Sarcoplasmic Proteome Profile and Internal Color of Beef Longissimus Lumborum Steaks Cooked to Different Endpoint Temperatures

The complex relationship between endpoint temperature, sarcoplasmic proteome, and internal color in cooked steaks is yet to be examined. The objective of the present study was to characterize the changes in sarcoplasmic proteome and their influence on the internal color of beef longissimus lumborum (LL) steaks cooked to different endpoint temper-atures. Two 2.5-cm-thick LL steaks were fabricated from 9 beef strip loins and were cooked to an internal endpoint temperature of either 60°C (C-60) or 71°C (C-71). Cooked steaks were cooled and sliced parallel to the grilled surface, and internal color was evaluated instrumentally. Sarcoplasmic proteome from the interiors of the cooked steaks was analyzed using two-dimensional electrophoresis, and the gel images were digitally analyzed. The protein spots exhibiting more than 2-fold intensity differences (P < 0.05) were subjected to in-gel tryptic digestion and were identified by tandem mass spectrometry. The C-60 steaks demonstrated greater (P < 0.05) redness and color stability than the C-71 ones. Eleven differentially abun-dant protein spots were identified, and they belonged to 6 functional groups (transport proteins, enzymes in energy metabolism, chaperones, antioxidant proteins, enzymes in amino acid metabolism, and glycolytic enzymes). While 10 spots were overabundant (P < 0.05) in C-60 steaks, 1 spot was overabundant (P < 0.05) in C-71 steaks. The spot overabundant in C-71 samples was identified as myoglobin, suggesting the possible role of post-translational modifications in the heme protein’s thermal stability. The results indicated that the endpoint cooking temperature influenced sarcoplasmic proteome profile and internal color of cooked beef LL steaks. The overabundant proteins in steaks cooked to 60°C may be exploited as potential biomarkers for undercooked beef, which is a source for foodborne infections.