This study aims to optimize the ultrasound treatment conditions for enhancing the degree of glycation (DG) of ovalbumin (OVA)-xylose conjugates through Maillard reaction and investigate the correlation between DG and functional properties affected by structural changes. The structural and functional properties of classical heating OVA, glycated OVA, ultrasonic treated OVA, and ultrasound-assisted glycated OVA were investigated to explore the interaction mechanism of ultrasound treatment on foaming and emulsifying properties improvement. Results indicated that the ultrasound assistance increased free sulfhydryl content, surface hydrophobicity and particle size of OVA-xylose conjugates, and thus enhancing the surface properties, which were strongly linear correlated with DG under different glycation parameters (pH, xylose/OVA ratio, heating time). Additionally, circular dichroism spectroscopy analysis revealed that ultrasound promoted the conversion of α-helices to β-sheets and unfolded structures, which was consistent with the formation of short amyloid-like aggregates that observed by atomic force microscopy phenomenon. Overall, our study provides new insights into the effects of ultrasound treatment on Maillard-induced protein functional properties enhancement, which may be a new strategy to tune the DG and functionality of protein-saccharide grafts during ultrasound processing.

Egg white proteins pose notable limitations in emulsion applications due to their inadequate wettability and interfacial instability. Polyphenol-driven alterations in proteins serve as an effective strategy for optimizing their properties. Herein, covalent and non-covalent complexes of egg white proteins-proanthocyanins were synthesized. The analysis of structural alterations, amino acid side chains and wettability was performed. The superior wettability (80.00° ± 2.23°) and rigid structure (2.95 GPa) of covalent complexes established favorable conditions for their utilization in emulsions. Furthermore, stability evaluation, digestion kinetics, free fatty acid (FFA) release kinetics, and correlation analysis were explored to unravel the impact of covalent and non-covalent modification on emulsion stability, dynamic digestion process, and interlinkages. Emulsion stabilized by covalent complex exhibited exceptional stabilization properties, and FFA release kinetics followed both first-order and Korsmeyer–Peppas models. This study offers valuable insights into the application of complexes of proteins-polyphenols in emulsion systems and introduces an innovative approach for analyzing the dynamics of the emulsion digestion process.