• Asian-Australasian Journal of Animal Sciences
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• v.15 no.1
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• pp.111-116
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• 2002

This study investigated quantitative changes in the spaces between and within myofibrils and the impact of high and low voltage electrical stimulation on muscle ultrastructure as seen in electron micrographs. In addition, the relationships of these spaces and the impact to meat tenderness were investigated. The degradation of myofibrils during aging appeared to be localized across the muscle fibre. Structural deterioration of muscle fibres was evident 1 day post-mortem, involving the weakening in the lateral integrity of the myofibrils and Z-disc regions. Meat tenderisation, as shown by objective measurements, coincided with these increases in degradation, as assessed by the sum of the gaps between and within myofibrils. The results showed that the total size of gaps between and within myofibrils can be used as an indicator of meat tenderization during aging, but that ultrastructural alteration in electrically stimulated muscle had little relationship with meat tenderness.

• Applied Microscopy
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• v.28 no.1
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• pp.1-19
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• 1998

Ultrastructural study of the development of the atrioventricular (AV) node was studied by electron microscopy in human fetus ranging from 30 mm to 260 mm crown rump length, and compared with human adult. By 30 mm fetus, the right AV nodal primordium was located below the attachment of the right venous valve. The left AV nodal primordium was observed below the attachment of septum primum. The cytoplasm of the nodal primordia contained few mitochondria, and myofibrils. These cells were apposed to each other with occasional desmosomes. In 40 mm fetus, the AV node cells were poorly organized myofibrils, while working myocardial cells were well organized myofibrils with sarcomere. At 70 mm fetus, intercalated discs were developed in the working myocardial cells. At 100 mm fetus, the nodal cells contained a relatively clear cytoplasm with a few groups of myofibrils and mitochondria. By $140\sim200$ mm fetuses, the nodal cells were an increasing number of myofibrils and mitochondria and these were scattered throughout the cytoplasm. At 260 mm fetus, the nodal cells were small and contained a clear cytoplasm with sparse and poorly organized myofibrils and mitochondria. All major ultrastructural features which characterize the adult AV nodal cells were found in this stage. The working myocardial cells were larger and had a more compact cytoarchitecture than nodal cells. Zonula adherens or fasciae adherens type junction were not found between nodal cells, but they frequently observed between nodal and working myocardial cells.

• Korean Journal of Food Science and Technology
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• v.6 no.2
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• pp.79-85
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• 1974

To obtain further information concerning the nature myofibrillar proteins in a food system, an investigation has been conducted to compare the change in the biochemical property of the myofibril with the changes in the morphological structure of the myofibril. When myofibrils were prepared with 0.16 M KCl-0.04 M Tris-HCl, the band pattern was clear and distinct. There was a uniform thickening of A-band, a sharp appearence of Z-lines and a wide I-band. The band pattern of myofibrils was changed as the composition of extraction solution was changed. Also the ATPase activity of myofibril changed as the length of sarcomere changed. When myofibrils were treated with a low concentration of trypsin, myofibrils turned in the contracted state. With the progress of prolonged trypsin treatment, most of myofibrils exhibited a pattern of alternating light and dark bands, supercontracted pattern. Although myofibrils exhibited a supercontracted band pattern, the ATPase activity of myofibril continued to increase with the progress of trypsin treatment. An assumption was made that tropomyosin may be located in Z-line and that troponin-tropomyosin complex can inhibit the ATPase activity of myofibrils through the structural alternation of myofibril.

• Food Science of Animal Resources
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• v.18 no.4
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• pp.292-300
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• 1998

This study was undertaken to determine the influence in the Z-disk domain of titin on the tenderization of meat by the structure change of myofibrillar Z-disks during post-mortem aging. After weakening the structure of Z-disks, the Z-disk region was splitted. As the results, myofibrils were fragmented by mechanical strength. Using indirect immunofluorescence microscopy, we show that the Z-disk domain of titin was disappeared from myofibrils in this period. There phenomenon were also shown by treating myofibrils with a solution containing 0.1mM $Ca^{2+}$. We conclude that change in Z-disk domain of titin is directly effected on the tenderization of meat during post-mortem aging and these change is due to manily calcium ions.

• Food Science of Animal Resources
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• v.32 no.5
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• pp.578-583
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• 2012

The purpose of this study was to evaluate the ultrastructural and shear force changes of duck breast and leg meat during aging at $0^{\circ}C$. Pekin ducks (45 d old) purchased from Greemud Co. were used for this experiment, and were stored at $0^{\circ}C$ for 7 d in order to determine the changes of the meat structure using transmission electron microscopy (TEM) and shear force. At day 0, A-band, I-band, M-line and Z-line of sarcomeres were seen clearly, but sarcomeres started to lose structure and become extended in length from day 2. With extended aging periods, myofibrils were destroyed and symptoms of aging became more obvious. In the duck breast meat, some myofibrils were also destroyed at the Z-line, but were mainly destroyed at the M-line. The change in structure of duck leg meat over time was similar to that of breast meat. After five days and seven days of aging, mitochondria size and quantity were determined to be increased between the myofibrils. Shear force was decreased over time. From this study, aging at $0^{\circ}C$ was found to negatively influence the ultrastructure and shear force of duck meat.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.6
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• pp.994-1001
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• 2007

Changes in shear force value, transverse sections, myofibrils and intramuscular connective tissue of bovine skeletal muscle exposed to the combination of high-pressure up to 400 MPa and heat (30 and $60^{\circ}C$) were studied. The shear force value decreased by pressure-heat treatment up to 200 MPa at 30 and $60^{\circ}C$, and then slightly increased over 200 MPa at $30^{\circ}C$. Shear force values of treated muscles were lower than those of untreated ones. Gaps between muscle fibers in the untreated muscle were a little clear, and then they became very clear in the treated muscles up to 200 MPa at 30 and $60^{\circ}C$. However, the gaps reduced significantly over 200 MPa at $30^{\circ}C$. The remarkable rupture of I-band and loss of M-line materials progressed in the myofibrils with increasing pressure applied. However, degradation and loss of the Z-line in myofibrils observed in the muscle treated at $60^{\circ}C$ was not apparent in the muscle treated at $30^{\circ}C$. The length of the sarcomere initially contracted by pressure-heat treatment of 100 MPa at $30^{\circ}C$ seemed to have recovered with increase of the pressure up to 400 MPa. In the muscle treated at $60^{\circ}C$, the length of sarcomere gradually decreased with increase of the pressure up to 400 MPa. In the treated muscles, changes in the honeycomb-like structure of endomysium were observed and accelerated with increase of the pressure. A wavy appearance clearly observed at the inside surface of endomysium in the untreated muscles gradually decreased in the treated muscles with increase of the pressure. Tearing of the membrane was observed in the muscles treated over 150 MPa at $30^{\circ}C$, as observed in the sample pressurized at 100 MPa at $60^{\circ}C$. The roughening, disruption and fraying of the membrane were observed over 200 MPa at $60^{\circ}C$. From the results obtained, the combination of high-pressure and heat treatments seems to be effective to tenderize tough meat. The shear force value may have some relationship with deformation of intramuscular connective tissue and myofibrils.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 1996.06a
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• pp.50-50
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• 1996

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.1
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• pp.123-130
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• 1989

Myofibrillar protein(myofibil) was prepared from Yellowtail fish (Seriola quinqueradiata), and then, it was stored at $0^{\circ}C$(ice-cooling), $-3.5^{\circ}C$(partial freezing) and $-20^{\circ}C$(freezing). Another myofibrils were prepared from the fish stored with ice-cooling, partial freezing and freezing for a week as the maximum. Denaturation of muscle protein during the storage was investigated by the measurement of $Ca^{2+}-$ and $Mg^{2+}-ATPase$ activity. Specific activity of $Ca^{2+}-\;and\;Mg^{2+}-ATPase$ associated with Yellowtail myofibrils was 0.155 and $0.149\;{\mu}\;mole$ Pi/min/mg of protein, respectively, before storgae. ATPase activity of myofibils did not show any significant difference between $0^{\circ}C$ and $-3.5^{\circ}C$ whereas it was decreased faster at $-20^{\circ}C$ than at $0^{\circ}C$ or $-3.5^{\circ}C$. ATPase activity of myofibirls extracted from the fish stored for a week was 1.2-1.8 times higher than myofibils stored with ice-cooling or partial freezing while it was 2.5-3 times higher than that with freezing. Apparent denaturation constant of $Ca^{2+}-ATPase$ of myofibrils was between 0.48-0.65, and it was 2-3 times higher than that of $Mg^{2+}-ATPase$. The constant of myofibrils extracted from the fish did not show significant difference between $Ca^{2+}-\;and\;Mg^{2+}-ATPase$.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.5
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• pp.721-724
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• 2002

Postmortem Proteolysis of breast (BM) and leg (LM) muscles in Chiayi native chickens at $5^{\circ}C$ were compared. Myofibrils were purified from BM and LM samples that were randomly taken from carcasses after 0, 1, 3, 7 and 14 days of storage at $5^{\circ}C$. Fragmentation of myofibrils were determined, and degradation of myofibrillar proteins were analyzed by the SDS-PAGE and western blots. The results showed that myofibril fragmentation index (MFI) was significantly (p<0.05) higher in BM than in LM samples. Disappearance of titin and nebulin and appearance of the 30 kDa component were more rapidly as seen on SDS-PAGE in BM than in LM samples. Western blots labeled with a monoclonal antibody to desmin also demonstrated that desmin degraded more quickly in BM samples. Our data suggested that postmortem proteolysis occurred more rapidly in breast muscles in Chiayi native chickens.

• Applied Microscopy
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• v.19 no.2
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• pp.85-98
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• 1989

The ventricular myocardia of 14, 16, 18 and 20-day-old rat fetuses and newborns have been studies by light and electron microscopic morphometrics. The volume density of the myocyte and interstitial compartments as well as volume, surface and numerical density of nuclei were estimated by light microscopic morphometrics. Whereas, the volume density of myofibrils and glycogen granules as well as the volume, surface and numerical density of mitochondria were assessed by electron microscopic morphometrics. The volume density of myocyte compartment of the ventricular myocardia in developing fetuses decreased, but increased in newborn rats. On the other hand, the volume density of the interstitial compartment increased in growing fetuses and decreased in newborns. In all groups the volume, surface and numerical density of nuclei decreased gradually with elongation of myocytes. Conversely, the volume, surface and numerical density of mitochondria and volume density of myofibrils and glycogen granules in ventricular myocytes incresed. The increase in numerical density of mitochondria probably reflects an increase in metabolic activity. Sarcomere length also increased during development.