Hydrophobic polyphenols, with a variety of physiological activities, are often practically limited due to their low water solubility and chemical instability, among which curcumin (Cur) is a representative hydrophobic polyphenol. To improve Cur, the cod protein (CP)-Cur composite particles (CP-Cur) were successfully prepared using the pH-shift method, but this pH-shift method (7-12-7) required a higher pH, which limited application and increased cost. The critical pH of CP structure unfolding during pH-shift and its encapsulation effect on Cur were investigated in this paper. During the pH-shift process, the critical pH of the structural unfolding of CP was pH 10, and the degree of protein structure unfolding was higher, which was attributed to the increasing electrostatic repulsion, and the weakened hydrogen bond and hydrophobic interaction. The encapsulation efficiency of CP-Cur formed after pH 10-shift was higher than that formed after pH 9.8-shift, which increased by 22.17 %. At pH 9.8, the binding sites in CP reached saturation at the molar ratio of 10, while at pH 10 and 10.2, the binding sites in CP both reached saturation at the molar ratio of 14, also indicating that the protein treated with critical pH could bind more Cur. The binding between Cur and CP was mostly hydrophobic interaction, accompanied by hydrogen bonding and electrostatic interactions. The above results verified the necessity of critical pH in the experiment, indicating that critical pH could indeed improve the encapsulation effect and obtain a higher encapsulation efficiency. This work will help improve the large-scale application of hydrophobic functional substances in production.
Keywords: Cod protein; Conformational change; Critical pH; Curcumin; Interaction.
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