Inhibition of Oxidation during Washing Improves the Functionality of Bovine Cardiac Myofibrillar Protein

The effect of antioxidative treatments during bovine cardiac myofibril isolation on rheological and gelling properties of the myofibrillar protein was examined. Minced beef heart muscle was washed four times in 25 mM phosphate buffer (pH 7.0) without (control wash) or with combined antioxidants (0.02% propyl gallate, 0.2% sodium ascorbate, and 0.2% sodium tripolyphosphate). Washing with antioxidants inhibited oxidation in fresh myofibrillar pellets and in pellets stored for up to 8 days. The antioxidant treatment increased the shear stress and viscosity of protein suspensions by 20–100%. Both control and antioxidant-washed myofibrillar proteins exhibited complex dynamic viscoelastic characteristics during thermal gelation, but the antioxidant-washed protein showed greater storage and loss moduli than the control within 50–60 °C. An extrusion test indicated that the antioxidant-treated, freshly isolated protein formed stronger gels than the control. Thus, the functionality of myofibrillar protein can be protected by the inclusion of antioxidants in the muscle washing process.