Casein phosphopeptides (CPP) which develop in Grana Padano cheese at different ages were isolated by precipitation with Ba2+ and analysed by HPLC. Profiles were complex throughout the period between 4 and 38 months. CPP in a cheese sample 14 months old were identified by a combination of fast atom bombardment-mass spectrometry and Edman degradation. They were found to consist of a mixture of components derived from three parent peptides, β-CNf(7-28)4P, α(s1)-CNf(61-79)4P and α(s2)-CNf(7-21)4P. In total, 45 phosphopeptides were identified: 24 from α-CN, 16 from α(s1)-CN and 5 from α(s2)-CN. The presence of aminopeptidase activity during cheese ripening was deduced from the presence of a number of CPP of different lengths with the loss of one or more residues from the N-terminus. The longest had C-terminal lysine and seemed to be progressively hydrolysed by carboxypeptidases A and B to shorter peptides. CPP in cheese appeared to be shortened plasmin-mediated products. Moreover, those most resistant to further hydrolysis contained at least three closely located phosphoserine residues. The anticariogenic activity of CPP is also discussed.

Phosphopeptides from Grana Padano cheese: nature, origin and changes during ripening / P. Ferranti, F. Barone, L. Chianese, F. Addeo, A. Scaloni, L. Pellegrino, P. Resmini. - In: THE JOURNAL OF DAIRY RESEARCH. - ISSN 0022-0299. - 64:4(1997), pp. 601-615.

Phosphopeptides from Grana Padano cheese: nature, origin and changes during ripening

L. Pellegrino
Penultimo
;
P. Resmini
Ultimo
1997

Abstract

Casein phosphopeptides (CPP) which develop in Grana Padano cheese at different ages were isolated by precipitation with Ba2+ and analysed by HPLC. Profiles were complex throughout the period between 4 and 38 months. CPP in a cheese sample 14 months old were identified by a combination of fast atom bombardment-mass spectrometry and Edman degradation. They were found to consist of a mixture of components derived from three parent peptides, β-CNf(7-28)4P, α(s1)-CNf(61-79)4P and α(s2)-CNf(7-21)4P. In total, 45 phosphopeptides were identified: 24 from α-CN, 16 from α(s1)-CN and 5 from α(s2)-CN. The presence of aminopeptidase activity during cheese ripening was deduced from the presence of a number of CPP of different lengths with the loss of one or more residues from the N-terminus. The longest had C-terminal lysine and seemed to be progressively hydrolysed by carboxypeptidases A and B to shorter peptides. CPP in cheese appeared to be shortened plasmin-mediated products. Moreover, those most resistant to further hydrolysis contained at least three closely located phosphoserine residues. The anticariogenic activity of CPP is also discussed.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/197553
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