Title of article :
Proteomic changes involved in tenderization of bovine Longissimus dorsi muscle during prolonged ageing
Author/Authors :
Polati، نويسنده , , Rita and Menini، نويسنده , , Michele and Robotti، نويسنده , , Elisa and Millioni، نويسنده , , Renato and Marengo، نويسنده , , Emilio and Novelli، نويسنده , , Enrico and Balzan، نويسنده , , Stefania and Cecconi، نويسنده , , Daniela، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2012
Abstract :
To study proteomic changes involved in tenderization of bovine Longissimus dorsi four Charolaise heifers and four Charolaise bull’s muscles were sampled at slaughter after early and long ageing (2–4 °C for 12 and 26 days respectively). Descriptive sensory evaluation of samples were performed and their tenderness evaluated by Warner–Bratzler shear force test. Protein composition of fresh muscle and of meat aged was analysed by cartesian and polar 2-D electrophoresis. Student’s t-test and Ranking-PCA analyses were performed to detect proteomic modulation, and the selected protein spots were identified by nano-HPLC-Chip MS/MS.
esearch has demonstrated that there are no differences between proteomic patterns of male and females Longissimus dorsi muscle, and that the extension of ageing beyond 12 days, did not brings any concrete advantage in terms of sensory quality. Furthermore, the data presented here demonstrated that meat maturation caused changes of the abundance of proteins involved in metabolic, structural, and stress related processes.
Keywords :
P-dimensional (2-PE) electrophoresis , Polar 2-D electrophoresis , Ranking-PCA , M. longissimus dorsi , Post-mortem proteome
Journal title :
Food Chemistry
Journal title :
Food Chemistry