Comparative proteomic insights into tenderness development of beef, pork, and chicken tenderloins during wet-aging

Meat-aging enhances meat quality through proteolysis and structural modifications; however, the extent of quality improvement and protein degradation differs among species. This study compares the physicochemical traits and proteomes of beef, pork, and chicken tenderloins during 14 d of aging to identify potential biomarkers of tenderness. The water-holding capacity and moisture content increase in beef and pork after aging, whereas those of chicken show no significant changes. The myofibrillar protein solubility increases in pork and chicken but remains unchanged in beef, potentially because of differences in the ratio of proteolytic enzymes. The myofibril fragmentation index and tenderness improve in all species to varying degrees, reflecting intrinsic muscle characteristics and protein-structure modifications. Several biomarkers and their dynamic patterns differ among species, whereas isoforms of myosin-binding protein C (MYBPC) are consistently detected across all species. These findings provide species-specific aging mechanisms and support the optimization of aging strategies. The identified species-specific markers and universal biomarker across the three species can be utilized as practical industrial indicators for monitoring tenderness development during meat aging.