Journal of Food Science · 1990 · 47 citations · 14 references
Muscle FunctionMyofibrillar ProteinsCytoskeletonAnalytical UltracentrifugationProtein RefoldingCellular PhysiologyMuscle PhysiologySkeletal MuscleBioenergeticsProtein FoldingT MaxWhole Hake MuscleThermodynamicsProtein DegradationBiophysicsProtein ChemistryBiochemistryAbstract DenaturationNatural SciencesPhysiologyDifferential Scanning CalorimetricThermal DenaturationCellular BiochemistryMedicine
ABSTRACT Denaturation of hake ( Merluccius hubbsi ) proteins was studied with DSC by monitoring T max of transitions and denaturation enthalpies. Whole muscle free of connective tissue showed two transitions (T max 46.5°C and 75.3°C), and ΔH of 4.27 cal/g. The exudative sarcoplasmic fraction showed three transitions (T max 45.2°C, 59.0°C and 75.5°C) and ΔH of 3.92 cal/g. The sarcoplasmic proteins from whole hake muscle contributed to both denaturation peaks. Muscle depleted of sarcoplasmic proteins by chloride extraction showed a higher thermal sensitivity and a diminished denaturation enthalpy on the second transition. This suggested an additional effect of chloride upon actin in addition to sarcoplasmic protein extraction. pH had an effect upon the native conformation of thick filament proteins, specifically myosin.
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