Solubilization strategy of myofibrillar proteins in low-ionic media (prototype soup): The effect of high-intensity ultrasound combined with non-covalent or covalent modification of polyphenols on myosin molecular assembly

This study investigated the effect of (-)-Epigallocatechin-3-gallate (EGCG) non-covalent/covalent grafting onto myofibrillar protein (MP) by high-intensity ultrasound (HIU) on its water-solubility and filament forming behavior. The results showed that the introduction of EGCG, especially in the case of covalent grafting, could inhibit the molecular assembly of myosin and improve the MP water solubility from 2.7% to 53.1% (P < 0.05). The HIU pretreatment provided more opportunities for EGCG grafting onto the ultrasound-treated protein (UMP) by disrupting the filamentous polymerization of myosin and thus further facilitated MP dissolution. Additionally, compared with the UMP-EGCG non-covalent complexes, the covalent complexes with a yellow appearance exhibited a higher absolute zeta potential (35.9 mV) and a lower particle size (53.7 mu m) (P < 0.05). Overall, the combination of HIU pretreatment and EGCG covalent modification may provide a promising method for improving the solubility and processing properties of MP in low ionic media (prototype soup).

Automated summary

This study found that covalent grafting of EGCG onto myofibrillar protein inhibited molecular assembly and improved water solubility. High-intensity ultrasound pretreatment further facilitated protein dissolution. Covalent complexes exhibited higher zeta potential and smaller particle size compared to non-covalent complexes.