Thermally Induced Interactions and Gelation of Combined Myofibrillar Protein from White and Red Broiler Muscles |
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Authors: | YOULING L XIONG |
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Affiliation: | Author Xiong is with the Food Science Section, Dept. of Animal Sciences, Univ. of Kentucky, Lexington, KY 40546. |
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Abstract: | 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. |
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Keywords: | chicken protein protein aggregation gelation myofibrils |
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