Hydroxyl radical oxidation destabilizes subfragment-1 but not the rod of myosin in chicken myofibrils

Tooru Ooizumi, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The thermal denaturation process of myosin in oxidized chicken myofibrils was investigated. Exposures of myofibrils to hydroxyl radical-generation systems (HRGS) resulted in an enhanced susceptibility of myosin to thermal inactivation of Ca-ATPase and a loss of salt solubility. The chymotryptic production of subfragment-1 (S-1) from myosin in oxidized myofibrils decreased more rapidly than that in un-oxidized myofibrils upon heating, which paralleled the Ca-ATPase decay. However, the heat-induced decrease in chymotryptic production of rod from myosin was not affected by the HRGS treatment. The results suggested that free radical oxidation promoted thermal destabilization of myosin in the S-1 portion instead of the rod portion. The altered myosin denaturation pattern due to hydroxyl radical oxidation was likely a cause for functionality changes in oxidatively stressed myofibrillar proteins in meat processing.

Original languageEnglish
Pages (from-to)661-668
Number of pages8
JournalFood Chemistry
Issue number2
StatePublished - Jan 15 2008

Bibliographical note

Funding Information:
This study was supported, in part, by the NRI of the USDA CSREES, Grant No. 2004-35503-14122.


  • Ca-ATPase
  • Chymotryptic digestibility
  • Denaturation
  • Myofibrils
  • Myosin
  • Oxidation
  • Salt solubility

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science


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