Proteomic and parallel reaction monitoring approaches to evaluate biomarkers of mutton tenderness

Intensive fattening usually results in the changes of meat quality. Tenderness is a central attribute for mutton sensory qualities and consumers' choice. Here, we reported that intensive fattening mutton was more tender than that of traditionally raised sheep. By proteomic approach, we found 49 differentially expressed proteins in longissimus dorsi muscle. After bioinformatics analysis, 5 cytoskeletal proteins, 3 protein binding proteins and 7 metabolic enzymes were identified as potential biomarkers for mutton tenderness. Finally, we verified the expression of these abundant proteins by parallel reaction monitoring (PRM). Collectively, our results reveal that the mutton of sheep raised by intensive fattening is more tender than that of traditionally raised sheep. Myosin-2, myosin-13, vimentin, carbonic anhydrase, carbonic anhydrase-2, Glutathione S-transferase and Microtubule-associated protein 4 isoform X1 can be candidate biomarkers for mutton tenderness. Our data also indicate a central role of cytoskeletal proteins and metabolic enzymes in determining mutton tenderness.

Automated summary

The study found that mutton from intensively fattened sheep was more tender than that from traditionally raised sheep. Proteomic analysis revealed 49 differentially expressed proteins in the longissimus dorsi muscle, and after bioinformatics analysis, 5 cytoskeletal proteins, 3 protein binding proteins, and 7 metabolic enzymes were identified as potential biomarkers for mutton tenderness. The expression of these proteins was verified using parallel reaction monitoring (PRM). Cytoskeletal proteins and metabolic enzymes play a central role in determining mutton tenderness.