2-D DIGE and mass spectrometry to analyse the effects of postmortem storage temperature on sea bass (Dicentrarchus labrax) muscle protein degradation.

One of the most unfavourable changes related to fish freshness is the postmortem tenderization of muscle, which promotes the progressive loss in quality. Therefore, the biochemical processes that are involved here have been extensively studied in order to identify potential quality indicators or to control postmortem degradation. Recent developments in cutting-edge technologies such as proteomics can provide better insight into the biochemical processes occurring postmortem in fish, thus facilitating the identification of markers useful to evaluate and monitor fish quality. One of the most popular methods of differential proteome analysis combines protein separation by high-resolution 2-DE with mass spectrometry (MS) identification of selected protein spots. Here, 2-D DIGE and MS/MS were used to trace changes in the protein profiles of aquacultured sea bass (Dicentrarchus labrax) muscle proteins over 5 days of postmortem storage at different temperatures, with the aim of identifying potential biochemical markers enabling monitoring and evaluation of fish filet quality.