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 ≥ 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.