Fac-simile Scheda Linee di Ricerca - Federalimentare

Dati pubblicati inerenti il tema di ricerca:1. Chianese L, Quarto M, Pizzolongo F, Calabrese Mg, Caira S, Mauriello R, De Pascale S,Addeo F. Occurrence of genetic polymorphism at the α s1 -CN locus in Mediterranean waterbuffalo milk. International Dairy Journal 19:181-1899, 2009A study on casein genetic polymorphism in water buffalo milk of Mediterranean breed, reared in Southern Italy,was carried out by means of immunoelectrophoretic and chromatographic techniques coupled with mass spectrometryanalysis. When compared with reference α s1 -CN variant A, the results showed the occurrence of a newas1-casein (α s1 -CN) B genetic variant having a single silent amino acid substitution Leu 178 (A)/Ser 178 (B). InMediterranean buffalo milks the allelic frequency of new α s1 -CN B was very similar to that determined in Mozzarelladi bufala campana (MBC), a Protected Denomination of Origin (PDO) cheese, made exclusively fromwhole raw buffalo milk of this breed. The relative percentage of the two α s1 -CN variants, either in bulk milk orMBC cheese, can be used in defining the authenticity of PDO MBC cheese.2. Somma A, Ferranti P, Addeo F, Mauriello R, Chianese L. A peptidomic approach based oncombined capillary isoelectric focusing and mass spectrometry analysis for the characterizationof the plasmin primary products from bovine and water buffalo β-casein. J ChromatographyA 1192:294-300, 2008The main peptides produced by hydrolysis of water buffalo β-casein with plasmin were characterized by capillaryelectrophoresis and mass spectrometry and compared with their bovine homologous. A novel breakdownproduct arising from the hydrolysis of water buffalo β-casein, originated by the presence of a plasmin-sensitiveLys bond at position 68 was identified, which was not present in bovine β-casein. On the basis of this evidence,an improved procedure for the detection and the differentiation of the products of plasmin hydrolysis of bovineand water buffalo β-casein by capillary soelectric focusing was set-up. In the experimental conditions, the β-casein from the two species was efficiently separated. Comparison of the capillary electropherograms with thoseobtained by ultra-thin-layer isoelectric focusing, the reference method for routine analysis of plasmin digests ofcasein, suggests that capillary electrophoresis isoelectric focusing may constitute a successful alternative to thetraditional slab gel electrophoresis analysis of plasmin digests of casein either for basic structural studies or forapplications in the quality assessment of dairy products.3. Pirisi A, Pinna G, Addis M, Piredda G, Mauriello R, De Pascale S, Addeo F, Chianese L. Relationshipbetween the enzymatic composition of lamb paste rennet and proteolytic and lypoliticpattern and texture of PDO Fiore Sardo cheese. Int. Dairy Journal 17:143-156, 2007Two types of lamb rennet pastes, traditional (A) and industrial (B), were used for making two types of PDOFiore Sardo cheese (FSA and FSB) to ascertain the influence of their use on cheese characteristics. Traditionalrennet was produced from the stomachs of lambs fed only milk and slaughtered, after suckling, on a full stomach.Industrial rennet was produced from the stomachs of lambs weaned and slaughtered on an empty stomach.The cheeses were significantly different (P