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  • 1
    Electronic Resource
    Electronic Resource
    Changes in the Melting Characteristics of Bovine Tendon Collagen Induced by a Bacterial Collagenase (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 51 (1986), 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: Differential scanning calorimetry was used to study the changes produced by a commercial Clostridium histolyticum collagenase preparation on the melting behavior of bovine Achilles tendon collagen. The samples were heated at 5°C/min from 25 to 100°C. As a result of proteolysis, the collagenase-treated samples were partially gelatinized at 25°C and, during the calorimetric experiments, exhibited significant decreases in their melting transition parameters when compared to intact collagen. The denaturation temperatures and enthalpies obtained were 61.6°C and 44.4 J/g sample for intact collagen and 43.6°C and 26.1 J/g sample for collagenase-treated collagen. These differences may be accounted for by changes produced in the structural organization of the collagen fibrils by the collagenase treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1986.tb13944.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Stability of Bovine Muscle Connective Tissues (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), 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: Endomysium, perimysium and epimysium were isolated from beef stemomandibularis muscle. The susceptibilities of these fractions to degradation by a C. histolyticum collagenase preparation were tested; highest proteolysis was found in the perimysium, followed by epimysium and endomysium. The thermal stability of samples obtained from animals of two different age groups was studied by differential scanning calorimetry; although age had no effect on stability, in both age groups the stability of endomysium was significantly lower than those of the other two fractions. These differences may be related to the type of structural arrangement, collagen composition and the non-collagenous components present in the connective tissue fractions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb14231.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Interactions in Protein/Polysaccharide/Calcium Gels (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), 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: Protein-polysaccharide-calcium gels were prepared using combinations of crude myofibrillar protein, whey protein concentrate, sodium alginate, methylcellulose, low methoxyl pectin, carrageenan and CaCl. The nature of the interactions taking place in the gels and the effect of freezing or heating on viscosities and water losses were investigated. In most cases the stability of the gels was increased by freezing and lowered by heating. Myofibrillar protein with added whey protein concentrate formed stronger gels with the polysaccharide gums than did the myofibrillar protein extract alone. With the exception of methylcellulose gels, electrostatic interactions seemed to be the main forces involved in the formation and stability of the gels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb14023.x
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    Paper (German National Licenses)
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