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

• Published in: Food chemistry 2022-12, Vol.397, p.133746-133746, Article 133746
• Main Authors: Zheng, Kaizhi, Yin, Yuyang, Cao, Yang, Guo, Liangyong, Li, Peng, Jiang, Junfang, Huang, Xin, Jiang, Yongqing, Wu, Jianliang
• Format: Article
• Language: English
• Subjects: Biomarker; Intensive fattening; Mutton; PRM; Proteomics; Tenderness
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2022.133746

•Intensive fattening influenced mutton tenderness.•Proteomic analysis revealed fifteen proteins as potential biomarkers of mutton tenderness.•After PRM verification, myosin-2, myosin-13, vimentin, carbonic anhydrase, carbonic anhydrase 2, GSTM3 and MAP4 can be candidate 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.