Covalent Interaction between High Hydrostatic Pressure-Pretreated Rice Bran Protein Hydrolysates and Ferulic Acid: Focus on Antioxidant Activities and Emulsifying Properties

Rice bran protein hydrolysates (RBPH) pretreated with high hydrostatic pressure (HHP) covalently interacted with ferulic acid (FA) (0.5 to 2.5 mg/mL) under alkaline conditions. The structural and functional properties of the conjugates were investigated. The results revealed that the FA binding equivalent on RBPH increased from 6.03 to 207.64 nmol/mg. FTIR spectral analysis indicated that the content of a-helix increased, whereas the contents of beta-sheet, beta-turn, and random coil decreased. The surface hydrophobicity (H-0) of RBPH increased, the fluorescence intensity decreased, and the tertiary structure changed because of covalent interactions between RBPH and FA. The emulsifying activity index of RBPH-FA (1.5 mg/mL) was 35.10% higher than that of the control, whereas FA concentrations higher than 1.5 mg/mL had a negative effect on emulsifying properties. RBPH-FA (2.5 mg/mL) exhibited the strongest antioxidant activity. This study provides a new reference for the application of RBPH-FA conjugates in food processing.

Automated summary

The study found that the covalent interaction between RBPH and FA increased the binding equivalent of FA on RBPH, altering the structure and properties of RBPH, and enhancing the emulsifying activity and antioxidant activity of RBPH-FA.