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.
|Number of pages||8|
|State||Published - Jan 15 2008|
Bibliographical noteFunding Information:
This study was supported, in part, by the NRI of the USDA CSREES, Grant No. 2004-35503-14122.
- Chymotryptic digestibility
- Salt solubility
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science