Abstract
ABSTRACTThe thermal behavior of oat globulin was studied by differential scanning calorimetry (DSC). The effects of pH, salts, and of various structure perturbants upon thermal characteristics were determined. Raising or lowering pH from near neutrality reduced denaturation temperature. (Td), enthalpy (ΔH) and cooperativity indicated by increase in width at half height (ΔT1/2). The effect of salts on thermal stability was related to their position in the lyotrophic series and suggests involvement of hydrophobic interaction in the thermal stability of oat globulin. Increasing concentrations of urea progressively lowered Td and ΔH and increased ΔT1/2; sodium dodecyl sulfate (SDS) lowered ΔH without affecting Td; ethylene glycol (EC) lowered Td without changing ΔH. Dithiothreitol did not affect DSC characteristics suggesting that disulfide bonds do not contribute to the thermal response of oat globulin.
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