Proteome Research Reveals New Insights into Meat Quality

Recent research conducted at the University of Lisbon has unveiled the significance of serpentina chevon, a product of immense nutritional and cultural value, especially in Portugal. The study aimed to evaluate the effect of dry-ageing in bag and thermal processing on the proteome of Longissimus thoracis et lumborum muscle of chevon. The researchers analyzed 1264 proteins, identifying 3, 9, 39, and 41 differentially abundant proteins in four comparisons, respectively. The study concludes that proteins such as actin, MYL1, MYL4, MYL6B, TNNC1, TNNC2, TPM3, CA3, PVALB, COL1A1, and COL12A1 are associated with meat quality, indicating the potential of proteomics in studying the effects of ageing and cooking.

Key Takeaways:

• The study aimed to evaluate the effect of dry-ageing in bag and thermal processing on the proteome of Longissimus thoracis et lumborum muscle of chevon.
• Four females were aged for 46 days and then cooked, and proteomic analysis was carried out using label-free quantification, identifying 1264 proteins.
• Four comparisons were computed: aged vs non-aged meat, cooked aged vs cooked non-aged meat, cooked aged vs aged meat, and cooked non-aged vs non-aged meat.
• Actin was identified as a potential indicator of ageing and cooking stability.
• Proteins MYL1, MYL4, MYL6B, TNNC1, TNNC2, TPM3, CA3, PVALB, COL1A1, and COL12A1 were associated with quality, being involved in actin binding, muscle contraction/regulation, and connective tissue composition.
• Collagen-related proteins in MC vs M comparison suggest aging affects meat quality.
• The results establish different proteins as putative meat quality indicators and demonstrate the usefulness of proteomics for studying the effect of ageing and cooking.

Statistics:

• 1264 proteins were identified through proteomic analysis.
• 3, 9, 39, and 41 differentially abundant proteins were identified in four comparisons, respectively.
• The study analyzed four females aged for 46 days and then cooked.
• The proteome of Longissimus thoracis et lumborum muscle of chevon was analyzed using label-free quantification.

Sources:

• Food Research International, "The goat Longissimus thoracis et lumborum muscle proteome: effects of dry ageing and cooking in chevon," 2025;220:117089.
• LEAF - Linking Landscape, Environment, Agriculture and Food Research Centre, Instituto Superior de Agronomia, University of Lisbon, Tapada da Ajuda, 1349-017 Lisboa, Portugal.
• Elsevier, Radarweg 29, 1043 Nx Amsterdam, Netherlands.