Fatty acid profile, oxidative status, and content of volatile organic compounds in raw and cooked meat of different chicken strains.

Chicken meat is rich in unsaturated fatty acids. Therefore, it is more susceptible to lipid oxidation and production of volatile organic compounds (VOC). In this study, we evaluated the fatty acids, antioxidants, and VOC profiles of raw and cooked meat samples derived from 4 strains of chicken differing in their growth rates, which were as follows: slow-growing (SG, Leghorn), medium-growing (MG, Hubbard and Naked Neck), and fast-growing (FG, Ross). The VOC profile of meat was measured using proton-transfer reaction-mass spectrometry (PTR-MS). The VOC were identified using PTR-time of flight-MS (PTR-ToF-MS). The data were analyzed using both univariate and multivariate models. Twenty main VOC were identified, which were classified into the following chemical categories: aldehydes, alkadienes, alkenes, furans, amides, alcohols, and other compounds. Our results revealed that the chicken genotype and the method of cooking strongly influenced the VOC profile of the meat. Identifying the relationships between these traits allowed us to highlight the trade-off of the main substrates such as n-3 and n-6 polyunsaturated fatty acids (PUFA), protective substances (antioxidants), and degradation products (VOC) of the poultry meat produced during cooking. The extent of VOC production and n-3 loss was found to be higher for the SG genotype. Reduction of n-6 was higher in MG, whereas small losses in antioxidants and PUFA were observed in the FG genotype, consequently, resulting in the lowest production of VOC. The SG and MG are genotypes more active from a kinetic point of view respect to the FG ones. For this reason, in the FG genotypes, the antioxidants are less involved in the oxidative stress induced by the movement; thus, they were available to protect the lipid of the meat during the cooking process. These results suggested that the use of SG and MG genotypes requires a specific dietary protocol (i.e., increasing the antioxidants content) to counteract the lipid oxidations in all the phases: in vivo, postmortem, and during/after cooking.

Effect of NaCl and sucrose tastants on protein composition of oral fluid analysed by SELDI-TOF-MS.

During eating, human saliva is secreted into the oral cavity by salivary glands. The relative contribution of different glands to total salivary flow rate depends, among other factors, on the tastants in the food. Few reports indicated that also the salivary protein composition depends on the tastant make-up of the food. We studied the influence of sodium-chloride- and sucrose solutions on the presence of proteins in the M(r) range 2-20kDa in whole saliva. Upon oral stimulation with a sodium chloride solution, a sucrose solution or water, we collected whole saliva from 14 volunteers after t=1 min, t=11 min and t=20 min. Saliva protein profiles were analysed by SELDI-TOF-MS. SELDI-TOF-MS intensities of m/z values representing different protein masses were compared between subjects, tastants and time conditions. For subsets of the 33 detected masses, significant effects were observed for all factors, with most masses involved in the Subjects effect: m/z(Subjects)>m/z(Time×Stimulus)>m/z(Stimulus)>m/z(Time). Most effects on saliva protein composition were observed at t=1 min, whilst almost no effects were observed at t=11 min and t=20 min. When considering the Stimulus×Time interaction, we identified four different stimulus-response patterns. Proteins identified in the present study, and attributed to specific glands or tissues in literature, were used to associate stimulus-response patterns with tissue provenances. Observed stimulus-response patterns were not uniquely associated to particular glands and tissues. Hence, there was no evidence of the involvement of particular tissues or glands in tastant-specific protein responses. In conclusion, oral stimulation with different tastants affects salivary protein composition in a protein- and stimuli dependent way, which seems not be associated with any specific tissues or glands of origin.

Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin.

The study of homologous proteins belonging to the same family can provide a rationale for important molecular properties such as oligomer formation, folding mechanism and mode of binding. We report here a physico-chemical characterization of porcine beta-lactoglobulin, purified from pooled milk: size-exclusion chromatography, CD and NMR measurements were used to study the aggregation and stability of this protein. In spite of the high sequence identity and homology of porcine beta-lactoglobulin with the widely studied bovine species, the two proteins exhibit very different behaviours. The porcine protein shows a monomer-dimer equilibrium with a pH dependence opposite to that observed for the bovine species. Unfolding experiments revealed the presence of an intermediate that probably has excess alpha helices, as reported for equine species. Modelling studies were performed on bovine, porcine and equine proteins, and, interestingly, electrostatic surface potential calculations led to results consistent with the different dimer interface found for porcine beta-lactoglobulin in the crystal structure. Interaction studies revealed that porcine beta-lactoglobulin is unable to bind fatty acids at any pH, thus questioning the main functional role proposed for lactoglobulins as fatty acid transporters or solubilizers.