From molecular interactions to macroscopic stability: How ionic strength modulates fish myofibrillar protein...

This study employed a multi-scale approach to elucidate the interfacial adsorption behavior of myofibrillar proteins (MPs) and the molecular mechanisms underlying emulsion stability under different ionic strengths. The interfacial adsorption of MPs primarily depends on electrostatic and hydrophobic interactions. When MPs approach the interface, structural changes occur, accompanied by angular deflection and orientation towards the horizontal direction. High ionic strengths (0.6-1.0 mol/L) enhance the K_diff of MPs, with the thickness and mass of the interface film showing significant changes as ionic strength increases (1 > 0.8 > 0.4 > 0.6 > 0.2 > 0). At 0.6 mol/L, the elasticity of the interface film reaches its peak, the emulsion exhibits the strongest deformation resistance, and achieves optimal stability. This discovery deepens our understanding of protein adsorption behavior at oil/water interfaces and provides new theoretical basis and methodological guidance for the practical application of MPs in the field of food emulsions.