Browsing Food Quality & Sensory Science by Subject "Mass spectrometry"
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Meta-proteomics for the discovery of protein biomarkers of beef tenderness: An overview of integrated studiesThis meta-proteomics review focused on proteins identified as candidate biomarkers of beef tenderness by comparing extreme groups of tenderness using two-dimensional electrophoresis (2-DE) associated with mass spectrometry (MS). We reviewed in this integromics study the results of 12 experiments that identified protein biomarkers from two muscles, Longissimus thoracis (LT) and Semitendinosus (ST), of different types of cattle: young bulls, steers or cows from beef breeds (Charolais, Limousin, Blond d’Aquitaine), hardy breed (Salers) or mixed breed (PDO Maine-Anjou). Comparative proteomics of groups differing in their tenderness evaluated by instrumental Warner-Bratzler shear force (WBSF) or by sensory analysis using trained panelists, revealed 61 proteins differentially abundant (P < 0.05) between tender and tough groups. A higher number of discriminative proteins was observed for LT (50 proteins) compared to ST muscle (28 proteins). The Gene Ontology annotations showed that the proteins of structure and contraction, protection against oxidative stress and apoptosis, energy metabolism, 70 family HSPs and proteasome subunits are more involved in LT tenderness than in ST. Amongst the list of candidate biomarkers of tenderness some proteins such as HSPB1 are common between the 2 muscles whatever the evaluation method of tenderness, but some relationships with tenderness for others (MYH1, TNNT3, HSPB6) are inversed. Muscle specificities were revealed in this meta-proteomic study. For example, Parvalbumin (PVALB) appeared as a robust biomarker in ST muscle whatever the evaluation method of tenderness. HSPA1B seems to be a robust candidate for LT tenderness (with WBSF) regardless the animal type. Some gender specificities were further identified including similarities between cows and steers (MSRA and HSPA9) in contrast to bulls. The comparison of the 12 proteomic studies revealed strong dissimilarities to identify generic biomarkers of beef tenderness. This integrative analysis allowed better understanding of the biological processes involved in tenderness in two muscles and their variations according to the main factors underlying this quality. It allowed also proposing for the first time a comprehensive list of candidate biomarkers to be evaluated deeply to validate their relationships with tenderness on a large number of cattle and breeds.