The preserved eggs were processed by immersion method. The effect of internal interactions on the formation of egg yolk gel during salting and ageing were determined by fluorescence spectrophotometer and FTIR et al. The sum of α-helical and β-turn of the secondary structure of the exterior egg yolk protein decreased by 54.71% under strong alkaline environment, with the surface hydrophobicity decreased significantly (P＜0.05), and the dramatic increase of ion bonds and disulfide bonds promoted the egg yolk proteins to form a gel. The sum of α-helical and β-turn of the secondary structure of the interior egg yolk protein increased by 54.05%, and the changes of surface hydrophobicity was not obviously (P＞0.05). The obvious increase of hydrophobic interaction and disulfide bond caused the interior egg yolk to transform into the exterior egg yolk gradually, which also enhanced the gel strength of the egg yolk. The result of gel electrophoresis showed that the exterior egg yolk protein was alkaline denatured earlier than interior egg yolk, and the more stable protein was high-density lipoprotein.