Impact of cosolvent (glucose) on the stabilization of ovalbumin

Proteins are stabilized by glucose against denaturation due to extremes of pH. This was studied by means of density, ultrasonic velocity, viscosity and surface tension measurements in the ovalbumin (5 mg/ml) dissolved in phosphate buffer (pH 2, 5, 7, 9 and 12). Few thermo-acoustical parameters such as adiabatic compressibility, intermolecular free length, acoustic impedance, the partial apparent specific volume and the partial apparent specific adiabatic compressibility were calculated for the said systems. Obtained results suggest that the stabilization of ovalbumin occurs in the presence of glucose through strengthening of hydrophobic interactions supported by other non-covalent interactions and the steric exclusion effect of the cosolvent molecules.

Graphical abstractExtreme pH denaturizes ovalbumin and the addition of glucose stabilizes it.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Ovalbumin is characterized ultrasonically at various pH values at room temperature. ► Impact of glucose in stabilizing the ovalbumin against pH denaturation is analyzed. ► Presence of strong and weak interactions are simultaneously noticed in the systems.