Effect of heating oxymyoglobin and metmyoglobin on the oxidation of muscle microsomes

Ricard Bou, Francesc Guardiola, Rafael Codony, Cameron Faustman, Ryan J. Elias, Eric A. Decker

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


Myoglobin (Mb) and its iron have been proposed to be major prooxidants in cooked meats. To understand the mechanisms and differentiate between the prooxidant and antioxidant potential of oxymyoglobin (OxyMb) and metmyoglobin (MetMb), their prooxidant activity, iron content, solubility, free radical scavenging activity, and iron binding capacity were determined as a function of thermal processing. The ability of native and heat denatured OxyMb and MetMb to promote the oxidation of muscle microsomes was different. MetMb promoted lipid oxidation in both its native and denatured states. Conversely, OxyMb became antioxidative when the protein was heated to temperatures ≥75 °C. The increased antioxidant activity of heat denatured OxyMb was likely due to a decrease in its prooxidative activity due to its loss of solubility. These data show that the impact on oxidative reactions of Mb is the result of the balance between its antioxidant and prooxidant activities.

Original languageEnglish (US)
Pages (from-to)9612-9620
Number of pages9
JournalJournal of agricultural and food chemistry
Issue number20
StatePublished - Oct 22 2008

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • General Agricultural and Biological Sciences


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