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SUMMARY: To investigate the inner mechanisms of meat quality differences between high‐quality (HQ) and low‐quality (LQ), a comparative quantitative study between longissimus thoracis and external intercostals of goat muscle was performed from proteome to phosphorylated proteome using RP‐HPLC in combination with the 'isobaric tag' for relative and absolute quantitation (iTRAQ) labelling strategy. Altogether, 1441 proteins were identified in our study, of which 673 were phosphoproteins, and a total of twenty were common differentially expressed proteins. Myosin, carbonic anhydrase, and phosphoglucomutase could be used as proteins marker for HQ and LQ meat. Bioinformatics analysis showed that these proteins exhibited different rates for glycolysis and oxidative phosphorylation reaction, thus causing the different pH and NADH change rates, and resulting in better colour, tenderness, and water retention in HQ meat. The release of Ca2+ and adenosine triphosphate changed the meat quality through calcium signalling. Our finding provides a comprehensive view of proteome changes and their phosphorylation levels in goat muscle, involved in producing meats of different muscle parts. It also gives a better understanding of the regulation of protein on various biological processes that determine the final meat quality attributes. [ABSTRACT FROM AUTHOR]

This study was designed to investigate differences in the proteomes of goat Longissimus thoracis during freeze-thaw processing using iTRAQ technology. The effects of repeated freeze-thaw cycles (1 and 2) on the color and total amino acids of goat Longissimus thoracis were clarified. In total, 159 differentially expressed proteins (DEPs) were identified in goat meat during freeze-thaw processing. The treatment of repeated freeze-thaw cycles was confirmed to affect protein digestion and fat decomposition in goat meat. DEP quality analysis identified the elongation factor 1-gamma (EF-1γ), cAMP-dependent protein kinase catalytic subunit alpha (PKA C-alpha), 40S ribosomal protein S12 (RPS12), and the collagen alpha-2(IV) chain (COL4A2) as potential proteins for reflecting the degree of meat freeze-thaw, whereas myosin regulatory light chain 2 (MYLPF), myosin light chain 1/3 (MYL1/3), and isocitrate dehydrogenase [NAD] subunit beta (IDH3B) were considered to be biomarkers for meat color. Image 1 • Novel proteome analysis of goat meat during freeze-thaw processing. • Bioinformatics showed freeze-thaw affects protein digestion and fat decomposition. • Four proteins were identified to reflect the degree of meat freeze-thaw. • Three proteins were confirmed to be biomarkers for meat color. [ABSTRACT FROM AUTHOR]