Thermal Denaturation of Pea Globulins (<i>Pisum sativum</i> L.)—Molecular Interactions Leading to Heat-Induced Protein Aggregation - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Agricultural and Food Chemistry Année : 2013

Thermal Denaturation of Pea Globulins (Pisum sativum L.)—Molecular Interactions Leading to Heat-Induced Protein Aggregation

Résumé

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 (T d) was heating-rate dependent. The T d value decreased by about 4 °C by lowering the heating rate from 10 to 5 °C/min. The SDS-PAGE analysis revealed that protein denaturation upon heating at 90 °C was mainly governed by noncovalent interaction. The SEC-HPLC measurements indicated that low-denatured legumin (≈350−410 kDa) and vicilin/convicilin (≈170 kDa) globulins were heat-denatured and most of their subunits reassociated into highmolecular weight, soluble aggregates (>700 kDa). The addition of N-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.
Fichier non déposé

Dates et versions

hal-04234483 , version 1 (29-11-2023)

Identifiants

Citer

Jean-Luc Mession, Nicolas Sok, Ali Assifaoui, Rémi Saurel. Thermal Denaturation of Pea Globulins (Pisum sativum L.)—Molecular Interactions Leading to Heat-Induced Protein Aggregation. Journal of Agricultural and Food Chemistry, 2013, 61 (6), pp.1196-1204. ⟨10.1021/jf303739n⟩. ⟨hal-04234483⟩
4 Consultations
1 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More