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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 15 (1967), S. 88-94 
    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
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), 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 proteolytic breakdown of the major contractile proteins of bovine longissimus muscle was examined during postmortem storage by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Samples of muscle stored at 4°C for 14 days exhibited little proteolysis of the major contractile proteins; however, samples stored at 37°C for 1 day showed significant degradation of myosin heavy chains and almost complete proteolysis of this protein by day 14. Major degradation products of the myosin heavy chains included a series of polypeptides having molecular weights between 145,000 and 125,000. These experiments demonstrate that substantial degradation of the myosin heavy chain and other muscle proteins can occur during the storage of meat, and this phenomenon was highly temperature dependent.
    Type of Medium: Electronic Resource
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  • 3
    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: Purified cathepsin D was incubated with bovine skeletal muscle myofibrils under in virro conditions resembling those found in postmortem muscle. SDS-PAGE analysis of myofibrils treated at pH 5.5 and 37°C and the sedimented, showed degradation of myosin heavy chains and titin. A small amount of actin, tropomyosin, troponins T and I, and myosin light chains also were degraded. The cathepsin D treated myofibrils were not fragmented to any greater extend than untreated myofibrils. Raising the pH and/or lowering the temperature greatly reduced the effectiveness of cathepsin D suggesting that the enzyme does not play a principal role in the tenderization process occurring in muscle postmortem.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study examined the in vitro effects of calcium-activated protease (CAF) on bovine myofibrillar proteins and structure under postmortem-like conditions of pH and temperature. Effects usually associated with this enzyme under optimal conditions were reduced as temperature and/or pH were lowered. However, significant activity remained at 15°C and pH 6.5, and some activity was detectable at even lower pH's and temperatures. Effects observed included: solubilization of myofibrillar protein, degradation of the myofibrillar protein titin and others, and an increase in the degree of myofibrillar fragmentation. These results suggest that CAF is able to hydrolyze proteins that are important to structural integrity under conditions mimicking those present in postmortem muscle.
    Type of Medium: Electronic Resource
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