Elucidation of interactions between myofibrillar proteins and κ-carrageenan as mediated by NaCl level: Perspectives on multiple spectroscopy and molecular docking.

The present study was aimed to investigate the intermolecular interaction between myofibrillar proteins (MP) and κ-carrageenan (KC) as mediated by KC concentration (0.1, 0.2, 0.3, and 0.4 %, w/w) and NaCl levels (0.3 and 0.6 M) based on the multiple spectroscopy and molecular docking. The results showed that the incorporation of KC increased the turbidity, zeta-potential, and surface hydrophobicity of MP-KC mixed sols with a dose-dependent manner, as well as significantly decreasing the protein solubility (P < 0.05), which indicated that the interaction between KC and MP promoted the expansion of protein structure and exposed more hydrophobic groups. Fluorescence spectra result revealed that the interaction between MP and KC was a static quenching in the fluorescence quenching process, which affected the aromatic amino acids residue microenvironment of MP. Moreover, the existence of KC decreased the α-helix contents of MP (P < 0.05), contributing to the transformation from random structure to organized configuration of MP. In addition, molecular forces, the molecular docking and thermodynamic parameters indicated that hydrophobic interactions, van der Waals force, and hydrogen bonding were considered as the main interaction forces between MP and KC. Furthermore, 0.6 M NaCl level rendered higher solubility and particle size, as well as lower turbidity and the surface hydrophobicity of MP-KC mixed sols than those with 0.3 M NaCl level (P < 0.05), which promoted the unfolding of MP molecule and subsequently increased the numbers of binding sites between MP and KC, facilitating the intermolecular interactions between MP and KC in mixed sols.