Proteomic features linked to tenderness of aged pork loins.

There is considerable evidence that the protein component of fresh pork makes a major contribution to tenderness. In particular, the proteomic profile can be linked to postmortem events including pH decline, tissue oxidation, and protein degradation. The objectives for this study were to determine differences in sarcoplasmic proteomes that contribute to tenderness variation in aged pork longissimus dorsi muscles (LM). A defined set of pork loins selected to be similar in pH, color, and lipid yet different in tenderness were used. Pork loins were assigned to tenderness groups based on their star probe values; a high star probe group (HSP; n=12 mean star probe 7.75 kg) and low star probe group (LPS; n=12 star probe 4.95 kg) Samples were selected for proteomic experiments based on star probe values, and selected samples were within specified ranges for ultimate pH (5.54-5.86), marbling score (1.0-3.0), and percent total lipid (1.61-3.37%). Two-dimensional difference in gel electrophoresis (2D-DIGE) and mass spectrometry were used to examine sarcoplasmic protein abundance and potential modifications. Proteins spots that were significantly different across groups were selected for identification. Results from 2D-DIGE showed that HSP samples had significantly more abundant metabolic, stress response, and regulatory proteins in the sarcoplasmic fraction compared with LSP samples. The stress response protein peroxiredoxin-2 was more abundant in HSP samples as determined by 2D-DIGE ( ≤ 0.01; 2 spots) and western blot assay ( = 0.02). Low star probe samples showed significantly more degradation of the structural protein desmin in 2D-DIGE ( < 0.01) and western blot assay ( < 0.01). These results demonstrate that extreme proteolytic differences influenced measured tenderness of LSP and HSP samples and that soluble desmin and peroxiredoxin-2 may be used as biomarkers to differentiate between tough and tender aged pork products.