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

J Agric Food Chem

UMR 1253, INRA, Science et Technologie du Lait et de l'Œuf, 65 rue de Saint Brieuc, F-35042 Rennes, France.

Published: December 2011

AI Article Synopsis

  • Ragusano cheese is a pasta filata variety made from raw milk in Sicily, which undergoes proteolysis analyzed at different ripening stages.
  • The analysis identified 123 peptides immediately after stretching, with a significant reduction in peptide quantity over 7 months, mainly due to the action of specific enzymes and bacteria.
  • Less than 10% of the original caseins remained intact after 7 months of ripening, indicating a unique protein structure, with some peptides exhibiting bioactive properties like mineral carrying and antihypertensive effects.

Article Abstract

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 α(s1)-casein, and 17 from α(s2)-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 α(s)-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.

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Source
http://dx.doi.org/10.1021/jf2027268DOI Listing

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