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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 92 (1970), S. 1488-1493 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 32 (1984), S. 1057-1060 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), 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 semitendinosus muscle was heated at 50, 60 and 90°C for 45 min and was prepared for scanning electron microscopy (SEM) by freeze fracturing parallel to the long axis of the muscle fibers. Samples were dried from ethanol in a stream of nitrogen gas. Topographical features of samples, as viewed by SEM, could be identified as muscle cell components and could be compared after the different heat treatments. The effects of heat on morphology were slight at 50°C but readily apparent at 60 and 90°C. Fracture patterns were similar in raw and 50°C cooked meat, and revealed a tendency to cleave along the lengths of myofibrils. Heating to higher temperatures caused fractures to occur increasingly at fiber surfaces and at Z-lines. Endomysial collagen appeared to be unaffected at 50°C, but was congealed and non-fibrous at 60 and 90°C. The sarcolemma became granular at 60°C. The most important changes in myofibrillar structure at 60 and 90°C were an evident increase in coagulation and compactness of the A-band portion of the sarcomere and disintegration of the I-band with occasional loss of whole sarcomeres from myofibrils. Despite the obvious deterioration of structure, the overall sarcomere array remained remarkably intact. even at 90°C.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), 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 semitendinosus and longissimus dorsi, both freshly slaughtered and aged, were prepared by various techniques prior to examination by SEM. The important problems of sample preparation were freeze damage, production of surface artifacts, and tissue shrinkage. Ethanol freeze fracture of fixed material followed by critical point drying or air drying from solvent circumvented most of the difficulties and provided the most useful specimens. Cleavage of muscle tissue by freeze fracture exposed muscle cell structures for observation. Useful magnifications up to 20,000 × were obtained and identification was made of A, I and H bands, nuclei, and structures suggestive of mitochondria and muscle cell triads. The structural consequences of cold shortening and rigor were observed.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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