Uncommonly thorough hydrolysis of peptides during ripening of Ragusano cheese revealed by tandem mass spectrometry
2011
Gagnaire , Valérie (INRA , Rennes (France). UMR 1253 Science et Technologie du Lait et de l'Oeuf) | Carpino , Stéfania (CorFilac, Ragusa(Italie). Ragusa Mare) | Pediliggieri , Concetta (CorFilac, Ragusa(Italie). Ragusa Mare) | Jardin , Julien (INRA , Rennes (France). UMR 1253 Science et Technologie du Lait et de l'Oeuf) | Lortal , Sylvie (INRA , Rennes (France). UMR 1253 Science et Technologie du Lait et de l'Oeuf) | Licitra , Giuseppe (CorFilacCatania University, RagusaCatania, Sicile(Italie). Ragusa MareDepartment of Agriculture and Food Production Science)
Ragusano is a pasta filata cheese produced from raw milk in Sicily. The proteolysis was extensively analyzed after stretching (day 0), at 4 and 7 months of ripening through soluble nitrogen, urea-PAGE, and peptide identification by tandem mass spectrometry. After stretching, 123 peptides were identified: 72 arising from β-casein, 34 from αs1-casein, and 17 from αs2-casein. The main protein splitting corresponded to the action of plasmin, chymosin, cathepsin D, cell envelope proteinase, and peptidase activities of lactic acid bacteria. Unlike other types of cheeses, <10% residual β- and αs-caseins remained intact at 7 months, indicating original network organization based on large casein fragments. The number of identified soluble peptides also dramatically decreased after 4 and 7 months of ripening, to 47 and 25, respectively. Among them, bioactive peptides were found, that is, mineral carrier, antihypertensive, and immunomodulating peptides and hosphopeptides.
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