2013 Early Career Achievement Award-proteomics of muscle- and species-specificity in meat color stability

S. P. Suman, G. Rentfrow, M. N. Nair, P. Joseph

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Meat color is the most important quality trait influencing consumer purchase decisions. The interinfluential interactions between myoglobin and biomolecules govern color stability in meat. The advances in proteomics, such as high throughput analytical tools in mass spectrometry, 2-dimensional electrophoresis, and bioinformatics, offer themselves as robust techniques to characterize the proteome basis of muscle- and speciesspecific meat color phenomena. Differential abundance of chaperones and antioxidant proteins contributes to muscle- specific color stability in beef; the greater abundance of chaperones and antioxidant proteins in color-stable Longissimus lumborum than in color-labile Psoas major protects myoglobin and contributes to superior color stability of beef Longissimus steaks. Lipid oxidationinduced myoglobin oxidation is more critical to beef color than pork color due to the inherent differences in myoglobin chemistry; the number of nucleophilic histidine residues adducted by reactive aldehydes is greater in beef myoglobin than in pork myoglobin. Preferential adduction of secondary products of lipid oxidation to beef myoglobin accelerates metmyoglobin formation at a greater degree than in its pork counterpart. Mass spectrometric investigations revealed that although cherry-red carboxymyoglobin is more stable than oxymyoglobin, both redox forms undergo lipid oxidation-induced oxidation in model systems. The accuracy of mass spectrometry to detect the molecular mass of proteins has been applied to differentiate myoglobins from closely related meat animals, such as goats and sheep or emu and ostrich. In addition, this approach indicated that turkey myoglobin is 350 Da greater in molecular mass than beef myoglobin, and the unique biochemistry of turkey myoglobin could be responsible for its greater thermostability in model systems as well as the pink color defect observed in fully cooked uncured turkey products.

Original languageEnglish
Pages (from-to)875-882
Number of pages8
JournalJournal of Animal Science
Issue number3
StatePublished - Mar 2014


  • Color stability
  • Mass spectrometry
  • Meat color
  • Myoglobin
  • Proteomics

ASJC Scopus subject areas

  • Food Science
  • Animal Science and Zoology
  • Genetics


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