Studies of Thermal Denaturation of Oat Globulin by Differential Scanning Calorimetry

Thermal denaturation of oat globulin was studied by differential scanning calorimetry (DSC). Prior heat treatments at 100°C and 110°C resulted in a progressive decrease in enthalpy (ΔH) indicating partial denaturation. Marked increase in denaturation temperature (T d ) and onset temperature (T m ) and decrease in width at half peak height (ΔT 1/2 ) suggest that the preheated protein assumed a more compact conformation or associated to a complex structure with higher thermal stability and cooperativity. The heated globulin was segregated into soluble and insoluble fractions containing native and denatured protein respectively. The denaturation kinetics of oat globulin was studied and results show a reaction order of 2.5 and an activation energy of 505 KJ/mol. Heat treatments caused a pronounced increase in activation energy and pre‐exponential factor.