Validation of protein biological markers of lamb meat quality characteristics based on the different muscle types

This work investigated the ability of 8 potential biomarkers (phosphoglycerate kinase-1 (PGK1), pyruvate kinase-M2 (PKM2), phosphoglucomutase-1 (PGM1), & beta;-enolase (ENO3, myosin-binding protein-C (MYBPC1), myosin regulatory light chain-2 (MYLPF), troponin C-1 (TNNC1) and troponin I-1 (TNNI1)) to characterize meat quality by analyzing their relative abundance and enzymatic activity. Two different meat quality groups (Quadriceps femoris (QF) and Longissimus thoracis (LT) muscles) were selected at 24 h postmortem from 100 lamb carcasses. The relative abundance of PKM2, PGK1, PGM1, ENO3, MYBPC1, MYLPF, and TNNI1 was significantly different between LT and QF muscle groups (P < 0.01). Moreover, PKM, PGK, PGM, and ENO activity in LT muscle group was significantly lower than that in QF muscle (P < 0.05). Suggesting that PKM2, PGK1, PGM1, ENO3, MYBPC1, MYLPF, and TNNI1 can be used as robust biomarkers of lamb meat quality, providing the reference for under-standing the molecular mechanism of postmortem meat quality formation in future.

Automated summary

This study investigated the potential of 8 biomarkers (PGK1, PKM2, PGM1, ENO3, MYBPC1, MYLPF, TNNC1, and TNNI1) to characterize lamb meat quality based on their abundance and enzymatic activity. Different meat quality groups (QF and LT muscles) were sampled from 100 lamb carcasses at 24 h postmortem. The relative abundance of PKM2, PGK1, PGM1, ENO3, MYBPC1, MYLPF, and TNNI1 was significantly different between LT and QF muscle groups (P < 0.01), and the activity of PKM, PGK, PGM, and ENO was lower in the LT group compared to the QF group (P < 0.05). These findings indicate that these biomarkers can serve as robust indicators of lamb meat quality and provide insights into the molecular mechanisms of meat quality formation.