Thermal properties of globulin from buckwheat (Fagopyrum esculentum Moench)

Abstract

The thermal properties of buckwheat (Fagopyrum esculentum Moench) proteins with different lipid contents (2.5, 6.5 and 17.8%) were studied by differential scanning calorimetry (DSC) under various medium conditions. From DSC curves, many DSC characteristics including denaturation temperature (T d), enthalpy change (ΔH) and the width at half peak height (ΔT 1/2) of endothermic peaks were obtained and evaluated. The DSC curves of various buckwheat proteins (BWPs) in the 0.05 M phosphate buffer (pH 7.0) showed a major endotherm at about 102°C and a minor endotherm at about 80°C, attributed to thermal transitions of 13S and 8S globulins, respectively. T d and ΔH of the globulins of BWPs were independent of their lipid contents, while the presence of high lipid content (17.8%) to some extent increased the ΔT 1/2. The progressive increase in T d of 13S globulins with increase in NaCl concentration, suggests a more compact conformation with higher thermal stability. The influence of chaotropic salts on the DSC characteristics of 13S globulins was also independent of their lipid contents. Thermal analysis of the 13S globulins in the presence of protein perturbants (including urea, sodium dodecyl sulfate, ethylene glycol, dithiothreitol and N-ethylmaleimide) indicated that hydrophobic and hydrogen bondings are the major interactions for stabilizing protein conformation of buckwheat 13S globulins and the SS-SH interchange also attributes to the stabilization of the protein conformation.