Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems

Donkeun Park, Youling L. Xiong, Amy L. Alderton, Tooru Ooizumi

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178 Scopus citations


The objective of the study was to compare three different oxidizing systems commonly present in muscle foods for their influence on the biochemical properties of muscle proteins. Myofibrillar protein isolate (MPI) prepared from pork serratus ventralis muscle was suspended (30 mg protein/mL) in 15 mM piperazine-N,N-bis(2-ethane sulfonic acid) buffer (pH 6.0). Oxidation was induced by incubating the protein suspension at 4°C for 24 h with (i) a hydroxyl radical-generating system (HRGS: 10 μM FeCl3, 0.1 mM ascorbic acid, and 0.05-5.0 mM H2O2), (ii) a lipid-oxidizing system (LOS: 0.05-5.0 mM linoleic acid and 3750 units of lipoxidase/mL), or (iii) a metmyoglobin-oxidizing system (MOS: 0.05-0.5 mM metmyoglobin). Changes in oxidized MPI were measured as Ca- and K-ATPase activities, formation of protein carbonyls and 2-thiobarbituric acid-reactive substances (TBARS), loss of protein thermal stability, and protein aggregation. The three oxidizing matrixes induced complex MPI changes; for example, the Ca- and K-ATPase activities were altered mainly by low-concentration oxidants, but the changes were unique for each oxidizing system. The carbonyl content in MOS-treated MPI was the highest, while the TBARS production, changes in thermal properties, and loss of the myosin heavy chain were the greatest in HRGS-treated MPIs. Overall, the hydroxyl radical-producing medium appeared to be the most oxidative to myofibrillar proteins under the experimental conditions employed in the study.

Original languageEnglish
Pages (from-to)4445-4451
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Issue number12
StatePublished - Jun 14 2006


  • ATPase
  • Carbonyls
  • DSC
  • Myofibrils
  • Myosin
  • Protein oxidation

ASJC Scopus subject areas

  • Chemistry (all)
  • Agricultural and Biological Sciences (all)


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