title: Thermal denaturation of pea globulins (Pisum sativum L.)-molecular interactions leading to heat-induced protein aggregation.
abstract: 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 high-molecular 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.
authors.affiliation: Agrosup Dijon, UMR PAM 02.102 , Equipe PAPC (Procédés Alimentaires et PhysicoChimie), 1 Esplanade Erasme, 21000 Dijon, France. jeanluc.mession@laposte.net
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Mession
authors.forename: Nicolas
authors.initials: N
authors.lastname: Sok
authors.forename: Ali
authors.initials: A
authors.lastname: Assifaoui
authors.forename: Rémi
authors.initials: R
authors.lastname: Saurel
mesh_terms: D002152:Calorimetry, Differential Scanning; D004591:Electrophoresis, Polyacrylamide Gel; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D018532:Pisum sativum / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D005916:Globulins; D010940:Plant Proteins