Impact of pH and Sucralose on the Non-Covalent Interaction of Ovalbumin: FT-IR Analysis

Analysis of pH and cosolvent effects on protein structure is a popular study in food biophysics research since the function of protein is primarily dependent on its structure. The structure-function relationship of protein could be well reflected in changes in non-covalent interactions of protein. In this aspect, the present work deals with the Fourier transform infrared (FT-IR) spectroscopy analysis of ovalbumin (OVA) in different pH conditions with and without cosolvent sucralose (SUC) inclusion. The FT-IR spectrum of proteins provides an absorption spectrum in the frequency region of 4000-400 cm-1. These absorption bands consist of amide A, amide B, and amide I to amide VII. The results are interpreted in terms of noncovalent interactions, such as van der Waals interactions, hydrogen bonds, and hydrophobic and electrostatic interactions. The obtained results indicate that OVA is denatured from its native state against pH and SUC inclusion.