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  • 1990-1994  (4)
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 41 (1993), S. 372-379 
    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
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 38 (1990), S. 824-829 
    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
    ISSN: 1573-4943
    Keywords: Thermodynamic linkage ; ligand-induced associations ; caseins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The caseins occur in milk as colloidal complexes of protein aggregates, calcium, and inorganic phosphate. As determined by electron microscopy, these particles are spherical and have approximately a 650 Å radius (casein micelles). In the absence of calcium, the protein aggregates themselves (submicelles) have been shown to result from mainly hydrophobic interactions. The fractional concentration of stable colloidal casein micelles can be obtained in a calcium caseinate solution by centrifugation at 1500g. Thus, the amount of stable colloid present with varying Ca2+ concentrations can be determined and then analyzed by application of equations derived from Wyman's Thermodynamic Linkage Theory. Ca2+-induced colloid stability profiles were obtained experimentally for model micelles consisting of only α s1- (a calcium insoluble casein) and the stabilizing protein κ-casein, eliminating the complications arising from β- and minor casein forms. Two distinct genetic variants α s1-A andB were used. Analysis of α s1-A colloid stability profiles yielded a precipitation (salting-out) constantk 1, as well as colloid stability (salting-in) parameterk 2. No variations ofk 1 ork 2 were found with increasing amounts of κ-casein. From the variation of the amount of colloidal casein capable of being stabilized vs. amount of added κ-casein an association constant of 4 L/g could be calculated for the complexation of α s1-A and κ-casein. For the α s1-B and κ-casein micelles, an additional Ca2+-dependent colloidal destabilization parameter,k 3, was added to the existingk 1 andk 2 parameters in order to fully describe this more complex system. Furthermore, the value ofk 3 decreased with increasing concentration of κ-casein. These results were analyzed with respect to the specific deletion which occurs in α s1-caseinA in order to determine the sites responsible for these Ca2+-induced quaternary structural effects.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The lipase found in oat seeds acts upon castor oil in organic solvent, yielding approximately 90% ricinoleic acid. Initial velocity is a poor predictor of the time required for complete lipolysis except at low oil concentrations. Equations were developed to estimate kinetic parameters necessary to accurately predict the degree of lipolysis.
    Type of Medium: Electronic Resource
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