Molecular structural modification of egg white protein by pH-shifting for improving emulsifying capacity and stability

Abstract The effect of pH-shifting on the molecular structure and emulsifying properties of egg white protein (EWP) was investigated. EWP was subjected to extreme alkaline pH treatment (11, 11.5, 12, 12.5, and 13) and then adjusted to neutral (pH 7.0). The results showed that the emulsifying activity and emulsion stability of EWP were enhanced under pH-shifting, especially at pH 13. The surface hydrophobicity of EWP13 increased significantly from 306.94 to 11653.67 (p