Divalent metal ions under low concentration environment improved the thermal gel properties of egg yolk

) and apparent viscosity of egg yolk, destroying the disulfide bonds and the hydrophobic interactions in gel. Fourier transform infrared spectroscopy (FT-IR) and fluorescence spectra analysis revealed that metal ions promoted the hydrophobic aggregation among egg yolk proteins and induced the transition of protein secondary structure from ordered to disordered. This work will provide a theoretical reference for the development of low salt and nutrient fortified egg yolk products.