期刊
FOOD CHEMISTRY
卷 328, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2020.127133
关键词
Pig; Meat quality; TMT; Proteomic
资金
- National Key Technology R&D Program of China [2015BAD03B02-2]
- National Natural Science Foundation of China [31301952, 31501919]
- National Swine Industry Technology System [CARS-35]
- Agricultural Science and Technology Innovation Program of Chinese Academy of Agricultural Sciences [ASTIP-IAS02]
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 Ca-2(+), 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.
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