Abstract
With 0.3 M KCl replacing NaCl, the effect of L-Arg on beef myosin's gel, structure, and aggregation was investigated. L-Arg could enhance hydrogen and ionic bonds, increasing myosin solubility and reducing turbidity. The content of regular secondary structures (β-sheet) increased, and the content of random coil structures decreased significantly (p < 0.05). The results of dynamic light scattering (DLS) and atomic force microscope (AFM) further demonstrated that L-Arg could improve the uniformity and dispersion of myosin aggregate size and inhibit the aggregation of myosin between the head and the tail. Moreover, as the hydrophobic interaction and disulfide bonds were the main forces, a thermal gel dominated by myosin oligomers and filaments was formed. In the 0.3 M KCl, 0.1 M NaCl, and 0.2 M L-Arg system, the hardness, elasticity, and water holding capacity (WHC) of beef myosin gel were effectively improved, providing a salt reduction reference for beef products.