Species-specific myoglobin oxidation

Shuang Yin, Cameron Faustman, Nantawat Tatiyaborworntham, Ranjith Ramanathan, Naveena B. Maheswarappa, Richard A. Mancini, Poulson Joseph, Surendranath P. Suman, Qun Sun

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

The effect of the lipid oxidation product, 4-hydroxy-2-nonenal (HNE), on oxidation of oxymyoglobin (OxyMb) from seven different meat-producing species was investigated. Relative to controls, HNE increased OxyMb oxidation within all species (p < 0.05) at both 25 and 4 °C, pH 5.6. The relative effect of HNE was greater for myoglobins (Mbs) that contained 12 ± 1 histidine (His) residues than for those that contained 9 His residues (p < 0.05); HNE efficacy in all species except chicken and turkey decreased with time. Mono-HNE adducts were detected in all species except chicken and turkey. In general, HNE alkylation increased the Mbs' ability to accelerate lipid oxidation in a microsome model. However, neither an HNE nor a Mb species dependent effect was observed. Results suggested that microsome model system associated lipid oxidation overshadowed HNE and species effects on OxyMb oxidation observed in lipid-free systems.

Original languageEnglish
Pages (from-to)12198-12203
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume59
Issue number22
DOIs
StatePublished - Nov 23 2011

Keywords

  • 4-hydroxy-2-nonenal
  • lipid oxidation
  • mass spectrometry
  • meat color
  • myoglobin

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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