Deamidation post-translational modification in naturally generated peptides in Spanish dry-cured ham

•A peptidomic approach to identify deamidated peptides in dry-cured ham.•282 peptides showing deamidation from a total of 2118 peptides derived from major muscle proteins.•Deamidation was not influenced by the type of muscle but by salt, pH and temperature. A large number of peptides are generated d...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Food chemistry 2017-08, Vol.229, p.710-715
Hauptverfasser: Cañete, Manuel, Mora, Leticia, Toldrá, Fidel
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:•A peptidomic approach to identify deamidated peptides in dry-cured ham.•282 peptides showing deamidation from a total of 2118 peptides derived from major muscle proteins.•Deamidation was not influenced by the type of muscle but by salt, pH and temperature. A large number of peptides are generated during the processing of dry-cured ham that can be affected by post-translational modifications (PTM). One of the most studied PTMs is the oxidation of susceptible residues but other modifications such as deamidation have been scarcely reported in the literature. This work has been focused on the impact of deamidation in those peptides generated in 12-months dry-cured hams. The results obtained in Biceps femoris and Semimembranosus muscles showed that 52% and 48% of the identified peptides, respectively, were affected by PTMs, with a total of 277 and 282 sequences showing deamidation in both muscles, respectively. It appears that deamidation is not influenced by the type of muscle but is probably favored by characteristic processing conditions like temperature, pH, and salting of hams. The knowledge of the affected sequences provides novel information for a better characterisation of proteolysis phenomena during the processing of dry-cured ham.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2017.02.134