Interactions in casein micelle Pea protein system (part I) : Heat-induced denaturation and aggregation
Mession, J.-L.; Roustel, S.; Saurel, R.
Food Hydrocolloids 67: 229-242
The aim of this work was to investigate the heat-induced interactions between pea proteins (vicilin 7S or legumin 11S enriched-fractions) in admixture with suspended casein micelles (SCM), at weight protein ratio of 1:1 and pH 7.1. The single-protein samples and mixtures thereof were prepared at concentrations of 18 and 36 mg(protein)/g(sample), respectively, then heated from 40 to 85 degrees C and incubated for 0-60 min. As compared to single-protein samples, differential scanning calorimetry (DSC) data indicated that the denaturation temperature of pea proteins increased of about 4 degrees C in the presence of SCM. Heat-induced change in protein composition of the soluble (SP) and micellar (MP) phases from centrifuged SCM pea protein mixture was assessed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and densitometry. Likewise SP was analyzed by size-exclusion chromatography (SEC-HPLC). While pea legumin 11S and vicilin 7S oligomers were markedly sedimentable in MP from their respective unheated mixture, thermal denaturation and protein aggregation (>= 75 degrees C) resulted in increasing levels of dissolved pea proteins in SP. Heating of the SCM legumin mixture (85 degrees C, 15-60 min incubation) resulted in the dissociation of the legumin subunits L-alpha beta into acidic Le and basic L-beta polypeptides, yielding in comparable amounts soluble and insoluble disulfide-bonded aggregates, respectively. In contrast in the SCM vicilin mixture, the heat-denatured vicilin polypeptides in a temperature range of 70-80 degrees C produced in majority soluble and non-covalent aggregates. Though the heat-induced interactions between pea proteins were altered in the presence of micelles, caseins would not be involved into pea proteins aggregation.