Myosin supramolecular self-assembly: The crucial precursor that manipulates the covalent aggregation, emulsification and rheological properties of myosin.

The transformation of molecular conformation and self-assembly properties of myosin during the heating process at different ionic strengths (0.2 M, 0.4 M and 0.6 M NaCl) and its effect on rheological behavior and emulsification properties were investigated. Under incubation temperatures between 40 °C and 50 °C, myosin underwent a supramolecular self-assembly stage dominated by noncovalent forces (hydrogen bonding, ionic bonding and hydrophobic interactions). Higher ionic strength facilitated molecular rearrangement through enhanced swelling of myosin heads and head-to-head assemblies, which contributed to enhanced ordering and homogeneity of myosin covalent aggregates (above 60 °C) and manifested itself macroscopically as enhanced gel viscoelasticity and emulsion stability. In contrast, at lower ionic strength, the tail-to-tail assemblies of myosin led to the preferential formation of covalent cross-links in the tails, which resulted in the inability of molecular rearrangement and the formation of disordered aggregates and finally led to the deterioration of the gel and the destabilization of the emulsion. In conclusion, the supramolecular self-assembly behavior of myosin, as an intermediate process in myosin's sol-gel transition, is crucial for the orderliness of myosin assemblies, gel network strengthening, and emulsion stability. The obtained insight provides a reference for the precise implementation of quality improvement strategies for meat products.