Details

Autor(en) / Beteiligte

• Gagnaire, Valérie
• Carpino, Stefania
• Pediliggieri, Concetta
• Jardin, Julien
• Lortal, Sylvie
• Licitra, Giuseppe

Titel

Uncommonly Thorough Hydrolysis of Peptides during Ripening of Ragusano Cheese Revealed by Tandem Mass Spectrometry

Ist Teil von

• Journal of agricultural and food chemistry, 2011-12, Vol.59 (23), p.12443-12452

Ort / Verlag

Washington, DC: American Chemical Society

Erscheinungsjahr

2011

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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 phosphopeptides.