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The thin filaments are assembled by actinmonomers bound to Nebulin. The thick filament system is composed of myosin protein which is connected from the M-line to the Z-disc by Titin It also contains myosin-binding protein C which binds at one end to the thick filament and the other to Actin. MUSCLE FIBER AT BIOLOGICAL SALT CONCENTRATIONS Sarcomeres are multi-protein complexes composed of three different filament systems. The basic unit of the muscle fiber is the sarcomere.Ī sarcomere is the basic unit of a muscle's cross-striated myofibril. To understand the mechanism further it is important to first take a look at muscle fiber anatomy.
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While low concentrations of NaCl produced swelling of the fibers, and high values of the water holding capacity at higher NaCl concentrations the phenomenon was reversed, fiber volume decreased, the tissue lost its own water and proteins precipitated causing disruption in the matrix Gravier et.al (2005). The increase in water holding capacity is likely attributed to the lateral expansion of myofibrils, which is coupled to protein solubilization (see below). At low NaCl concentrations, swelling of the fibers, and high values of water holding capacity were observed by Offer and Trinick (1983) Belitz and Grosch (1997) and Gravier et.al (2005). at a concentration of 4.6 - 5.8 % Changes in myofibrils in high salt solutions have been verified using phase contrast microscopy (Offer and Trinick, 1983 and scanning electron microscopy Graiver et. From Offer: the major effect on the increase in water mobility was probably due to the increased protein electrostatic repulsion leading to increase myofilament spacing. The majority in the interfilament spaces with the myofribrils but a substantial part in extracellular space and the spaces between myofibrils. In meat water seems to be held by capillary action. In porcine meat three distinct water populations were identified using proton LF NMR: one tightly bound to the the muscle proteins a second trapped within the myofibril structure and the third corresponding to water outside the myofibrillar lattice or even outside the muscle cells (Bertram et. Myofibrils can swell to more than twice their original volume when immersed in salt solutions (Offer and Trinick, 1983). Thus the majority of water in meat lies in the myofibrils in the spaces between the thick and thin filaments. Mybofibrils contain about 20% of protein, the rest being water. The main structural component of meat is the myofibril which occupies about 70% percent of the volume of lean meat. In addition, the dissolved protein does not coagulate into the normally dense aggregates, so the cooked meat seems more tender.Ĭhanges in Muscle Fiber as a Result of Brining The meat’s weight can increases by 10% or more, allowing for greater moisture in the food after cooking. The end result is the muscle fibers draws in and retain a substantial amount of water by both osmosis and capillary action. The high salt concentration immediately begins to do its work on the protein complexes within the muscle fiber (see below for detailed explanation). This leads salt ions to enter the cell via diffusion. The brine surrounding the muscle fiber cell has a higher concentration of salt than the fluid within the cells.