Unfolding Kinetics of Egg Protein

This study explores denaturing kinetics of egg white using high resolution calorimetric technique. Fresh egg was scanned fro heating and cooling to see the thermodynamics 10$^{\circ}$ C to 100$^{\circ}$ C at different heating ramp rates varying from 1 to 20$^{\circ}$ C/min. An endothermic peak was found on heating scan showing denaturing of protein which was found absent at the cooling indicating the absence of any residue after heating. The denature peak shifted towards higher temperature as ramp rate increases following Arrhenius behavior and shows an activated denaturing kinetics of the egg protein. This peak was also compared with the water to avoid water effects. Behavior of denaturing peak can be explained in terms of Arrhenius theory.