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    Application of small-angle scattering to study the effects of moisture content on a native soy protein

    Access Status
    Fulltext not available
    Authors
    Kealley, Cat
    Elcombe, M.
    Wuhrer, R.
    Gilbert, E.
    Date
    2008
    Type
    Journal Article
    
    Metadata
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    Citation
    Kealley, C. and Elcombe, M. and Wuhrer, R. and Gilbert, E. 2008. Application of small-angle scattering to study the effects of moisture content on a native soy protein. Journal of Applied Crystallography. 41 (3): pp. 628-633.
    Source Title
    Journal of Applied Crystallography
    DOI
    10.1107/S0021889808012648
    ISSN
    0021-8898
    School
    Department of Medical Radiation Sciences
    URI
    http://hdl.handle.net/20.500.11937/31911
    Collection
    • Curtin Research Publications
    Abstract

    The nano- and microstructure of glycinin, a soybean protein, has been investigated as a function of moisture for moisture contents between 4 and 21 wt%. Glycinin exhibits peaks in the small-angle region whose positions show minimal change with X-rays for samples up to 13% moisture. However, the use of neutron scattering, and the associated enhancement in contrast, results in the Bragg peaks being well resolved up to higher moisture contents; the associated shift in peak positions between 4 and 21% moisture are consistent with the expansion of a hexagonal unit cell as a function of moisture content. A Porod slope of ~-4 indicates that the interface between the 'dry' protein powder and the surrounding medium at a length-scale of at least 3 µm down to ~20 nm is smooth and sharp. Scanning electron microscopy indicates that the powders, with low moisture content, have a porous appearance, with the porosity decreasing and microstructure expanding as the moisture content increases. © 2008 International Union of Crystallography.

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