Phospholipid-regulated myosin interfacial adsorption orderliness as a key determinant of gel network order and water holding capacity in emulsified meat systems.

To investigate the effect of phospholipids on the gel properties of myosin in emulsion systems, this study was based on the ratio of endogenous phospholipids to myosin, using lecithin as a representative phospholipid model. Different myosin-lecithin ratio emulsions (M-L1:0 to M-L1:2) were first prepared. The results showed that phospholipids combined with myosin light chains 1 and 3 (MLC-1 and MLC-3). The addition of phospholipids (M-L1:0 to M-L1:1) promoted the exposure of myosin sulfhydryl groups and altered disulfide bonds. Environmental scanning electron microscopy (ESEM) confirmed that lecithin enhanced the adsorption orderliness of myosin at the water-oil interface, thereby improving the rheological properties of the emulsion. The M-L1:1 emulsion formed an ordered, high-fractal-dimension emulsion gel network after thermal induction at 70 °C. The main stabilizing forces of this gel network were hydrophobic interactions and hydrogen bonds. Moreover, phospholipids addition (M-L1:0 to M-L1:1) converted some free water in the gel into bound water, thereby enhancing the water-holding capacity (WHC) and rheological properties of the gel. However, excess phospholipids (M-L1:2) disrupted interfacial protein adsorption orderliness, hindered formation of a stable "pre-structured" state during the emulsion-to-thermally-induced gel transition, and thus compromised gel WHC and structural stability. This study linked the adsorption orderliness of myosin at the interface with the order of the gel, clarifying the mechanism by which phospholipids improve the water distribution and network stability of myosin emulsion gels from a new perspective.