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Article Dans Une Revue Journal of Agricultural and Food Chemistry Année : 2011

Uncommonly thorough hydrolysis of peptides during ripening of Ragusano cheese revealed by tandem mass spectrometry

Résumé

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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hal-01454142 , version 1 (29-05-2020)

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Valérie Gagnaire, Stéfania Carpino, Concetta Pediliggieri, Julien Jardin, Sylvie Lortal, et al.. Uncommonly thorough hydrolysis of peptides during ripening of Ragusano cheese revealed by tandem mass spectrometry. Journal of Agricultural and Food Chemistry, 2011, 59 (23), pp.12443-12452. ⟨10.1021/jf2027268⟩. ⟨hal-01454142⟩
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