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TAG from collision-induced fragments; bromination allowed clear separation of saturated and unsaturated TAG.Differences in the fatty acid composition amongst homologous isobaric TAG of different structures wereidentified by post-source decay analysis of hydrogenated precursors. MALDI-TOF has proven advantageous forsimultaneously detecting TAG at various unsaturation degrees within different TAG classes (Cn). The dataprovide insight into animal fat differentiation on a molecular basis, increasing the analytical description to a newlevel, proving the so far underestimated capacity of MALDI-TOF MS in this field.2. Mamone G, Ferranti P, Rossi M, Roepstorff P, Fierro O, Malorni A, Addeo F. Identificationof a peptide from alpha-gliadin resistant to digestive enzymes: implications for celiac disease.J Chromatogr B Analyt Technol Biomed Life Sci. 15;236-241, 2007Current knowledge indicates that both innate and adaptive immune responses are involved in Celiac disease(CD) driven by different gliadin peptides. By studying a representative recombinant -gliadin form, a further 25-mer peptide resistant to gastric, pancreatic, and human intestinal brush-border membrane enzymes was detected.This peptide latter encompasses the sequence 31–43 known to elicit the innate immune response in CD. Theresistance of 25-mer, as well as that of the already described 33-mer related to the CD adaptive immuneresponse, was confirmed on a standard flour wheat sample representative of the most widespread Europeanvarieties.3. Caira S, Calabrese Mg, Lilla S, Vangone P, Nicolai Ma, Chianese L, Addeo F. Milk proteinsand their antigenicity . In Immunochemistry in Dairy Research, pp. 1-35, 2006 (ResearchSignpost Rosa Pizzano Editor)The main elements of milk proteins can be summarized as follows: variable phosphorylation degree of the fourcaseins, variable glycosylation of κ-CN and α-La, frequent presence of casein peptides generated by the action ofendogenous and bacterial enzymes, wide molecular mass range whey proteins, easy thermodenaturation of wheyproteins. With more knowledge of the primary structure, the location of the phosphate groups on the caseinchains, and intra-and inter-protein disulphide bond exchanges during milk processing, particularly duringdigestion by proteolytic enzyme, the function and the role of most important milk proteins are now betterunderstood. Further insight into the basic properties of milk proteins should lead to a greater understanding ofthe natural function of milk and the roles its components play in human nutrition. In this paper milk proteins arereviewed in the perspective of preventing milk allergies in newborns.4. Pizzano R, Manzo C, Nicolai Ma, Addeo F. Detection of milk protein adducts using antipeptideantibodies. In Ibidem, pp. 121-131, 2006The anti-peptide antibody technology was exploited in order to obtain immunochemical reagents for detectingprotein adducts arising in milk owing to heat treatments or exposure to formaldehyde. Properly designedpeptides, mimicking the novel structures of the protein adducts, were used as model antigens. The polyclonalantibodies raised against these peptides recognized effectively the targeted structures in the protein adducts and,moreover, they proved to be able to distinguish modified from native protein components in milk and cheesesamples.5. Addeo F, Caira S, Chianese L, Lilla S. Bioactive peptides from milk proteins. Focus onphosphopeptides and enzyme mediated casein peptides. In Microorganisms as healthsupporters. Probiotics and bioactive peptides. The new Biotherapeutic Frontier, pp. 206-326,2007 (MOFIN-ALCE Editor, Novara)The casein proteolysis gives rise to bioactive peptides that have special physiological functions. Bioactivity ofthe peptides encrypted in milk proteins is latent until they are released and activated by enzyme hydrolysis.Many milk-derived peptides have revealed multi-functional properties in the sense that two or more differentbiological effects are exerted by single peptide sequences. These overlapping primary structures of caseins havebeen also defined as strategic zones because they seem to be intrinsically protected from proteolytic digestions.SISTAL - SOCIETA’ ITALIANA DI SCIENZE E TECNOLOGIE ALIMENTARIDipartimento di Scienze e Tecnologie Agroalimentari, Università degli Studi della TusciaVia San Camillo de Lellis, 01100 ViterboTel.: 0761- 35 74 94/7 , Fax: 0761- 35 74 98, e-mail: mmoresi@unitus.it270