Effect of Ultrastructural Disruption and Protein Dispersion on Gel-forming in Myofibrillar Gels
The pH shifting process involves chopping the muscle with water, adjustment low (2-3) or high (10.5-11) pH values, and then precipitation by adjusting to the isoelectric point (5.3-5.5). The resulting meat protein isolate is then dewatered and ready for further use. Interestingly the pH shifting treatment eliminates the necessity for salt addition in order to maximize the strength and deformability of cooked gels made from the meat so treated. Experiments were carried out using this process on King Mackerel. The slurries produced by the process and gels made from the slurries were evaluated for disruption and dispersion by transmission election microscopy, TEM. The evaluation of these micrographs was assisted by a trained sensory panel to generate quantitive data describing the micrographs. The gel-forming ability was measured using torsion.
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Effects of Ph Shifting on Gel Forming Ability of King Mackerel
Effects of Calpain Treatment on Gelforming Ability of Isolated
9 decreasing actin Agricultural and Food bar represents 0.3 C-protein calpain Cell Biology coiled coil comminution cooked gels Craig and Padron Cytoskeletal and Motor decreasing pH disruption and dispersion editors Error bars represent evaluated Figure Food Chemistry Food Science Fracture Strain gel at pH hydrophobic increasing pH interactions intermediate filaments Journal of Agricultural Journal of Cell Journal of Food Journal of Molecular King Mackerel muscle Labeit M-line Mackerel muscle gel Meat Science micrograph of pH Molecular Biology Motor Proteins muscle at pH muscle proteins muscle ultrastructure MyBP-C myofibrillar proteins myofibrils myofilaments myosin myosin molecules nebulin Panel Score pH 7 decreasing pH 9 increasing pH shifted King pH shifting process Plot of trained protein dispersion represents 0.3 micron represents 1 micron salt addition samples sarcomere Scale bar represents Schematic Showing shifted King Mackerel skeletal-muscle slurry solubilization Surimi thick filament titin trained panel Transmission electron micrograph tropomyosin troponin ultrastructure disruption