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BACKGROUND RESULTS CONCLUSION This study aimed to explore how interactions between reactive oxygen species (ROS) and reactive nitrogen species (RNS) affect oxidative properties, nitrosative properties, and myofibrillar protein degradation during postmortem aging of yak meat.Yak longissimus dorsi was incubated with saline, ROS activator (H2O2)/inhibitor N‐Acetyl‐L‐cysteine (NAC) and RNS activator S‐Nitrosoglutathione (GSNO)/inhibitor L‐NAME hydrochloride (L‐NAME) combined treatments at 4 °C for 12, 24, 72, 120, and 168 h. The results indicated that regardless of whether RNS was activated or inhibited, activated ROS played a dominant role in myofibrillar protein degradation by oxidative modification to increase carbonyl content, disulfide bonds, surface hydrophobicity, and dimerized tyrosine while decreasing sulfhydryl content, thereby degrading nebulin, titin, troponin‐t and desmin. Notably, the Warner–Bratzler shear force (WBSF) of the H2O2 + L‐NAME group was the smallest, whereas that of the NAC + GSNO group was smaller than that of the NAC + L‐NAME group.These findings provide new insights into meat tenderization patterns through the interaction between ROS and RNS. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

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°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. [ABSTRACT FROM AUTHOR]

Tenderness is one of the most important qualities in meat. A proteomic approach is a suitable way to ensure meat tenderness. Thirty‐six tenderloin samples from yak were classified as exhibiting high (n = 12) or low (n = 12) tenderness and were evaluated using label‐free proteomics for the identification of the proteins and pathways most influential in tenderness variability. Between the two groups, proteomic changes were mainly caused by 33 differentially expressed proteins as displayed in reference patterns in heat maps. The expression of ENO2, SUCLG2, ETFDH, PGM1, TNNT3, TNNT1, HSDL2, GPI, ALAD, and COL1A1 proteins was very different between yak meats with high and low tenderness, and therefore, they are candidate biomarkers of yak meat tenderness. Furthermore, bioinformatics analyses revealed that the identified proteins are related to pentose phosphate, glycolysis, the citrate cycle, fatty acid metabolism, and the calcium signaling pathway. [ABSTRACT FROM AUTHOR]