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Proteome changes derived from animals that have suffered pre-slaughter stress are a fact. In this study, Proteomic analysis was carried out on 20 bovine loin samples from Asturiana de los Valles and crossbreds cattle previously classified as normal and DFD meat at 24 h post-mortem using pH measurements. Sarcoplasmic sub-proteome of Longissimus thoracis at 24 h post-mortem was fractionated by the use of liquid isoelectric focusing (OFFGEL) in the pH range 3–10, followed by SDS-PAGE analysis of each retrieved fraction. The protein fractionation profile showed high reproducibility along the different sample groups. Five protein bands showed significant differences (p, This work was funded by the Spanish Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (RTA2014-00034-C04).

Meat consumption is an important part of human diet with strong implications in health, economy and culture worldwide. Meat is a proteinaceous product and therefore proteomics holds a considerable value to the study of the protein events underlying meat production and processing. In this article we will review this subject in an integrated “farm to fork” perspective, i.e. focusing on all the major levels of the meat producing chain: farm, abattoir and transformation industry. We will focus on the use, importance and applications of proteomics, providing clear examples of the most relevant studies in the field. A special attention will be given to meat production, as well as quality control. In the latter, a particular emphasis will be given to microbial safety and the detection of frauds. Fil: Paredi, Gianluca. University of Parma. Department of Pharmacy; Italia; University of Parma. Interdepartmental Centre; Italia; Fil: Sentandreu, Miguel Angel. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España; Fil: Mozzarelli, Andrea. University of Parma. Department of Pharmacy; Italia; University of Parma. Interdepartmental Centre; Italia; National Institute of Biostructures and Biosystems; Italia; Fil: Fadda, Silvina G.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina; Fil: Hollung, Kristin. NOFIMA AS—Matforskningsinstituttet; Noruega; Fil: de Almeida, André Martinho. Instituto de Investigação Científica Tropical; Portugal; Instituto de Tecnologia Química e Biológica; Portugal

Angiotensin I-converting enzyme (ACE) inhibitory activity of peptides derived from the hydrolysis of sarcoplasmic and myofibrillar porcine proteins by the action of Lactobacillus sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in order to fractionate the extracts for further evaluate the ACE inhibitory activity of the collected peptide fractions. Bioactive fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed lactic acid bacteria. Identification of peptides contained in these bioactive fractions was carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the mascot seach engine. A total of eighteen peptides were characterized from the two most active fractions obtained from the hydrolysis made by L. sakei CRL1862. Regarding L. curvatus CRL705, its proteolytic action was able to generate thirty and twenty peptides, which were identified in the two most active fractions, respectively. It is worth noting that the sequence FISNHAY was generated by the proteolytic action of the two species. Sequence similarity analyses between the peptides identified in this study and those previously identified as ACE inhibitory peptides and detailed in the BIOPEP database were outlined. Results suggest that lactic acid bacteria selected in this study were able to generate peptides with ACE inhibitory activity, thus having potential to be used in the development of functional fermented products. Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina; Fil: Aristoy, María Concepción. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España; Fil: Sentandreu, Miguel Ángel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España; Fil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina; Fil: Toldrá, Fidel. Consejo Superior de Investigaciones Cientificas. Instituto de Ciencia y Teconologia de Alimentos y Nutricion; España