Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4°C

Surendranath P. Suman, Cameron Faustman, Sheryl L. Stamer, Daniel C. Liebler

Research output: Contribution to journalArticlepeer-review

72 Scopus citations


Myoglobin (Mb) redox stability affects meat color and is compromised by lipid oxidation products such as 4-hydroxy-2-nonenal (HNE). Pork lipids are generally more unsaturated and would be expected to oxidize readily and produce more oxidation products than beef. Supranutritional supplementation of vitamin E improves Mb redox stability of beef but not pork. The present study investigated HNE-induced redox instability in porcine and bovine myoglobins at 4°C and pH 5.6. Oxymyoglobin (OxyMb) was incubated with HNE (0.075 mM porcine OxyMb + 0.5 mM HNE; 0.15 mM bovine OxyMb + 1.0 mM HNE). In porcine Mb, only monoadducts formed via Michael addition were detected after 72 h, whereas in bovine Mb both mono- and diadducts were identified. LC-MS-MS identified four histidine residues (His 36, 81, 88, and 152) of bovine Mb that were readily adducted by HNE, whereas in porcine Mb only two histidine residues (His 24 and 36) were adducted. These results suggested that the primary structure of bovine Mb predisposes it to greater nucleophilic attack by HNE and subsequent adduction than is suffered by porcine Mb.

Original languageEnglish
Pages (from-to)3402-3408
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Issue number9
StatePublished - May 3 2006


  • 4-hydroxy-2-nonenal
  • Lipid oxidation
  • Mass spectrometry
  • Myoglobin

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences


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