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  • 1
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    Problems of post-harvest technology in Southeast Asia (2021)
    Marine Fisheries Research Department, Southeast Asian Fisheries Development Center | Singapore
    In:  http://aquaticcommons.org/id/eprint/26857 | 23782 | 2019-11-05 05:20:59 | 26857 | Southeast Asian Fisheries Development Center, Marine Fisheries Research Department
    Details
    Publication Date: 2021-07-24
    Description: Improvement of post-harvest technology in Southeast Asian countries and the various problems involved are discussed, considering the following topics: fresh fish handling; traditional products; fish products for export; utilization of available resources for direct human consumption; and, the role of post-harvest technologies.
    Keywords: Fisheries ; Fish handling ; Food technology ; Quality control ; Fishery products ; South East Asia
    Repository Name: AquaDocs
    Type: book_section
    Format: application/pdf
    Format: application/pdf
    Format: 3-8
    Format: 6
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  • 2
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    A simple way to maintain the fish processing industry (2021)
    Marine Fisheries Research Department, Southeast Asian Fisheries Development Center | Singapore
    In:  http://aquaticcommons.org/id/eprint/26682 | 23782 | 2019-08-15 02:07:40 | 26682 | Southeast Asian Fisheries Development Center, Marine Fisheries Research Department
    Details
    Publication Date: 2021-07-24
    Description: This paper emphasizes that efforts in the upgrading of the fish processing industry in Southeast Asia should be directed at each country s traditional fish products. In the coming era, the increase in food production may not match the world s population growth. In this respect, the major challenge for the fish processing industry is the utilization of all fish caught. Emphasis on development of new products might be one area of responsibility. However, this paper stresses the importance of traditional fish products of each country because these products have survived many decades without any assistance from government or perhaps even society. In other words, there must be some reason for their existence. When fish technologists are able to help the traditional fish products industry, the industry will play a more powerful role in the future. This paper focuses on a simple and fast way of boosting the fish processing industry in the region by emphasizing on the upgrading of existing traditional fish products.
    Keywords: Fisheries ; Fishery industry ; Processing fishery products ; Fishery products
    Repository Name: AquaDocs
    Type: book_section
    Format: application/pdf
    Format: application/pdf
    Format: 3-5
    Format: 3
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  • 3
    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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  • 4
    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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  • 5
    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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  • 6
    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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  • 7
    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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  • 8
    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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