Quality improvement of tilapia fillets by light salting during repeated freezing-thawing: Contribution of structural rearrangement and molecular interactions
14
Citation
33
Reference
10
Related Paper
Citation Trend
Keywords:
Salting
Myofibril
Texture (cosmology)
The research was aimed to know the method of fish skin preservation by salting to obtain good physical quality of Tilapia fish skin leather tanned by chrome.
It was concluded that for fish skin preservation before tanning is by using crystal salt on salting process.
Salting
Aquaculture of tilapia
Cite
Citations (0)
ABSTRACT Purified chicken myofibrils were suspended in 0.6M NaCl at various pH values to study gelation properties of the myofibrils. Postrigor breast myofibrils showed a greater protein extractability and gel strength than prerigor breast myofibrils, but the reverse was found for leg myofibrils. Salt‐soluble protein was least extractable at pH 5.50 for both breast and leg myofibrils. The pH for optimum gelation, indicated by increased penetration force, was 6.00 for breast and 5.50 for leg myofibrils. Heating at 1°C/min from 20 to 70°C produced stronger breast but weaker leg myofibril gels than isothermal heating at 70°C for 20 min. Muscle rigor state showed a greater effect on protein extractability and gel strength for breast myofibrils than for leg myofibrils.
Myofibril
Cite
Citations (92)
The ATPases of activated and relaxed rabbit psoas myofibrils were studied by the rapid flow quench method in a solvent of near physiological pH and ionic strength. Both types of myofibrils bind and hydrolyze ATP with transient kinetics very similar to those found with myosin. But the kcat of activated myofibrils was 100× that with the relaxed myofibrils. Relaxed myofibrils and myosin could not be distinguished kinetically.
Myofibril
Cite
Citations (0)
Myofibril
Cite
Citations (52)
Adenosine triphosphatase (ATPase) activity of myofibrils isolated from fresh muscle and the muscle stored at 4°C have been measured. An increase in Mg-activated ATPase activity of myofibrils was caused by lengthened homogenization. With the progress of aging of muscle, Mg-activated ATPase activity of myofibrils increased remarkably. When myofibrils from pre-rigor and rigor muscle in 0.16M KCl were treated with 0.6M KCl18mM Tris-maleate solution (pH 7.0), Mg-activated ATPase activity of myofibrils at low ionic strength increased markedly. However, the Mg-activated ATPase activity of the myofibril isolated from the muscle stored at 4°C for 8 days (8-myofibril) increased slightly after the similar treatment. The dependence of myofibrillar ATPase activity on KCl concentration became greater with the progress of aging of muscle. These results may show that, as long as ATPase activity and the dependence of ATPase activity on KCl concentration are concerned, 8-myofibril is the most similar to the isolated actomyosin among myofibrils, although actomyosin in muscle may exist in a different form from that in solution. It is suggested that, with the progress of aging, the structural alteration of myofibril occurred and the myofibril became more susceptible to ATP-induced transformation.
Myofibril
Cite
Citations (16)
Abstract Tilapia ( Oreochromis niloticus ) was processed by varying salting time (0‐24 h), drying time (6‐20 h) and drying temperature (40‐60°C) using the central composite rotatable design. Equations for predicting objective and subjective indices were developed. The critical salting times for attaining minimum moisture were 20.5, 12 and 8.5 h, respectively, for products dried at 40, 50 and 60°C. At each salting time the mean hardness score was dependent on the drying temperature and time whilst the mean colour and acceptability scores were influenced by the drying temperature. Salting and drying conditions could be manipulated to produce salted‐dried tilapia of acceptable quality.
Salting
Central composite design
Dried fish
Cite
Citations (17)
Abstract When cardiac muscle cells are isolated from embryonic chicks and grow in culture they attach to the substrate as spherical cells with disrupted myofibrils, and over several days in culture, they spread and extend lamellae. Based on antibody localizations of various cytoskeletal proteins within the spreading cardiomyocyte, three types of myofibrils have been identified: 1) fully formed mature myofibrils that are centrally positioned in the cell, 2) premyofibrils that are closest to the cell periphery, and 3) nascent myofibrils located between the premyofibrils and the mature myofibrils. Muscle‐specific myosin is localized in the A‐bands in the mature, contractile myofibrils, and along the nascent myofibrils in a continuous pattern, but it is absent from the premyofibrils. Antibodies to non‐muscle isoforms of myosin IIB react with the premyofibrils at the cell periphery and with the nascent myofibrils, revealing short bands of myosin between closely spaced bands of α‐actinin. In the areas where the nascent myofibrils border on the mature myofibrils, the bands of non‐muscle myosin II reach lengths matching the lengths of the mature A‐bands. With the exception of a small transition zone consisting of one myofibril, or sometimes several sarcomeres, bordering the nascent myofibrils, there is no reaction of these non‐muscle myosin IIB antibodies with the mature myofibrils in spreading myocytes. C‐protein is found only in the mature myofibrils, and its presence there may prevent co‐polymerization of non‐muscle and muscle myosins. Antibodies directed against the non‐muscle myosin isoforms, IIA, do not stain the cardiomyocytes. In contrast to the cardiomyocytes, the fibroblasts in these cultures stain with antibodies to both non‐muscle myosin IIA and IIB. The premyofibrils near the leading edge of the lamellae show no reaction with antibodies to either titin or zeugmatin, whereas the nascent myofibrils and mature myofibrils do. The spacings of the banded α‐actinin staining range from 0.3 to 1.4 μm in the pre‐ and nascent myofibrils and reach full spacings (1.8‐2.5 μm) in the mature myofibrils. Based on these observations, we propose a premyofibril model in which non‐muscle myosin IIB, titin, and zeugmatin play key roles in myofibrillogenesis. This model proposes that pre‐ and nascent myofibrils are composed of minisarcomeres that increase in length, presumably by the concurrent elongation of actin filaments, the loss of the non‐muscle myosin II filaments, the fusion of dense bodies or Z‐bodies to form wide Z‐bands, and the capture and alignment of muscle myosin II filaments to form the full spacings of mature myofibrils. © 1994 Wiley‐Liss, Inc.
Myofibril
Myofilament
Cardiac muscle
Cite
Citations (328)
Adenosine triphosphatase (ATPase) activity of myofibrils isolated from fresh muscle and the muscle stored at 4°C have been measured. An increase in Mg-activated ATPase activity of myofibrils was caused by lengthened homogenization. With the progress of aging of muscle, Mg-activated ATPase activity of myofibrils increased remarkably. When myofibrils from pre-rigor and rigor muscle in 0.16 m KCl were treated with 0.6 m KCl-18 mm Tris-maleate solution (pH 7.0), Mg-activated ATPase activity of myofibrils at low ionic strength increased markedly. However, the Mg-activated ATPase activity of the myofibril isolated from the muscle stored at 4°C for 8 days (8-myofibril) increased slightly after the similar treatment. The dependence of myofibrillar ATPase activity on KCl concentration became greater with the progress of aging of muscle. These results may show that, as long as ATPase activity and the dependence of ATPase activity on KCl concentration are concerned, 8-myofibril is the most similar to the isolated actomyosin among myofibrils, although actomyosin in muscle may exist in a different form from that in solution. It is suggested that, with the progress of aging, the structural alteration of myofibril occurred and the myofibril became more susceptible to ATP-induced transformation.
Myofibril
Cite
Citations (11)
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.
Myofibril
Tropomyosin
Cite
Citations (0)
Abstract Vacuum steam pulsed blanching (VSPB) was employed as a novel blanching technology on Cornus officinalis to soften the tissue for subsequent coring and dehydration. The current work aims to explore its effect on mass transfer behavior, PPO inactivation, drying characteristics, physicochemical properties, antioxidant capacity, and microstructure of C. officinalis . Results showed that VSPB increased water loss, decreased solid gain, and increased weight reduction with increased blanching cycles. Besides, VSPB significantly changed physical properties and extensively reduced drying time which was attributed to the cell wall components dissolving and cell turgor pressure decreasing, also verified by observing microstructure alteration. PPO was completely denatured after blanching in 6 cycles, but phenolic compounds were still diffused or degraded. Notably, the content of flavonoids and antioxidant capacity significantly increased compared to fresh samples probably due to increased extractability caused by the disrupting cell structure. Besides, the carotenoids and ascorbic acid could be well preserved.
Blanching
Sinigrin
Cite
Citations (4)