Proteins may be classified as aerated dietary products based on their stability and foaming capability. When gas is disseminated in aqueous solutions to create foams, surface-active chemicals keep the bubbles from bursting. In our everyday activities, proteins and polyphenols are often combined. Sinapic acid (SA) is one of the most widely distributed polyphenols. It has been examined if the foam would remain stable when coupled with ovalbumin (OVA) and Sinapic acid (SA). The results of this study showed that polyphenols may be used in the food industry as a stabilizing agent to improve the functional characteristics of foam and provided some fundamental understanding of how polyphenols alter the foaming properties of OVA. UV-visible spectroscopy was used to study and characterize the relationship between ovalbumin and Sinapic acid .The experimental results indicated that the fluorescence quenching mechanism between Sinapic acid (SA) and ovalbumin (OVA) was static quenching which was proved again by the analysis of fluorescence lifetime by time resolved fluorescence Spectro fluorimeter .Utilizing FT-IR spectra, the structural and functional groups of the tyrosine (Try) and tryptophan (Trp) residues were also examined. The binding constant and the total number of SA binding sites on OVA were also determined in this research.