Early Postmortem Proteome Changes in Normal and Woody Broiler Breast Muscles.

Abstract

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.