Enhancing the emulsifying properties of tea water-insoluble proteins by liposomes based on pH-induced weak force transitions.

To address the poor solubility and stability of tea water-insoluble protein (TWIP), liposomes (LS) were employed to modify TWIP, and the interaction mechanism between LS and TWIP, as well as its effects on solubility and emulsifying properties, were investigated. The results showed that LS bound to TWIP primarily through hydrophobic interactions and promoted the exposure of internal hydrophobic groups by altering the spatial conformation of TWIP, thereby enhancing its solubility, surface hydrophobicity, and emulsifying performance. In addition, the TWIP:LS ratio and pH regulated the interaction forces between the two components, thereby affecting the binding behavior and functional properties of the complex. Under the optimal conditions (TWIP:LS = 1:2, pH = 7.0), the TWIP-LS complex exhibited the best overall performance. Therefore, LS can effectively improve the solubility and emulsifying properties of TWIP, providing a feasible strategy for the utilization of TWIP in food.