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  • 1
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    Cryoprotective effects of chemicals on proteins of fish muscle (2021)
    Marine Fisheries Research Department, Southeast Asian Fisheries Development Center | Singapore
    In:  http://aquaticcommons.org/id/eprint/26865 | 23782 | 2019-11-05 03:25:17 | 26865 | Southeast Asian Fisheries Development Center, Marine Fisheries Research Department
    Details
    Publication Date: 2021-07-24
    Description: A review is made of studies conducted on cryoprotectants for use in the frozen storage of processed fishery products, such as surimi. Some 150 compounds were screened for cryoprotective effects on fish actomyosin; the findings of experiments investigating the behaviour of carp actomyosin, and fish myosin, actin and other constituent proteins during frozen storage are described. The mechanism of freeze denaturation and of the effects of cryoprotectants is outlined and the application of cryoprotectants in the development of new fish gel products considered.
    Keywords: Chemistry ; Fisheries ; Food technology ; Product development ; Freezing storage
    Repository Name: AquaDocs
    Type: book_section
    Format: application/pdf
    Format: application/pdf
    Format: 64-67
    Format: 4
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    PAPER (OA)
  • 2
    Electronic Resource
    Electronic Resource
    Discriminative Characterization of Different Texture Profiles of Various Cooked Fish Muscles (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 49 (1984), 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: Textural differences in cooked fish muscle tissues, according to species, were demonstrated quantitatively by acquiring fresh tissue samples of five species, cooking them under specific conditions, measuring the common physical properties of each (drip, residual weight, fumness, cohesiveness, penetration, fiber volume, fiber diameter, and fiber length) and scoring them in a range of −1.2 to −1.8 for skipjack to 1.0 to 2.0 for channel rock fish using discriminant analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1984.tb13195.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of Ionic Strength on Dynamic Viscoelastic Behavior of Myosin during Thermal Gelation (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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 ionic strength on the thermal gelation process of myosin was investigated by dynamic viscoelasticity measurements. The dynamic viscoelastic behavior of myosin was divided into three ionic strength groups. Each ionic strength group was closely related to the state of myosin molecules before the rise in temperature. Both the head and the tail portions of the molecule participated in the gel formation of myosin, but the temperature ranges differed. It was proposed that the first development of gel elasticity of myosin (30–45 °C) was attributed many to the tail portions of the molecules and that the second development (above 50 °C) was mainly to the head portions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb06014.x
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  • 4
    Electronic Resource
    Electronic Resource
    Role of F-actin in Thermal Gelation of Fish Actomyosin (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 thermal gelation processes of the myosin-natural actomyosin system were investigated to determine the role of F-actin in thermal gelation of actomyosin. The dynamic viscoelastic behavior during thermal gelation changed considerably depending on the (F-actin)/ (myosin) ratio. F-actin gave the viscosity to an actomyosin sol but did not affect the elasticity development occurring in the 30 - 46°C range. The decrease in storage modulus in the 46 - 53°C range was directly induced by the presence of F-actin. The gel of myosin alone showed the highest elasticity, while that of myosin containing a small amount of F-actin had the highest elastic modulus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb07886.x
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  • 5
    Electronic Resource
    Electronic Resource
    Dynamic Viscoelastic Behavior of Natural Actomyosin and Myosin during Thermal Gelation (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), 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 changes in viscoelasticity of natural actomyosin and myosin during thermal gelation were investigated by dynamic viscoelasticity measurements. Thermal gelation of natural actomyosin could be divided into four characteristic temperature ranges. The storage modulus increased considerably in the 32–43°C range, decreased sharply in the 43–52°C range, and then increased again in the 52–80°C range. For the thermal gelation of myosin, the storage modulus increased in two steps at two temperature ranges, i.e., 30–41°C and 51–80°C. An increase in the loss modulus was observed at an early stage of each of the two ranges.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1988.tb08987.x
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  • 6
    Electronic Resource
    Electronic Resource
    Role of Muscle Fibers in Contributing Firmness of Cooked Fish (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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: Cooked muscle tissue of five fish species were observed by optical and scanning electron micrography. Species with firm texture had thin muscle fibers with considerable heat-coagulating material between them; species having soft texture had thick muscle fibers with little heat-coagulating material. When the cooked muscles were compressed by a Texturometer, muscle fibers of the species having firm texture slid or shifted over one another to a lesser extent than those of species with soft texture. The heat-coagulating material seemed to obstruct the displacement of the fibers. The diameter and mobility of muscle fibers are determinative of firmness of fish muscle tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb05208.x
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  • 7
    Electronic Resource
    Electronic Resource
    Paramyosin-Myosin-Actin Interactions in Gel Formation of Invertebrate Muscle (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: Even when actomyosin dissociated into myosin and actin in the paramyosin-natural actomyosin system, the indices of gel properties increased on increasing the paramyosin content; however, their increases were smaller. Also, in the paramyosin-myosin system gels, the indices of gel properties increased on increasing the paramyosin content; however, the increases were smaller than those for the paramyosin-natural actomyosin system gels. In both systems, a high linearity was observed between each index of gel properties and paramyosin. It was likely that the paramyosin-myosin interaction did not bring about the characteristic texture of invertebrate muscle gel directly, but the binding of myosin and actin might be indispensable if the contribution of paramyosin was to occur.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb07885.x
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  • 8
    Electronic Resource
    Electronic Resource
    Contribution of Tropomyosin to Fish Muscle Gel Characteristics (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: To determine the contribution of tropomyosin to fish muscle gel characteristics, the gel properties of the tropomyosin-desensitized actomyosin system and of the tropomyosin-myosin system were investigated. For both systems, the indices of gel properties decreased considerably on increasing the tropomyosin content. Even when the two-step heating was carried out, the indices of gel properties decreased considerably on increasing the tropomyosin content. Tropomyosin negatively affected the gel formation of fish muscle and reduced the gel strength and elasticity of the fish muscle gels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb03056.x
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  • 9
    Electronic Resource
    Electronic Resource
    Carp Natural Actomyosin: Thermal Denaturation Mechanism (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: Structural changes of actomyosin, the major protein of muscle, on heating have been estimated on ATPase activity. We investigated carp actomyosin molecule changes on heating based on biophysical and biochemical techniques. Actomyosin molecules began to unfold at ∼30°C. Hydrophobic amino acid residues and SH groups, which had been inside the molecule, emerged to the surface. Because of hydrophobic interactions and disulfide bonds, actomyosin molecules formed aggregates. At 〉 40°C, a part of myosin molecules was dissociated from actin filaments. Thus, dissociated myosin and the myosin-lacking molecules co-existed. In addition, fragmentation of actin filaments was observed, which was associated with the dissociation of myosin molecules. At ≥ 60 °C actomyosin molecules formed larger aggregates, in which no filamentous shape was observed. This aggregation occurred mainly by formation of SS bonds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb08177.x
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  • 10
    Electronic Resource
    Electronic Resource
    Thermal Gelation Characteristics of Myosin Subfragments (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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: To elucidate the roles of the head and the tail portions of the molecule in the thermal gelation of myosin, the gelation characteristics of heavy meromyosin (HMM) and of light meromyosin (LMM) were investigated. The aggregation process of HMM corresponded to that of myosin alone in the temperature range above 50°C. Both the dynamic viscoelastic behavior and the aggregation process of LMM agreed fairly well with those of myosin alone in the temperature range up to 45 °C. Therefore, the first development of gel elasticity of myosin was attributable mainly to the tail portion of the molecule and the second was to its head portion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb06015.x
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