Interactions in casein micelle – Pea protein system (part I): Heat-induced denaturation and aggregation

Abstract : 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.
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Food Hydrocolloids, Elsevier, 2017, 67, pp.229 - 242. 〈10.1016/j.foodhyd.2015.12.015〉
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https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01533202
Contributeur : Pam - Université de Bourgogne <>
Soumis le : mardi 6 juin 2017 - 10:30:04
Dernière modification le : jeudi 11 octobre 2018 - 12:01:17

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Jean-Luc Mession, Sébastien Roustel, Rémi Saurel. Interactions in casein micelle – Pea protein system (part I): Heat-induced denaturation and aggregation. Food Hydrocolloids, Elsevier, 2017, 67, pp.229 - 242. 〈10.1016/j.foodhyd.2015.12.015〉. 〈hal-01533202〉

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