Proteome basis for the biological variations in color and tenderness of longissimus thoracis muscle from beef cattle differing in growth rate and feeding regime

[Display omitted] •Beef quality and proteome in cattle differing in growth and diet were evaluated.•Redness was impacted mainly by growth rate, while feeding regime affected tenderness.•Abundances of 16 proteins were different among the comparisons.•Proteins were clustered in energy metabolism- and...

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Veröffentlicht in:Food research international 2022-03, Vol.153, p.110947-110947, Article 110947
Hauptverfasser: Antonelo, Daniel S., Gómez, Juan F.M., Silva, Saulo L., Beline, Mariane, Zhang, Xue, Wang, Yifei, Pavan, Bruna, Koulicoff, Larissa A., Rosa, Alessandra F., Goulart, Rodrigo S., Li, Shuting, Gerrard, David E., Suman, Surendranath P., Wes Schilling, M., Balieiro, Julio C.C.
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Zusammenfassung:[Display omitted] •Beef quality and proteome in cattle differing in growth and diet were evaluated.•Redness was impacted mainly by growth rate, while feeding regime affected tenderness.•Abundances of 16 proteins were different among the comparisons.•Proteins were clustered in energy metabolism- and muscle structure-related proteins.•ANXA2, MYLPF, PGK1, PGM1, PGAM2 and TNNT3 are potential biomarkers for beef quality. The proteome basis for the biological variations in color and tenderness of longissimus thoracis muscle from ½ Angus (Bos taurus taurus) × ½ Nellore (Bos taurus indicus) crossbred steers was evaluated in a completely randomized experimental design consisting of four treatments (n = 9 per treatment): 1) feedlot finished, high growth rate (FH); 2) feedlot finished, low growth rate (FL); 3) pasture finished, high growth rate (PH); and 4) pasture finished, low growth rate (PL). The following comparisons were made to evaluate the effects of finishing systems and growth rates on muscle proteome: 1) FH × PL; 2) FL × PH; 3) FH × FL; and 4) PH × PL. Sixteen protein spots were differentially abundant among these comparisons (P ≤ 0.05), which were distinguished in two major clusters, energy metabolism- and muscle structure-related proteins that impacted glycolysis, carbon metabolism, amino acid biosynthesis and muscle contraction pathways (FDR ≤ 0.05). For FH × PL comparison, triosephosphate isomerase (TPI), phosphoglucomutase-1 (PGM1) and phosphoglycerate kinase 1 (PGK1) were overabundant in FH beef whereas troponin T (TNNT3), α-actin (ACTA1) and myosin regulatory light chain 2 (MYLPF) were overabundant in PL beef. For the FL × PH comparison, PGM1, phosphoglycerate mutase 2 (PGAM2) and annexin 2 (ANXA2) were overabundant in PH beef. For the FH × FL comparison, AMP deaminase (AMPD1) and serum albumin (ALB) were overabundant in FH beef whereas glycogen phosphorylase (PYGM) was overabundant in FL beef. For the PH × PL comparison, myoglobin (MB) was overabundant in PH beef whereas PYGM and MYLPF were overabundant in PL beef. In non-aged beef, L* was positively correlated with PGM1 (r = 0.54) while tenderness was negatively correlated with PGAM2 (r = -0.74) and ANXA2 (r = -0.60). In 7-d aged beef, color attributes (L*, a* and b*) were positively correlated with PGM1 (r = 0.67, 0.64 and 0.64, respectively) while tenderness was negatively correlated with TNNT3 (r = -0.57), PGK1 (r = -0.52) and MYLPF (r = -0.66). Therefore, finishing systems and growth rate affe
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2022.110947