The sol-gel-sol transformation behavior of egg white proteins induced by alkali.

In the current study, we found an interesting phenomenon that fresh egg white (EW) undergo the sol-gel-sol transition with alkali treatment. The transformation behavior at different alkalinity (1.5%, 2.0%, and 2.5%) was investigated. As the gel formed, the hardness, lightness, surface hydrophobicity and the total number of identified peptides increased, and then, remarkable reduction when the gel collapsed. Rheological behavior indicated that the viscosity varied with shear rate. Fourier transform infrared spectroscopy (FTIR) showed that β-sheets gradually decreased as the α-helices increased during gel-sol transformation. The quantification of EW peptides analysis revealed that there was no dramatic correlation between the number of identified peptides and alkalinity. It was concluded that the sol-gel-sol transition was strongly dependent on alkali levels, moreover, high concentration promoted gel formation as well as liquefaction. The EW transformation behavior induced by alkali had a significant effect on protein aggregation and denaturation, and further changed physicochemical properties.