Effect of enzymatic hydrolysis on characteristics and synergistic efficiency of pectin on emulsifying properties of egg white protein

Egg white protein is a kind of protein resource with distinctive nutritional value and functional properties, while performing weak emulsifying stability under neutral and alkaline conditions, limiting application in food industry. This study, we investigated the effect of enzyme on characteristics of egg white protein (EWP) and synergistic efficiency of pectin addition on properties (thermal stability, salt resistance and antioxidant activity) of emulsions stabilized by original or hydrolyzed EWP. The EWP solutions were incubated at pH 7.0, under 50 °C for 2 h, with various amount of enzyme (0%, 0.5%, 1%, 2%, and 4%) added in. With enzyme concentration increased, more ovotransferrin and ovalbumin were hydrolyzed, and more hydrophobic amino acids exposed to polar environment, especially tyrosine. In addition, the DPPH and ABTS radical scavenging activity of EWP increased with enzyme concentration increased. Pectin addition can effectively improve the stabilization of the emulsion droplets, inducing smaller effective diameter and polydispersity index. In comparison, the emulsions stabilized by hydrolyzed EWP with 0.3% pectin behaved better thermal and salty stability, while with poorer antioxidant capacity attributed to weaker intermolecular interactions. The rheological measurement showed that the viscosity of hydrolyzed EWP stabilized emulsion was relatively lower and G′ was more dependent on frequency, indicating weaker cross-links among droplets. The results may provide theoretical guidance for application of enzymatic and polysaccharide blends in improving protein functionality.