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  • Fourier transform infrared spectroscopy  (1)
  • NaCl  (1)
  • Protein hydration  (1)
  • 1
    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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  • 2
    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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  • 3
    ISSN: 1573-4943
    Keywords: Calcium binding ; casein structure ; Fourier transform infrared spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract κ-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE. The disulfide-bonded caseins present range from dimer to octamer and above and preparations contain about 10% monomer. All of these heterogenous polymers, however, self-associated into nearly spherical uniform particles with an average radius of 8.9 nm as revealed by negatively stained transmission electron micrographs. Evidence is presented that multivalent cations play a role in the stabilization of these spherical particles. Treatment with EDTA causes disruption of theκ-casein particles and leads to a broader size distribution as judged by electron microscopy and dynamic light scattering. The size and shape of the particles are in accord with earlier proposed 3D models forκ-casein that actually predicted participation of divalent cations in the structure.
    Type of Medium: Electronic Resource
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