Oxidation inhibition during washing, as it affects gelling properties and binding strength of beef heart myofibrillar protein, was investigated. Crude myofibrils isolated by repeated washing in the presence of propyl gallate, ascorbate and tripolyphosphate had a lower TBA value and formed stronger gels (puncture and compression strengths) in the pH range G-7.0 and in 0.6M NaCl than the control myofibrils. Inhibition of oxidation increased tensile stress of myofibrillar gels and enhanced bind strength in restructured meat. Functionality of myofibrillar protein could be protected by antioxidants used in the washing process.

Salt-soluble proteins (SSP) were extracted from porcine Serratus ventralis (red), Vastus intermedius (red) and Longissimus dorsi (white) muscles and heated to examine dynamic changes and transitions in protein aggregation. At pH 6.0, red muscle SSP typically showed 1 or 2 transitions and white muscle SSP exhibited 3 transitions. Addition of ortho-, pyro-, tripoly-and hexametaphosphate up to 1% increased SSP transition temperatures and altered transition patterns; NaCl at comparable ionic strengths did not show this effect. SSP transitions were most affected by 0.15-0.25% tripolyphosphate and low pH (~6.0). Red and white SSP exhibited different thermal properties and responses to phosphate treatments. These findings indicate red and white muscle types should undergo different processing treatments for optimum quality meat products.

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