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  • 1
    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
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 2450-2454 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 29 (1981), S. 11-15 
    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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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 32 (1984), S. 474-476 
    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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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 43 (1995), S. 2574-2579 
    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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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 3 (1988), S. 61-71 
    ISSN: 1476-5535
    Keywords: Casein ; Solubility profile ; Primary structure ; Posttranslational modification ; Protein functionality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Molecular biology holds the promise of new tools for the food industry which include proteins with tailor-made functionality. Without a fundamental knowledge of the molecular bases of these properties, implementation will be strictly empirical. For example, the phenomena of salt-induced precipitation of proteins (salting-out) and their resolubilization (salting-in) has heretofore been discussed only qualitatively. A quantitative method, using Wyman's theory of thermodynamic linkage, has been developed and tested on the calcium-induced solubility profiles of the major milk proteins, the caseins. Salting-out was described by a salt-binding constant,k 1, andn, the number of moles of salt bound; salting-in was described by the corresponding termsk 2 andm. The magnitude of these parameters indicated involvement of protein phosphate groups in binding and precipitation, but enzymatic dephosphorylation showed significant increases ink 1 andk 2 indicating involvement of carboxylate groups as well. Studies on two genetic variants of αs1-casein indicated the importance of a hydrophobically stabilized intramolecular ion pair in the functionality of the protein. These studies have led to a fuller understanding of the molecular basis for the solubility behavior of caseins and have laid the groundwork for future computer simulation of food protein functionality.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 3 (1988), S. 89-103 
    ISSN: 1476-5535
    Keywords: Food protein ; Milk protein ; Egg protein ; Protein structure, tertiary ; Small-angle scattering ; β-Lactoglobulin ; α-Lactalbumin ; Lysozyme ; Ribonuclease ; Riboflavin-binding protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary With current emphasis in bioengineering on developing new and better structure-function relationships for proteins (e.g., the need for predictability of expected properties prior to cloning), practical and reliable methodology for providing characterization of appropriate features has become of increasing importance. The most potent and detailed technique, X-ray crystallography, has severe limitations: it is so demanding and time-consuming that X-ray coordinates are frequently unavailable for materials of interest; its data relate to static and essentially unhydrated structures, whereas proteins exhibit a variety of dynamic features and function in an aqueous environment; and many proteins of technological importance may never be crystallized. Small-angle X-ray scattering, however, is particularly suitable as a methodology that can provide a substantial number of significant geometric parameters consistent with crystallographic results, that can readily show tertiary structural changes occurring under varying conditions, and that can deal with solutions and gels. Results are presented here from small-angle X-ray scattering investigations of the apo and holo forms of chicken egg-white riboflavin-binding protein, chicken egg-white lysozyme, bovine milk-whey α-lactalbumin and β-lactoglobulin, and bovine ribonuclease. We utilize these observations to compare tertiary structures of these proteins as well as conformational changes in these structures, and to provide a basis for discussion of their physical and biological significance.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1476-5535
    Keywords: Bacterial growth retardation ; Suppression of the activity of water ; Protein hydration ; Deuterium NMR relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Food microbiologists have long known that suppression of the activity of water,a w, can retard microbial growth in food systems. Traditionally,a w, suppression has been achieved by addition of salts or humectants to foods. To limit the amount of preservatives added to food products, studies were initiated to assess the feasibility of using proteins to suppressa w to a practical value for retarding bacterial growth and to determine the optimum environmental condition for maximizing this effect for milk proteins. New expressions were developed relating observed longitudinal and transverse NMR relaxation rates, in the absence of cross-relaxation, to protein hydration $$\bar \upsilon _w $$ , to the protein activity coefficient, γp, and to the correlation time of the bound water, τc. From γp, the second virial coefficient of the protein,B o, can be found. By use of $$\bar \upsilon _w $$ andB o,a w could then be directly evaluated at any protein concentration. Resulting expressions were tested by2H-NMR relaxation measurements made as a function of protein concentration, for: β-lactoglobulin A (the major whey protein) under nonassociating (pH 6.0) and associating (pH 4.65) conditions; and for casein (the major milk protein) in the micellar (with added Ca2+) and submicellar (without Ca2+) forms. Values ofa w calculated from these2H-NMR data show that casein, at all the concentrations and temperatures examined, suppressesa w more than does β-lactoglobulin A because of a largerB o. In turn, micellar casein suppressesa w to a larger extent than does submicellar casein because of a larger $$\bar \upsilon _w $$ . Extrapolation ofa w at 4°C to a concentration ten times that in normal milk yields a value, ofa w of less than 0.95, at whichSalmonella and some strains ofClostridium botulinum no longer grow. These results are in agreement with what is known about storageability of condensed milk. Generalizations regarding the types of proteins and cosolutes to be used for suppressinga w will be discussed. Structural information on these proteins calculated from τc will also be presented.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 19 (2000), S. 85-92 
    ISSN: 1573-4943
    Keywords: Soluble collagen ; thermal stability ; NaCl ; KCl
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The thermal stability of acid-soluble collagens was studied by circular dichroism (CD) spectroscopy. Adult bovine dermal collagen (BDC), rat-tail tendon collagen (RTC), and calf skin collagen (CSC) were compared. Despite some variability in amino acid composition and apparent molecular weight, the CD spectra for helical and unordered collagen structures were essentially the same for all the sources. The melting of these collagens occurs as a two-stage process characterized by a pretransition (T p) followed by complete denaturation (T d). The characteristic temperatures vary with the source of the collagen; for mature collagens (BDC, RTC) T p = 30°C and T d = 36deg;C, and for CSC T p = 34°C and T d = 40°C. Neutral salts, NaCl or KCl, at low concentrations (0.02–0.2 M) appear to bind to the collagens and shift the thermal transitions of these collagens to lower temperatures.
    Type of Medium: Electronic Resource
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