Heat treatmentsThermal 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 (AH) indicating partial denaturation. Marked increase in denaturation temperature (Td) and onset temperature (T,) and decrease in width at half peak height (ATr,,) 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.Oat globulin was heated at either 100°C or 110°C in O.OlM phosphate buffer (pH 7.4) containing l.OM NaCI. The temperatures and buffer were chosen such that the results can be compared directly with previous data on thermal coagulation of oat globulin . One milligram (2 0.05 mg) freeze-dried protein was weighed to polymer-coated DSC pan (DuPont Co., Wilmington, DE) and 10 )LL buffer were added without mixing. The pan was sealed with a lid and heated on the reference or sample platform of a DuPont DSC high pressure cell preset at 100" or 110°C. Since the sample size (1 mg protein in 10 pL buffer) was small and the solids were evenly distributed on the bottom of the pan, the lags between recorded and actual sample temperatures should be small. After heating for the prescribed time, the pan was cooled rapidly in an ice bath, and reequilibrated to room temperature.