THERMALLY INDUCED INTERACTIONS AND GELATION OF COMBINED MYOFIBRILLAR PROTEIN FROM WHITE AND RED BROILER MUSCLES

The gelling properties of broiler myofibrillar protein were studied by determining protein-protein interactions during heating. Breast and leg salt-soluble protein (SSP) showed 1-3 transitions in protein-protein interactions within pH 5.5-6.5. The maximum transition temperatures of leg SSP decreased when leg SSP was mixed with breast SSP. The combined breast/leg myofibrils formed stronger gels than leg myofibrils alone at pH greater-than-or-equal-to 6.0, and stronger gels than breast myofibrils alone at pH < 6.0. The results suggest that interactions existed between breast and leg myofibrillar proteins, and the transitions in these interactions were useful for predicting gel strength of the combined breast/leg myofibrils.