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  • 1
    Electronic Resource
    Electronic Resource
    Studies in Meat Tenderness II. Proteolysis and the Aging of Beef (1966)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 31 (1966), S. 0 
    Details
    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 changes which occur in the longissimus dorsi muscles of beef carcasses during 30 days' aging at 2°C give rise to a mean increase of nonprotein nitrogen of 0.045mM/g meat, representing a degradation of 2.3% of the meat protein. The tenderizing and proteolysis which occur during aging are not related, for differences in the rates of tenderizing among carcasses arc not paralleled by similar differences in the rates of proteolysis. Bacterial action is not responsible for the observed proteolytic and tenderizing changes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1966.tb00467.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Studies in Meat Tenderness. 7. Changes in the Fine Structure of Meat During Aging (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 34 (1969), S. 0 
    Details
    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 fiber pieces prepared from bovine sternomandibularis muscles, a loss of adhesion occurs between adjacent myofibrils. This is evidenced by increased readiness of fiber pieces to distintegrate into individual myofibrils during a period of standard disruption. Alterations also appear within the myofibrils themselves in the regions of the Z lines, sometimes leading to the apparent dissolution of this structure. Ethylenediamine tetraacetate present in the suspensions during storage not only prevents these changes, but also preserves the refractory character of the fiber pieces. Meat aging is considered therefore to be due to disruption and possible dissolution of Z-line material, leading to a weakening of inter-myofibrillar linkages probably located at the junctions of adjacent Z lines, and to loss of tensile strength of the myofibrils themselves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb14364.x
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  • 3
    Electronic Resource
    Electronic Resource
    Studies in Meat Tenderness. (1968)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 33 (1968), S. 0 
    Details
    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— Changes during aging in the extractability of the myofibrillar proteins of meat from beef and rabbit carcasses have been examined, using a buffer which dissociates the actomyosin complex of the muscle cell. Approximately 52% of the myofibrillar proteins of unaged meat is extracted in 40 min at 2°C whereas from aged meat as much as 78% is extracted.The rate and extent of these changes are determined largely by the ultimate pH value of the meat. Similar increases in protein extraction, displaying the same pH dependence, occur during the aging of well-washed myofibrillar preparations.The increase in the percentage of myofibrillar protein extracted during aging results from either a progressive weakening of the fibrous protein linkages with the insoluble stroma of the meat cell, or from a disintegration of the insoluble stroma itself.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1968.tb00873.x
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  • 4
    Electronic Resource
    Electronic Resource
    Studies in Meat Tenderness. 6. The Nature of Myofibrillar Proteins Extracted from Meat During Aging (1968)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 33 (1968), S. 0 
    Details
    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– A study has been made of the myofibrillar proteins extracted from beef and rabbit meat by a buffer that dissociates the actomyosin complex of the muscle cell. Myosin, which constitutes 50-52 per cent of the myofibrillar protein, can be wholly extracted throughout aging, whereas actin can be extracted in increasing amounts as aging proceeds. In contrast, tropomyosin cannot be extracted and remains firmly held within the myofibrillar structures throughout aging. A complex mixture of extra protein, soluble at low ionic strength, is also released in increasing quantity during aging. It is proposed that in meat aging there is a progressive loss of the tensile strength of the myofibrillar component of muscle brought about by the weakening and final dissolution of the Z-band structures. Such a disintegration would lead to the observed changes in the extractabilities of the myofibrillar proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1968.tb03627.x
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