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  • Blackwell Publishing Ltd  (2)
  • Wiley-Blackwell
  • 1985-1989  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), S. 0 
    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 microstructural changes in ice-chilled and cooked prawn, M. rosenbergii were studied with the scanning electron microscopy (SEM) and transmission electron microscopy (TEM) techniques. The SEM study revealed muscle fibers in the control samples were wrapped in bundles by the endomysium and subsequently by the perimysium. During ice-chilling, degradation of these intact structures proceeded gradually. The TEM study showed the organized myofilaments of muscle fiber, presence of M line in the H Zone, and abundance of sarcoplasma in the controlled sample. During ice-chilling, the disappearance of sarcoplasma and the fine structure of myofilaments in the H Zone was clearly demonstrated. These findings supported previous observations of mushiness development and textural changes under similar conditions.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    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 changes of freshwater prawn during ice-chilled/refrigerated storage are believed in part to be due to an autolytic process. A collagenolytic enzyme fraction, isolated from the hepatopancreas of the freshwater prawn, was most active at 37°C and pH 6.5-7.5 and was also active at 0°C. The addition of this enzyme fraction to prawn tissue increased the hydrolysis of prawn collagen at 0°C for 96 hr indicating that this enzyme fraction might be responsible for the textural change in prawn during ice-chilled storage.
    Type of Medium: Electronic Resource
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