Non-isothermal unfolding/denaturing kinetics of egg white protein

Egg protein is an important part of our food to get protein in our daily diet, and makes this protein more important to researchers to understand its kinetic behavior to understand the energy involved in the digestion of the egg protein. Hence, the present study explores the denaturing kinetics of the protein obtained from the hen's egg white (EW) using high resolution calorimetric technique. Fresh EW was scanned for heating and cooling to see the thermodynamics from 10 to 100 A degrees C at different heating ramp rates varying from 1 to 20 A degrees C min(-1). 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 and further discussed to get the energy involved in digestion.