Storage stability of antioxidant-washed myofibrils from chicken white and red muscle

Oxidation and gel-forming ability of chicken white (breast) and red (leg) muscle myofibrillar proteins during storage at 0°C were examined. Breast myofibril gels exhibited greater shear moduli than leg myofibril gels throughout 8 days storage. Shear moduli of both breast and leg gels in the intermediate temperature zone (45-55°C) decreased during storage, but at >55°C, they either increased or remained unchanged. Lipid oxidation was inhibited by washing myofibrils with antioxidants propyl gallate, ascorbate, and tripolyphosphate. However, these antioxidants did not affect the content of protein carbonyls, and only slightly decreased the amine content during storage. Storage affected the kinetic process of myofibril gelation independently of antioxidant treatments.