Journal
FOOD CHEMISTRY
Volume 106, Issue 2, Pages 661-668Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2007.06.029
Keywords
myosin; myofibrils; oxidation; denaturation; Ca-ATPase; salt solubility; chymotryptic digestibility
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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-I 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. (c) 2007 Elsevier Ltd. All rights reserved.
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