Horse meat tenderization in relation to post-mortem evolution of the myofibrillar sub-proteome

The ageing process after animal slaughter enhances tenderness and influences the value of meat. Horse meat is becoming more popular but lacks standardized ageing practices that should be supported by a better understanding of post-mortem muscle biochemistry. Steaks from Longissimus Thoracis et Lumborum (LTL) of eight Hispano-Bretón horses were aged for 0, 7, 14 and 21 days and myofibrillar proteins were resolved by one dimensional gel electrophoresis (1-DE). Ten protein bands were found to change (p ≤ 0.05) among ageing periods. Most changes were observed between days 0 and 14, suggesting that tenderization occurred primary during the first two weeks. Liquid isoelectric focusing (OFFGEL) technology was applied to better resolve myofibrillar sub-proteome and evidenced fourteen protein bands that changed (p ≤ 0.05) between 0 and 21 days. Three of them were protein fragments coming from troponins T and I and from creatine kinase. Identified molecules could be further studied as potential markers for horse meat tenderness. •Myofibrillar proteome of horse meat aged up to 21 days was studied for first time.•Proteome changes during horse meat ageing occurred mainly during the first 2 weeks.•OFFGEL technology was successfully implemented for horse meat proteins.•OFFGEL evidenced fourteen protein bands that changed between 0 and 21 days.•Characterized proteins could become potential biomarkers of horse meat tenderness.