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Thermal Denaturation of Pea Globulins (<i>Pisum sativum</i> L.)īøMolecular Interactions Leading to Heat-Induced Protein Aggregation
The heat-induced denaturation and aggregation of mixed
pea globulins
(8%, w/w) were investigated using differential scanning calorimetry
(DSC), SDS-PAGE, and size-exclusion chromatography (SEC-HPLC). DSC
data showed that the pea proteins denaturation temperature (<i>T</i><sub>d</sub>) was heating-rate dependent. The <i>T</i><sub>d</sub> value decreased by about 4 Ā°C by lowering the heating
rate from 10 to 5 Ā°C/min. The SDS-PAGE analysis revealed that
protein denaturation upon heating at 90 Ā°C was mainly governed
by noncovalent interaction. The SEC-HPLC measurements indicated that
low-denatured legumin (ā350ā410 kDa) and vicilin/convicilin
(ā170 kDa) globulins were heat-denatured and most of their
subunits reassociated into high-molecular weight, soluble aggregates
(>700 kDa). The addition of <i>N</i>-ethylmaleimide slightly
modified the aggregation route of pea globulins. However, partially
insoluble macroaggregates were produced in the presence of dithiothreitol,
reflecting the stabilizing effect of disulfide bonds within legumin
subunits