Peroxiredoxin-6—A potential protein marker for meat tenderness in bovine longissimus thoracis muscle1

Abstract

The muscle sarcoplasmic proteins from bovine M. longissimus thoracis muscle were studied using proteomics to identify possible protein markers for meat tenderness. This study included 3 experiments: A1, A2, and B. From a collection of biopsies from the bovine M. longissimus thoracis muscle, excised 4 d before slaughter from 178 Norwegian Red young bulls, 26 biopsies were studied in Exp. A1. Based on Warner-Bratzler shear force (WBSF) values at 7 d postmortem, the biopsies were separated into a tender and a tough group of 13 bulls each and analyzed by 2-dimensional gel electrophoresis (2-DE) and Western blotting. The 2-DE experiments identified 4 different proteins: stress-70 protein, protein DJ-1, peroxiredoxin-6, and malate dehydrogenase, which were different in abundance in the tender and tough groups. However, only peroxiredoxin-6 was confirmed by quantification from Western blots. Peroxiredoxin-6 is an antioxidant enzyme that plays a role in protecting cells from oxidative stress. Peroxiredoxin-6 was identified through 3 spots of the same molecular weight, but with different pI on the Western blots. Only one of the spots was more abundant in the biopsies from the tender group. In Exp. A2, samples collected 1 h postmortem from the same animals and muscles as in Exp. A1 were analyzed by Western blotting. In these postmortem samples, the same spot from peroxiredoxin-6 as in Exp. A1 was more abundant in the tender group. In addition, one of the other peroxiredoxin-6 spots was also more abundant in the tender group. To verify the results from Exp. A, biopsies from 14 additional animals were analyzed in Exp. B by Western blotting against stress-70 protein, protein DJ-1, peroxiredoxin-6, and malate dehydrogenase. No significant differences between the tough and tender groups could be observed in these biopsies. However, for peroxiredoxin-6, the tendencies pointed in the same direction as in Exp. A. In conclusion, peroxiredoxin-6 might be a potential protein marker for meat tenderness detectable in biopsies and in samples collected shortly after slaughter. However, more animals are needed to verify the findings in the present study.

Peroxiredoxin 6: A Bifunctional Enzyme with Glutathione Peroxidase and Phospholipase A2Activities

“…Whether any of these associations will provide definitive insights into pathogenesis or will provide targets for therapy remains to be determined. Finally, expression of Prdx6 in bovine thoracic muscles was found to correlate with tenderness of the meat (33), so think of Prdx6 at that next meal with an especially tender steak.…”

Proteomic changes involved in tenderization of bovine Longissimus dorsi muscle during prolonged ageing

“…We reported in Table 3 a decrease of the abundance of PRDX1 after early maturation and a strong increase from early to long maturation. It is interesting to note that another peroxiredoxin, PRDX 6, has already been proposed as a potential biomarker of beef tenderness (Jia et al, 2009).…”

Changes in the Sarcoplasmic Proteome of Beef Muscles with Differential Color Stability during Postmortem Aging

“…Protein deglycase DJ-1 protects cells against oxidative stress and cell death by acting as an oxidative stress sensor, redox-sensitive chaperone, and protease. The protein was more abundant in ST7 compared to ST0 (Table 12), and has been previously identified to be differentially abundant in sarcoplasmic proteome in relation to meat color (Joseph et al, 2012;Wu et al, 2016), tenderness (Jia et al, 2009), and water holding capacity (Hwang et al, 2005). In general, chaperone proteins can prevent protein aggregation and protein denaturation occurring during the muscle-to-meat conversion (Sayd et al, 2006).…”