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  • 1
    Electronic Resource
    Electronic Resource
    Proteolysis Affects Thermal Gelation of Squid Mantle Muscle (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 57 (1992), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Thermal gelation of squid mantle muscle was studied by means of gel strength measurement and SDS-polyacrylamide gel electrophoresis. The gel strength of thermally induced squid meat gel decreased when squid meat paste was heated in two steps (35°C for 30 min followed by 90°C for 30 min). This decrease in gel strength was effectively depressed by the addition of protease inhibitors such as ethylenediaminetetraacetic acid (EDTA), phenylmethylsulfonyl fluoride (PMSF), and soybean trypsin inhibitor, indicating that me-tallo- and/or serine-proteases were mainly involved in the deterioration of squid meat gel prepared by two-step heating. SDS-PAGE analysis demonstrated that EDTA or PMSF suppressed the degradation of myosin heavy chain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1992.tb14322.x
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Pressure Treatment on Actomyosin ATPases from Flying Fish and Sardine Muscles (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of pressure treatment (1 atm ∼ 5000 atm) on flying fish and sardine actomyosin ATPases was studied from the standpoint of interaction between myosin and actin. The activities of actomyosin Mg-ATPases markedly decreased and those of the EDTA-ATPases rapidly increased with prolonged pressure treatment at 3000 atm and 5000 atm. Changes in activities of F-actin plus pressure-treated myosin Ca-ATPases showed results similar to those of pressure-treated actomyosin Ca-ATPases, while myosin plus pressure-treated F-actin resulted in decreased Mg-ATPase activity and increased EDTA-ATPase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb05275.x
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of Ultraviolet Irradiation on Thermal Gelation of Muscle Pastes (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The role of the actomyosin denaturation in the thermal gelation of muscle pastes by ultraviolet (UV) irradiation was studied. The pastes and actomyosins were obtained from sardine, beef, and pork. When UV irradiation (2,700 μW/cm2) from a photochemical mercury-arc lamp was applied to the pastes, the surface gel strength of thermal gels markedly increased with prolonged irradiating time. The effect of UV at 360 nm on the sardine gels was superior to that at 250 nm. UV denaturation of actomyosin ATPases revealed that activation of Mg-ATPase and decrease of EDTA-ATPase occurred simultaneously. The possible role of UV irradiation in the thermal gelation was discussed from the point of actomyosin ATPases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb05129.x
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  • 4
    Electronic Resource
    Electronic Resource
    Thermal Activation of Actomyosin Mg-ATPases from Ordinary and Dark Muscles of Tuna and Sardine (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Changes in activities of actomyosin, acto-heavy meromyosin (acto-HMM), and acto-subfragment-I (acto-S-I) ATPases from tuna and sardine due to heat treatment (20°, 25°, 30°, 35°, 40°C) were compared for ordinary muscle and dark muscle. Activation of ordinary muscle actomyosin Mg-ATPases was more than doubled for tuna and tripled for sardine by heating at 35°C, while activation of dark muscle actomyosin was not observed at any temperature. The occurrence of thermal activation corresponded to a rapid loss of the EDTA-ATPase activity. Activation of hybrid actomyosins from dark and ordinary muscles was dependent upon myosin. For acto-HMM and acto-S-I thermal activation was not observed. The role of myosin tail fragments in thermal activation is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb05150.x
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  • 5
    Electronic Resource
    Electronic Resource
    Fish Myosin Fragments Solubility and ANS-Fluorescence Intensity Affected by n-Butanol (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 59 (1994), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Changes in the solubility and 8-anilino-1-napthalene sulfonate (ANS)-fluorescence intensity of oval filefish, tilapia, and black marlin myo-sins and their fragments by n-butanol were examined in connection with myosin gel-forming abilities. The thermal gel-forming abilities of myosins were greatly enhanced by the addition of 0.3–0.8M n-butanol. KC1 concentration-solubility curves revealed that after n-butanol addition a marked decrease in the solubility was observed for myosins and S-1s, whereas there was a slight decrease for rods. The fluorescence intensity of myosins-ANS in the presence of n-butanol increased markedly by heating at 30° and 35°C. A similar increase in the fluorescence intensity occurred in all S-ls-ANS, but not in rods.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb06906.x
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  • 6
    Electronic Resource
    Electronic Resource
    Thermal Transitions of Myosins/Subfragments from Black Marlin (Makaira mazara) Ordinary and Dark Muscles (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Thermal transitions were studied by means of differential scanning calorimetry (DSC) and a spectrophotometric method. Three endothermic peaks (40, 43, 50°C: ordinary muscle; 46, 54, 62°C: dark muscle) were observed in DSC thermograms of both myosins. Thermograms of S-l fragments showed one peak (41°C: ordinary muscle, 43°C: dark muscle). But ordinary and dark muscle rod fragments gave two peaks (41, 62°C) and one peak (58°C), respectively. The spectrophotometric results also showed two thermal transitions for both myosins and one transition for their S-1 fragments. However, the rod from ordinary muscle myosin had two transitions, whereas that from dark muscle myosin had one transition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb14614.x
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  • 7
    Electronic Resource
    Electronic Resource
    Protein-Protein Interaction of Fish Myosin Fragments (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Protein-protein interaction of myosin fragments from flying fish and white marlin muscles was studied by means of absorbance changes resulting from aggregation at temperatures of 20°C to 70°C. Subfragment-1 (S-1) exhibited a high extent of interaction with the transition temperature of 35–36°C, while the interaction of heavy meromyosin (HMM) was very weak. Though light meromyosin (LMM) gave lower interaction values throughout the heating temperature, the addition of butanol promoted markedly the interactions at the temperature above 50°C. The degree of promotion was high for flying fish and low for white marlin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb14287.x
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  • 8
    Electronic Resource
    Electronic Resource
    Thermal Activation of Actomyosin Mg2+-ATPases from Flying Fish and Black Marlin Muscles (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 51 (1986), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of heat treatment (25°, 30°, 35°, 37°, and 40°C) on acto-myosin Mg2+-ATPase activity from flying fish and black marlin were studied with respect to setting of their meat pastes. The setting ability of flying fish had very high values but black marlin was low. Flying fish actomyosin Mg2+ATPase was activated more than three times by heating at 35°C, while the activation of black marlin was about two-thirds at 37°C. For acto-HMM ATPase, however, no appreciable difference in activation was observed between flying fish and black marlin. For both fishes, the acto-S-1 ATPase activities were not enhanced by the heat treatment. A possible role of myosin fragments in this activation is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1986.tb13822.x
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