Proteolysis of ß-Casein as a Marker of Grana Padano Cheese Ripening

¹ Inst. Pharmacological Sciences, University of Milan, Italy
² Inst. Microbiology, University of Brescia, Italy
³ Centro di Studio per l'Alimentazione degli, Animali in Produzione Zootecnica, Ivrea, Italy

Proteolysis has a critical role in defining the typical organoleptic characteristics of Grana Padano, a well-known Italian cheese. During the ripening process, hydrolysis of ß-casein produces different fragments, the most abundant and widely studied of which are -caseins, three polypeptides containing the HOOC-terminal portion of ß-casein. By sodium dodecyl sulfate-PAGE and a specific anti-ß-casein monoclonal antibody, two ß-casein-derived bands were identified in Grana Padano cheese: ß_a and ß_b. Thanks to the identification of the amino acid sequences, it was shown that: a) ß_a contains ₁-casein [ß-casein (29–209)] and the correlated peptide [ß-casein (30–209)]; b) ß_b contains ₂-casein [ß-casein (106–209)] and ₃-casein [ß-casein (108–209)].

The production of ß_a and ß_b by the three enzymes most involved in cheese proteolysis (pepsin, chymosin, and plasmin) was evaluated by performing in vitro digestions. A significant correlation between abundance of some polypeptides and ripening process was shown.

Key Words: ßbeta;-casein • grana cheese • proteolysis • ripening

Submitted on May 1, 2000
Accepted on July 13, 2000

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