During the egg storage, the change in structure of ovalbumin (OVA) was determined by spectroscopy of Fluorescence, Circular Dichroism and Fourier-Transform Raman. The relationships between the OVA properties and structure were also investigated in this study. Comparing with the consequence of Circular Dichroism and Fourier-Transform Raman spectra, it was obvious that the percentage of alpha-helix and beta-sheet showed downward trends after storage. In contrast, the percentage of beta-turn and random coil clearly presented raising trend. Furthermore, tryptophan residues were buried in a more hydrophobic environment. The emulsifying and foaming properties of OVA all decreased during the storage. Moreover, the correlation analysis indicated that beta-sheet related to the emulsifying stability of OVA (p < 0.01), a helix related to the foaming stability (p < 0.05) at the same time. This study provided new interesting idea for the study on the relationships between the structure and functional properties of protein during food storage. (C) 2017 Elsevier Ltd. All rights reserved.