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  • 2000-2004  (2)
  • 2001  (2)
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  • 2000-2004  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), 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 factors affecting myosin degradation that occurred during aging following high-pressure treatment over a pressure range from 200 to 600 MPa were investigated by using SDS-PAGE and immunoblotting analysis. The immunoblot pattern of myosin in muscle stored at 37°C for 48 h after pressure treatment at 0. 1 MPa (atmospheric pressure) or 200 MPa for 5 min was similar to that of native myosin incubated with cathepsin D, whereas at 400 or 600 MPa the pattern was close to that of native myosin incubated with cathepsin B. This phenomenon was reflected in the pressure-susceptibilities of cathepsins B and D as reported in the literature (Homma and others 1994). However, these catheptic enzymes released by pressure treatment are unlikely to play a role in pressure-induced tenderization of meat.
    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 66 (2001), 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: : Changes of chicken breast myosin during storage at 2°C and 37°C were monitored immunochemically. Anti-myosin subfragment-1 (S-1) monoclonal antibody, which recognized epitopes within the 27 kDa fragment of S-1, and the anti-myosin rod polyclonal antiserum, were prepared. Myosin degradation products were not detected in muscle extracts stored for 3 weeks at 2°C. In contrast, storage at 37°C brought about the degradation of myosin heavy chain to immunologically detectable small fragments. While, myosin rod produced during the conditioning period was not decomposed into any small filaments. Namely, storage of muscle at 37°C resulted in minor amounts of myosin heavy chain degradation, with initial conversion to rod and S-1 fragments, and subsequent breakdown occurred in the S-1 region only. Immunoblot assay also suggested that the pattern of changes in myosin heavy chain in muscle incubated at 37°C was similar to that produced by in vitro digestion with cathepsin D.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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