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  • Electronic Resource  (2)
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  • Electronic Resource  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of food science & technology 9 (1974), S. 0 
    ISSN: 1365-2621
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: In an attempt to explain the paradoxical tenderizing, observed when muscle shortening exceeds about 40% of the initial excised length, the fine structure of highly cold-shortened muscle has been studied by light and electron microscopy. Tissue at the ‘peak’ of toughness is uniformly shortened and shows no sign of structural weakness or damage, but with further shortening super-contraction and node formation take place in an increasing proportion of the sarcomeres. Widespread fibre fracturing is seen in the internodal zones when the length change has exceeded about 50%. This disruption appears sufficient to account for the declining toughness which accompanies supra-physiological shortening.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), 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: SUMMARY: During the aging of beef, the external loading required to stretch sterno- mandibularis muscle to its fullest extent declines 5-10-fold from the maximum of 2 Kg/cm2 muscle attained at rigor onset. This loss of tensile strength is due to a weakening of the myofibrillarstructures at the junction of the I filaments with the Z discs of the sarcomeres. The Z discs undergo progressive changes and lose ground substance as aging proceeds. There is no obvious structural change in the I filaments during aging although a weakening in the association of the constituent proteins of these structures apparently occurs.
    Type of Medium: Electronic Resource
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