Proteomic profiling of camel and cow milk proteins under heat treatment

Imène Felfoul (1, 2) , Julien Jardin (1) , Frederic Gaucheron (1) , Hamadi Attia (2) , M.A. Ayadi (2)

1 STLO - Science et Technologie du Lait et de l'Oeuf
2 LAVASA - Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d’Ingénieurs de Sfax

Cow and camel milk proteins before and after heat treatment at 80 C for 60 min were identified using LC/ MS and LC–MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80 C for 60 min, camel a-lactalbumin (a-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80 C for 60 min, a-lactalbumin (a-la) and b-lactoglobulin (b-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC–MS/MS. Casein fractions were kept intact under a heat treatment of 80 C during 60 min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80 C for 60 min.

Mots clés: traitement thermique; lait de chamelle; protéomique; protéine de lait; électrophorèse

Domaines: Alimentation et Nutrition; Ingénierie des aliments

Imène Felfoul, Julien Jardin, Frederic Gaucheron, Hamadi Attia, M.A. Ayadi. Proteomic profiling of camel and cow milk proteins under heat treatment. Food Chemistry, 2017, 216, pp.161-169. ⟨10.1016/j.foodchem.2016.08.007⟩. ⟨hal-01356901⟩