Mechanistic study of ultrasound synergy with soybean 11S globulin to improve myofibrillar protein gel properties in low-salt lamb: molecular conformation and water migration

The quality deterioration of low-salt meat products poses a significant technical challenge in the development of innovative meat products. This study, investigated the impact of co-sonication with soybean 11S globulin on the conformation and gel properties of myofibrillar proteins (MPs) derived from low-salt lamb. The findings revealed that ultrasound treatment for 30 min combined with 4 % soybean 11S globulin markedly improved the solubility, surface hydrophobicity, reactive sulfhydryl group content, and energy storage modulus (G') of low-salt MPs, while substantially reducing the particle size and turbidity. Ultrasound treatment induced protein depolymerization, accompanied by a structural transition from α-helix to β-sheet. Furthermore, disulfide bonding and hydrophobic interactions enhanced the cross-linking and aggregation of MP with 11S globulin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis confirmed the formation of new protein aggregates (63 kDa) and macromolecules through the interaction between 11S globulin and MP. This cross-linking mechanism promoted the formation of a more compact gel network, significantly enhancing the mechanical strength and water-holding capacity of the protein gel. In conclusion, the synergistic application of ultrasound and soybean 11S globulin significantly improved the gelation properties of low-salt MP, offering a promising technological solution for the production of high-quality, low-salt meat products.