Comparison of sarcoplasmic proteomes between two groups of pig muscles selected for shear force of cooked meat.
Two-dimensional electrophoresis was used to compare Longissimus sarcoplasmic protein abundance between two groups (tough meat and tender meat), defined on the basis of extreme Warner-Bratzler shear force values measured on cooked pork. Fourteen protein spots differed in quantity (P<0.05) between the two groups and were identified. Adypocyte fatty acid binding protein and acyl-CoA binding protein involved in lipid traffic and in the control of gene expression regulating cell proliferation and differentiation, and Enoyl-CoA hydratase, aldose reductase and triosephosphate isomerase indirectly related to lipid metabolism were overrepresented in the tender group. The tender group was further characterized by increased levels of proteins involved in protein folding and polymerization (initiation factor elf-3beta, chaperonin subunit 2, profilin II). The results suggest that the lower post-cooking shear force could at least in part be related to muscle adipogenetic and/or myogenetic status of which the possible underlying mechanisms are discussed.
Laville
Elisabeth
E
Unité Recherches Qualité des Produits Animaux, Institut National de la Recherche Agronomique, 63122 St-Genès-Champanelle, France. elaville@clermont.inra.fr
Sayd
Thierry
T
Terlouw
Claudia
C
Chambon
Christophe
C
Damon
Marie
M
Larzul
Catherine
C
Leroy
Pascale
P
Glénisson
Jérôme
J
Chérel
Pierre
P
D000818:Animals; D005524:Food Technology; D006358:Hot Temperature; D008460:Meat; D009124:Muscle Proteins / Q000032:analysis; D018482:Muscle, Skeletal / Q000737:chemistry*; D020543:Proteome / Q000032:analysis*; D012519:Sarcoplasmic Reticulum / Q000737:chemistry*; D033081:Shear Strength; D013552:Swine
D009124:Muscle Proteins; D020543:Proteome