Details

Autor(en) / Beteiligte

• Sayd, Thierry
• Morzel, Martine
• Chambon, Christophe
• Franck, Michel
• Figwer, Philippe
• Larzul, Catherine
• Le Roy, Pascale
• Monin, Gabriel
• Chérel, Pierre
• Laville, Elisabeth

Titel

Proteome Analysis of the Sarcoplasmic Fraction of Pig Semimembranosus Muscle:  Implications on Meat Color Development

Ist Teil von

• Journal of agricultural and food chemistry, 2006-04, Vol.54 (7), p.2732-2737

Ort / Verlag

Washington, DC: American Chemical Society

Erscheinungsjahr

2006

Quelle

MEDLINE

Beschreibungen/Notizen

• Two-dimensional electrophoresis was used to investigate sarcoplasmic protein expression in pig Semimembranosus muscles sampled 20 min after slaughter. Two groups (light and dark) of 12 animals were selected from 1000 pigs, based on meat L* values measured 36 h postmortem. Twenty-two proteins or fragments (p < 0.05) were differentially expressed. Muscles leading to darker meat had a more oxidative metabolism, indicated by more abundant mitochondrial enzymes of the respiratory chain, hemoglobin, and chaperone or regulator proteins (HSP27, αB-crystallin, and glucose-regulated protein 58kDa). Conversely, enzymes of glycolysis were overexpressed in the lighter group. Such samples were also characterized by higher levels of glutathione S-transferase ω, which can activate the RyR calcium channels, and higher levels of cyclophilin D. This protein pattern is likely to have severe implications on postmortem metabolism, namely, acceleration of ATP depletion and pH fall and subsequent enhanced protein denaturation, well-known to induce discoloration. Keywords: Proteomics; pig; Semimembranosus; L* value; GSTO; cyclophilin D