首页|Proteome basis of muscle-specific beef color stability
Proteome basis of muscle-specific beef color stability
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The objective of this study was to differentiate the sarcoplasmic proteomes of color-stable (Longissimus lumborum; LL) and color-labile (Psoas major; PM) beef muscles and to correlate the differences in protein abundance with color stability attributes。 LL and PM muscles were harvested from seven beef carcasses (USDA Select grade， 24 h post-mortem)， and samples for proteome analyses were collected and frozen at -80℃。 Muscles were fabricated into 2。54-cm steaks; steaks were aerobicallv packaged and assigned to refrigerated retail display for 0， 5， and 9 days。 On respective storage days， a~* value (redness) and ratio of reflectance at 630 nm to 580 nm (R630/580; indicator for surface color stability) were measured。 LL exhibited greater (P < 0。05) a~* value and R630/580 than PM during retail display indicating greater color stability。 Two-dimensional gel electrophoresis and tandem mass spectrometry identified sixteen differentially abundant proteins， which included antioxidant and chaperone proteins and enzymes involved in energy metabolism。 Proteins exhibiting positive correlation with a~* value (aldose reductase， creatine kinase， and beta-enolase) and R630/580 (peroxiredoxin-2， dihydropteridine reductase， and heat shock protein-27 kDa) were over-expressed in LL than in PM。 On the other hand， mitochondrial aconitase was more abundant in PM than in LL and correlated negatively to a~* value。 The greater color stability of beef LL compared to PM could be attributed to the over-expression of antioxidant (peroxiredoxin-2， dihydropteridine reductase， aldose reductase) and chaperone (heat shock protein-27 kDa) proteins。 Our result suggests the necessity to develop muscle-specific antioxidant and packaging strategies to improve beef color stability。
NETL
