Proteomic analysis of wild boar meat: Effect of storage method and time on muscle protein stability

Oxidation processes affect proteins from various molecular pathways and are crucial for wild boar meat quality, shelf life and human health. This study investigated the effects of different storage methods on the formation and composition of oxygen-induced protein aggregates in the muscles of European wild boar (Sus scrofa scrofa). Vacuum packaging (VAC), modified atmosphere packaging (MAP) and dry-ageing (DA) were compared over a 21-day storage period. The results showed significant differences in protein aggregation depending on the method and storage time. The most intense protein aggregation occurred in the MAP (80 % O₂), while air DA (20.9 % O₂) resulted in intermediate levels of protein aggregation. Crucial myofibrillar proteins involved in aggregate formation were titin, myosin isoforms (MYH1, MYH2 and MYH7) and nebulin, which were cross-linked with small sarcoplasmic enzymes, such as muscle creatine kinase, isocitrate dehydrogenase and ATPase 1. High‑oxygen storage conditions also promoted the oxidation of ATP synthase, beta-enolase 3, ADP/ATP translocase and myoglobin.