Proteomic changes involved in tenderization of bovine Longissimus dorsi muscle during prolonged aging

The biological mechanisms involved in structural and biochemical changes during aging that are responsible of tenderization of meat are not yet completely understood. To study proteomic changes involved in tenderization of bovine Longissimus dorsi, four Charolaise heifers and four Charolaise bulls muscles were sampled at slaughter and after early and long aging (storage at 2-4 \ub0C for 12 and 26 days respectively). Descriptive sensory evaluation of samples was performed and their tenderness was evaluated by Warner-Bratzler shear force test. Protein composition of fresh muscle and of meat aged for 12 and 26 days was analyzed by cartesian and radial 2-D electrophoresis. Student\u2019s t-test and Ranking-PCA analyses were performed to detect proteomic modulation during the different stages of maturation, and the selected protein spots were identified by nano-HPLC-Chip MS/MS. Proteomic analysis demonstrated that there were no differences between proteomic patterns of male and females LD muscle. Furthermore, meat maturation caused changes of (in) the abundance of proteins involved in metabolic, structural, and stress related processes. In addition, it must be remarked that the extension of aging beyond 12 days, in the conditions here tested, did not highlight any concrete advantage in terms of sensory quality