicating significantly greater efficiency in structural modification. Consequently, the SPI-MPN4 system exhibited the most pronounced structural transformation, leading to reduced disordered aggregation and improved system stability. To be specific, the system stability of the SPI-MPN4 system was enhanced by 28.94% when compared with that of the SPI-MPN2 group. Additionally, structural analyses revealed that ultrasound effectively disrupted hydrogen bonds, reduced α-helix content, and promoted the assembly of structurally ordered SPI-MPN complexes. Notably, the random coil contents in SPI-MPN4 increased by approximately 22.70%, facilitating trypsin accessibility. These findings highlighted that sono-processing intensity changes were critical factors governing the structural alteration of the dual-protein system. This insight was pivotal for designing targeted and energy-efficient processing strategies in the future.