Covalent Interaction between Rice Protein Hydrolysates and Chlorogenic Acid: Improving the Stability of Oil-in-Water Emulsions.

Protein hydrolysates, as surfactants, can scavenge radicals, but their poor distributions at the oil-water interface limit their storage stability. Therefore, we studied covalent interaction between rice protein hydrolysates and chlorogenic acid under alkaline conditions to improve the physical and oxidative stability of oil-in-water emulsions. Turbidity and particle size measurements demonstrated the formation of hydrolysates-chlorogenic acid complexes, and their covalent interaction resulted in the decrease and redshift of the fluorescence intensity. The emulsifying activity of the hydrolysates could be effectively improved after the covalent interaction with 0.025% chlorogenic acid. The modified emulsions possessed a notable physical stability according to the least changes in size (0.08 μm) and ζ-potential (3.34 mV) of the emulsion ( P > 0.05). Moreover, the covalent interaction endowed modified emulsions with high oxidative stability to effectively inhibit lipid oxidative deterioration during storage. The adsorption of hydrolysates to the emulsion interface was increased by the adequate addition of chlorogenic acid, which resulted in the oil droplet being surrounded by a thicker interfacial film. The covalent interaction between the protein hydrolysates and chlorogenic acid could be used to construct natural emulsion systems with a higher physical and oxidative stability during storage.