Early postmortem proteome changes in normal and woody broiler breast muscles

Xue Zhang, Wei Zhai, Shuting Li, Surendranath P. Suman, Jing Chen, Haining Zhu, Daniel S. Antonelo, Mark Wesley Schilling

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Early postmortem changes in the whole muscle proteome from normal broiler (NB) and woody broiler (WB) breasts at 0 min, 15 min, 4 h, and 24 h after slaughter were analyzed using two-dimensional gel electrophoresis (2DE) and liquid chromatography−tandem mass spectrometry (LC−MS/MS). Elongation factor 2, EH domain-containing protein 2, phosphoglycerate mutase 1 (PGAM1), and T-complex protein 1 subunit gamma were differentially abundant in both NB and WB muscles during the early postmortem storage. Twenty additional proteins were differentially abundant among four postmortem time points in either NB or WB muscles. In the postmortem WB, changes in protein degradation were observed, including the degradation of desmin fragments, ovotransferrin chain A, and troponin I chain I. Additionally, a few glycolytic proteins in the WB might have undergone post-translational modification, including enolase, phosphoglucomutase-1, PGAM1, and pyruvate kinase. These changes in protein biomarkers highlight the impact of WB myopathy on postmortem proteome changes and increase our understanding of the relationship between WB conditions, postmortem biochemistry, and meat quality.

Original languageEnglish (US)
Pages (from-to)11000-11010
Number of pages11
JournalJournal of agricultural and food chemistry
Issue number39
StatePublished - Sep 30 2020
Externally publishedYes


  • Postmortem change
  • Protein degradation
  • Proteomics
  • Woody breast

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences


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