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The file available on this record is a proof of the front matter and contents only. You may purchase the ebook from the publisher, Mimesa Edizione, at https://www.mimesisedizioni.it/libro/9788857552224. Quali sono i videogiochi made in Italy? E che immagine dell'Italia forniscono? Il videogame nel Bel Paese esprime caratteri di cultura nazionale tanto nelle produzioni nostrane quanto nell'adattamento e nella ricezione culturale dei prodotti esteri. I contributi di questa raccolta, firmati da ricercatori italiani e internazionali, trattano della fruizione e della produzione italiana di questi prodotti, della rappresentazione del nostro Paese, delle relazioni tra giochi, fumetti, cinema, sport e brand nazionali, delle comunità di giocatori, critici e studiosi e del crescente riconoscimento istituzionale del medium come veicolo per la promozione del patrimonio storico-culturale. Prefazione di Peppino Ortoleva.

High-resolution proton nuclear magnetic resonance (H-1-NMR) spectroscopv (400-600 MHz) was applied to the quantitative analysis of hydroperoxide decomposition products in thermally oxidized oils, Different oils (olive, sunflower and soybean) were heated in a thermostatic bath (180 degrees C for 360 min). Proton NMR quantitative aldehyde analysis (n-alkanals, trans-2-alkenals, 4-hydroxy-trans-2-alkenals, alka-2,4-dienals) of fifteen oil samples (0, 60, 120, 240 and 360 minute heating) was compared with that of total polar compounds through silica column chromatography and of short-chain fatty acids. A good linear relationship (R-2 = 0.94) was found between the unsaturated aldehyde level and the amount of methyl-octanoate as well as between total aldehyde determined by H-1-NMR and total polar compounds (R-2 = 0.92). The same NMR sensitivity obtained at 400 MHz through 3000 scans was reached with only 64 scans for a total acquisition time of 2 min at 600 MHz. The potential use of H-1-NMR as a direct tool to monitor the quality and oxidative degradation in heated and fried oils is discussed.

he possibility of detecting extraneous milk in singles species cheese-milk has been explored. A mass spectrometry (MS)-based procedure has been developed to detect 'signature peptides', corresponding to the predefined subset of 'proteotypic peptides', as matchless analytical surrogates of the parent caseins. Tryptic digests of skimmed milk samples from four species were analyzed by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS. Amongst the candidate signature peptides that are able to differentiate milks from the four species, the alpha(s1)-casein (CN) f8-22 peptide was selected as a convenient marker for bovine, ovine and water buffalo milk while the f4-22 peptide was selected as a marker for the two caprine alpha(s1)-CN A and B variants, which differ by a Pro(16) (B)->Leu(16) (A) substitution. MALDI analysis of the digest allowed the detection of alpha(s1)-CN f8-22 and caprine f4-22. The accurate evaluation of caprine milk in a quaternary mixture required the development of a liquid chromatography/electrospray ionization (LC/ESI)-MS procedure. Five synthetic signature peptide analogues, which differed from their natural counterparts by a single amino acid substitution, were used as internal standards to quantify the alpha(s1)-CN, which was chosen as a reference milk protein, from the different species. The limits of detection were 0.5% (1% for caprine) for either the MALDI or the LC/ESI-MS method. The isotopic-label-free quantification of isoform- or variant-specific signature peptides has disclosed a convenient approach for targeting proteins in complex mixtures.

Current 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 alpha-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. The resistance of 25-mer, as well as that of the already described 33-mer related to the CD adaptive immune response, was confirmed on a standard flour wheat sample representative of the most widespread European varieties.

A mass spectrometric-based procedure for anthocyanin profiling was set up to distinguish authentic Vitis vinifera from hybrid red grapevine cultivars. 3-O-Monoglucoside and the related acetyl-, p-coumaryl- and caffeoyl-monoglucoside anthocyanins occurred only in Vitis vinifera, whereas 3,5-O-diglucoside and the substituted acetyl-, p-coumaryl-, feruloyl- and caffeoyl-diglucoside anthocyanins were the additional pigments in hybrid grapevines. The procedure was applied expressly to identify red grape cultivars based on the anthocyanin chemo-type determination. In particular, a red grape cultivar, having 3,5-O-diglucoside anthocyanins and a novel class of anthocyanin monoglucosides, such as cyanidin-3-O-, cyanidin-3-O-(6-O-acetyl)- and cyanidin-3-O-(6-O-p-coumaryl)pentoside, was classified as hybrid. A second vine cultivar, characterized exclusively by 3-O-monoglucoside anthocyanins, was included among the Vitis vinifera species. Anthocyanin profiling by mass spectrometry could represent the core of a chemotaxonomic procedure for distinguishing American and European grapevines based on the identification of post-synthetic anthocyanidin modification.

The alphas1-casein (alphas1-Cas) locus in the goat is characterized by a polymorphism, the main feature of which is to be qualitative as well as quantitative. A systematic analysis performed in an autochthon southern Italy breed identified a new rare allele (M), which was characterized at both the protein and genomic level. The M protein displays the slowest electrophoretic mobility of the alphas1-Cas variants described so far. MS and automated Edman degradation experiments showed that this behavior was due to the loss of two phosphate residues in the multiple phosphorylation site (64SP-SP-SP-SP-SP-E-70E) consecutively to a Ser-->Leu substitution at position 66 of the peptide chain (64S-SP-L-SP-SP-E-70E). This was confirmed by sequencing a genomic DNA fragment encompassing exon 9 where the 8th codon (TCG) was shown to be mutated to TTG. Sequencing of amplified genomic DNA segments spanning the 5' and 3' flanking regions of each exon allowed us to identify 23 single nucleotide polymorphisms and two insertion/deletion events in the coding as well as the noncoding regions. A comparison of specific haplotypes defined for each of the alphas1-CasF, A and M alleles indicates that the M allele probably arises from interallelic recombination between alleles A and B2, followed by a C-->T transition at nucleotide 23 of the ninth exon. The region encompassing the recombination break point was putatively located between nucleotide 86 upstream and nucleotide 40 downstream of exon 8. Interallelic recombination therefore appears to be a possible means of generating allelic diversity at the alphas1-Cas locus, at least in the goat. The previously proposed molecular phylogeny must now be revised, possibly starting from two ancestral allelic lineages.

Chantier qualité spécifique "Auteurs Externes" département de Génétique animale : uniquement liaison auteur au référentiel HR-Access; International audience

"Chantier qualité spécifique "Auteurs Externes" département de Génétique animale : uniquement liaison auteur au référentiel HR-Access "; International audience

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The primary structures of ovine alpha(s1)-casein variants A, C and D (formerly called Welsh variant) were determined. Separation of variants from whole casein was achieved using a fast and reliable reversed-phase HPLC method. Extended structural characterization of the purified proteins using electrospray mass spectrometry, automated Edman degradation and peptide mapping by means of HPLC-fast atom bombardment-mass spectrometry demonstrated that the mature protein was a mixture of two molecular species that differed in the deletion of residues 141-148 and were therefore 199 and 191. residues long respectively. The 199 residue peptide chain, which accounted for similar to 80% of the entire translated alpha(s1)-casein, was as long as its caprine and bovine counterparts, and had a 98 and 89% degree of identity with those two proteins respectively. Nine serine residues (positions 12, 44, 46, 64 to 68 and 75) were fully phosphorylated in alpha(s1)-casein A, whereas Ser(115) and Ser(41) were phosphorylated by similar to 50 and similar to 20% respectively. The differences between the three genetic variants A, C and D were simple silent substitutions, which however involved the degree to which the protein was phosphorylated. Variant C differed from variant A in the substitution Ser(13) --> Pro(13) which determined the loss of the phosphate group on site 12 of the protein chain, SerP(12) --> Ser(12). A further substitution, SerP(68) --> Asn(68) caused the disappearance of both phosphate groups in the phosphorylated residues Ser(64) and Ser(66) in variant D; in this last casein variant there was no evidence of phosphorylation at Ser(41).

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