TY - JOUR
T1 - Proteomics of muscle-specific beef color stability
AU - Joseph, Poulson
AU - Suman, Surendranath P.
AU - Rentfrow, Gregg
AU - Li, Shuting
AU - Beach, Carol M.
PY - 2012/3/28
Y1 - 2012/3/28
N2 - The objective of the present study was to differentiate the sarcoplasmic proteome of color-stable (Longissimus lumborum; LL) and color-labile (Psoas major; PM) beef muscles. LL and PM muscles from seven beef carcasses (24 h post-mortem) were fabricated into 2.54 cm steaks, aerobically packaged, and assigned to refrigerated retail display for 9 days. LL steaks demonstrated greater (P < 0.05) color stability and lower (P < 0.05) lipid oxidation than PM steaks. Proteome analyses identified 16 differentially abundant proteins in LL and PM, including antioxidant proteins and chaperones. Proteins demonstrating positive correlation with redness (aldose reductase, creatine kinase, and β-enolase) and color stability (peroxiredoxin-2, peptide methionine sulfoxide reductase, and heat shock protein-27 kDa) were overabundant in LL, whereas the protein overabundant in PM (mitochondrial aconitase) exhibited negative correlation with redness. The color stability of LL could be attributed to the overabundance of antioxidant proteins and chaperones, and this finding suggests the necessity of developing muscle-specific processing strategies to improve beef color.
AB - The objective of the present study was to differentiate the sarcoplasmic proteome of color-stable (Longissimus lumborum; LL) and color-labile (Psoas major; PM) beef muscles. LL and PM muscles from seven beef carcasses (24 h post-mortem) were fabricated into 2.54 cm steaks, aerobically packaged, and assigned to refrigerated retail display for 9 days. LL steaks demonstrated greater (P < 0.05) color stability and lower (P < 0.05) lipid oxidation than PM steaks. Proteome analyses identified 16 differentially abundant proteins in LL and PM, including antioxidant proteins and chaperones. Proteins demonstrating positive correlation with redness (aldose reductase, creatine kinase, and β-enolase) and color stability (peroxiredoxin-2, peptide methionine sulfoxide reductase, and heat shock protein-27 kDa) were overabundant in LL, whereas the protein overabundant in PM (mitochondrial aconitase) exhibited negative correlation with redness. The color stability of LL could be attributed to the overabundance of antioxidant proteins and chaperones, and this finding suggests the necessity of developing muscle-specific processing strategies to improve beef color.
KW - Longissimus lumborum
KW - Psoas major
KW - beef color
KW - color stability
KW - sarcoplasmic proteome
UR - https://www.scopus.com/pages/publications/84859127509
UR - https://www.scopus.com/pages/publications/84859127509#tab=citedBy
U2 - 10.1021/jf204188v
DO - 10.1021/jf204188v
M3 - Article
C2 - 22369190
AN - SCOPUS:84859127509
SN - 0021-8561
VL - 60
SP - 3196
EP - 3203
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 12
ER -