Peptide bonds cleaved by pepsin are affected by the morphology of heat-induced ovalbumin aggregates - Université Rennes 2 Accéder directement au contenu
Article Dans Une Revue Food Chemistry Année : 2024

Peptide bonds cleaved by pepsin are affected by the morphology of heat-induced ovalbumin aggregates

Résumé

The study aimed to assess the extent to which protein aggregation, and even the modality of aggregation, can affect gastric digestion, down to the nature of the hydrolyzed peptide bonds. By controlling pH and ionic strength during heating, linear or spherical ovalbumin (OVA) aggregates were prepared, then digested with pepsin. Statistical analysis characterized the peptide bonds specifically hydrolyzed versus those not hydrolyzed for a given condition, based on a detailed description of all these bonds. Aggregation limits pepsin access to buried regions of native OVA, but some cleavage sites specific to aggregates reflect specific hydrolysis pathways due to the denaturation-aggregation process. Cleavage sites specific to linear aggregates indicate greater denaturation compared to spherical aggregates, consistent with theoretical models of heat-induced aggregation of OVA. Thus, the peptides released during the gastric phase may vary depending on the aggregation modality. Precisely tuned aggregation may therefore allow subtle control of the digestion process.
Fichier principal
Vignette du fichier
article pour affichagesuwareh et al 2024.pdf (2.32 Mo) Télécharger le fichier
Origine Fichiers produits par l'(les) auteur(s)
Licence

Dates et versions

hal-04630049 , version 1 (01-07-2024)

Licence

Identifiants

Citer

Ousmane Suwareh, David Causeur, Steven Le Feunteun, Julien Jardin, Valérie Briard-Bion, et al.. Peptide bonds cleaved by pepsin are affected by the morphology of heat-induced ovalbumin aggregates. Food Chemistry, 2024, 458, pp.140260. ⟨10.1016/j.foodchem.2024.140260⟩. ⟨hal-04630049⟩
0 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Mastodon Facebook X LinkedIn More