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  • 1985-1989  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 51 (1986), 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 effect of low-calcium-requiring calcium-activated factor (μM CAF) on the myofibrils under varying pH at 5°C and 25°C was examined spectrophotometrically (absorbance at 278 nm), electrophoretically (sodium dodecyl sulfate polyacrylamide gel electrophoresis), and microscopically (phase microscopy and transmission electron microscopy). Results indicated that at conditions similar to those of postmortem storage (i.e., pH 5.5–5.8 and 5°C), μM CAF retained 24–28% of its maximum activity (pH 7.5 at 25°C). This 24–28% of maximum activity was sufficient to reproduce most of the known changes associated with the tenderization process during postmortem aging. It was concluded that because of the activity of μM CAF under postmortem conditions, it seems reasonable to suggest that μM CAF may be responsible, in part, for some of the postmortem changes observed.
    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: Bovine sternomandibularis muscles were excised immediately following animal exsanguination for the study of collagen fibers and connective tissue network. Samples were cooked at 60°C or 80°C for 1 hr and were observed using the scanning electron microscope. An ordered array of collagen fibers was seen in the uncooked sample. The epimysium did not show large alterations after cooking; however, the perimysium and endomysium became granular at 60°C and gelatinized at 80°C. These differences may be related to the type of collagen or degree of crosslinking present in each location.
    Type of Medium: Electronic Resource
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