ELISA for monitoring the cleavage of β-casein at site Lys<sup>28</sup>–Lys<sup>29</sup> by plasmin during Comté cheese ripening - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Access content directly
Journal Articles Journal of Dairy Research Year : 2002

ELISA for monitoring the cleavage of β-casein at site Lys28–Lys29 by plasmin during Comté cheese ripening

Abstract

Proteolysis of casein is the principal cause of textural changes and flavour development in ripened cheese (Fox & McSweeney, 1996). Caseins are degraded into small peptides and free amino acids during a complex process, described by Grappin et al . (1985) as a two-step scheme. Caseins are initially broken down into large, well characterised fragments. This initial step, called primary proteolysis, is catalysed principally by the residual coagulant (chymosin and pepsin), and to a variable extent by endogenous milk proteases, such as plasmin, cathepsin D, and possibly somatic cell proteinases. Enzymes originating from either rennet or milk are active in most ripened cheese varieties. However, their relative contributions vary substantially depending on manufacturing practices. For instance, in Swiss-type cheeses, cooking the curd extensively inactivates the coagulant, and simultaneously enhances plasmin activity, which therefore becomes predominant (Ollikainen & Kivela, 1989).
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Dates and versions

hal-04304019 , version 1 (24-11-2023)

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Daniel Senocq, Didier Dupont, Odile Rolet-Répécaud, Didier Levieux. ELISA for monitoring the cleavage of β-casein at site Lys28–Lys29 by plasmin during Comté cheese ripening. Journal of Dairy Research, 2002, 69 (3), pp.491 - 500. ⟨10.1017/s0022029902005587⟩. ⟨hal-04304019⟩

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