Estimation of the proteome affecting changes in tenderness of yak meat during storage by label-free mass spectrometry

被引:4
作者
Li, Shengsheng [1 ,2 ]
Liu, Shujie [3 ,4 ]
机构
[1] Qinghai Univ, Acad Anim & Vet Sci, Xining 810016, Qinghai, Peoples R China
[2] Qinghai Univ, State Key Lab Plateau Ecol & Agr, Xining, Peoples R China
[3] Natl R&D Ctr Yak Meat Proc Technol, Xining, Peoples R China
[4] Key Lab Plateau Grazing Anim Nutr & Feed Sci Qing, Xining, Peoples R China
关键词
bioinformatics; label-free; proteomics; tenderness; yak meat; WATER-HOLDING CAPACITY; POSTMORTEM STORAGE; LONGISSIMUS-LUMBORUM; BEEF TENDERNESS; MU-CALPAIN; MUSCLE; PROTEOLYSIS; TENDERIZATION; QUANTITATION; MECHANISMS;
D O I
10.1002/vms3.801
中图分类号
S85 [动物医学(兽医学)];
学科分类号
0906 ;
摘要
Background: Tenderness is the main quality of meat products. However, the meat tenderness formation is a complex biological process, and pathways and proteins that affect the tenderness of yak meat are unknown. Methods: Label-free proteomics method was used to explore the effects of differentially expressed proteins on the tenderness of yak skeletal muscle (tenderloin) during post-mortem storage (0, 3, and 7 days) at 3 +/- 1 degrees C. Results: The tenderness of yak skeletal muscle improved significantly during storage. A total of 91 differentially expressed proteins of yak skeletal muscle during post-mortem storage were identified by the following comparisons: day 3 versus 0, day 7 versus 0, and day 7 versus 3. NDUFS6, CYCS, COX6A2, LDB3, HSPB7, TPM4, TAGLN, COL1A1, LUM, MYH11, ACTC1, and MYOZ1 proteins showed a significant difference during yak skeletal muscle post-mortem storage. Furthermore, bioinformatics analyses revealed that the identified proteins were related to carbon metabolism, citrate cycle, glycolysis, oxidative phosphorylation, and RNA degradation. Conclusion: The results of the present study could provide proteomic insights into changes in yak skeletal muscle tenderness during storage and may be a valuable resource for future investigations.
引用
收藏
页码:1640 / 1649
页数:10
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