Spectroscopic Approaches To Define The Interaction Between Gallic Acid And Ovalbumin

Abstract

Foaming capacity and stability are important characteristics for determining proteins as aerated food items. Surface-active chemicals stabilize the bubbles in foams, in which gas are distributed in aqueous solutions. Protein-polyphenol combinations are common in our routines. Gallic acid (GA) is one of the most abundant polyphenols. An attempt has been made for the stability of the foam in combination with ovalbumin (OVA) and Gallic acid. The results of this study provided some fundamental information on how polyphenols influence the foaming properties of OVA, and proved that polyphenols can be used as stabilizing agent in food industry to improve the functional properties of foam. The interaction between Gallic acid (GA) and ovalbumin (OVA) were studied and characterized by Ultraviolet-visible (UV–Vis). The conformation changes have been noted and quenching the mechanism between Gallic acid (GA) and ovalbumin (OVA) proved to be static quenching by fluorescence. Tryptophan (Trp) residues quenches vibrantly than Tyrosine (Try) which were analyzed by synchronous and the structural and functional group analyzed by FT-IR spectrum. The binding constant and the number of binding sites for GA on OVA were also calculated in this study.