Abstract
To explore the molecular mechanisms of meat quality, four high-quality (HQ) samples and four low-quality (LQ) samples from longissimus dorsi muscles were chosen, and tandem mass tag (TMT) labeling combined with mass spectrometry (MS) were performed to find associations between meat quality and proteome profiles. The LQ meats had lower pH, lighter color, and higher drip loss compared to the HQ meats. About 140 differentially expressed proteins were identified. Functional analysis results of differentially expressed proteins showed that decreased release of Ca2+, lower contents of type II fibers, lower contents of glycogen, and decreased glycogenolysis in HQ meats indicated a lower degree of glycolysis in HQ as compared to LQ meats. Meanwhile, some differentially expressed proteins suggested that the levels of oxidative stress and apoptosis were lower in HQ meats than in LQ meats. This study reveals physiological changes between HQ and LQ meats according to the proteome profiles.