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- W2133872812 abstract "ABSTRACT: Principal component analysis was performed on turkey breast muscle that originated from a pool of genetically distinct turkeys by separating the salt‐soluble from the salt‐insoluble proteins. The salt‐soluble proteins (SSP) formed thermally induced meat gels and the viscoelastic properties of the gels were analyzed. The storage modulus (G′) at 80 °C of thermally induced gels derived from the SSPs ranged from 3 to 400 Pa. Each protein fraction was analyzed using 5% to 20% sodium dodecyl sulfate polyacrylamide gel electrophoresis. Reverse stepwise regression analysis of the electrophoretic fingerprints of the protein fractions showed that G′ at 80 °C was associated with the 2 protein bands from the salt‐soluble fraction ( R 2 = 0.87, P < 0.01) and 1 protein from the salt‐insoluble fraction ( R 2 = 0.27, P < 0.05). Primary sequence analysis identified one of the SSPs positively associated with G′ at 80 °C as α‐tropomyosin and the other SSP negatively associated with G′ at 80 °C as pyruvate kinase. The salt‐insoluble protein identified as triose phosphate isomerase was negatively associated with G′ at 80 °C. These findings are unique in that they show that proteins other than myosin and actin participate in the mechanisms of forming thermally induced meat gels." @default.
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- W2133872812 date "2006-11-01" @default.
- W2133872812 modified "2023-10-17" @default.
- W2133872812 title "Proteins Associated with Thermally Induced Gelation of Turkey Breast Meat" @default.
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- W2133872812 doi "https://doi.org/10.1111/j.1750-3841.2006.00184.x" @default.
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