Solubilization and stable dispersion of myofibrillar proteins in water through the destruction and inhibition of the assembly of filaments using high-intensity ultrasound.

The insolubility and poor dispersion of myofibrillar proteins (MPs) in water have always been the primary factors limiting the development of novel meat-based products. This study aimed to explore the mechanisms by which high-intensity ultrasound (HIU) at various power settings (0, 150, 300, 450 and 600 W) improved the solubility and dispersion stability of MPs in water. According to the solubility analysis, HIU significantly increased the water solubility of MPs (p < 0.05). The MPs treated with 450 W exhibited the best dispersion stability in water, which corresponded to the highest zeta-potential, smallest particle size and most uniform distribution (p < 0.05). Based on the circular dichroism and fluorescence spectroscopy and surface hydrophobicity analysis, the loss of the MP superhelix and subsequent random dissociation of the filamentous myosin structure appeared to be the main mechanism of MP solubilization. In addition, according to the zeta-potential, SDS-PAGE and Nano LC-ESI-MS/MS analyses, the increase in surface charge and the formation of soluble oligomers may provide additional forces to inhibit filament assembly, thereby improving the stability of the aqueous MP suspension. Atomic force microscopy (AFM) observations further confirmed these results. In conclusion, an HIU treatment effectively improves the solubility and dispersion stability of MP in water.