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    Structure and molecular mobility of soy glycinin in the solid state

    Access Status
    Fulltext not available
    Authors
    Kealley, Cat
    Rout, M.
    Dezfouli, M.
    Strounina, E.
    Whittaker, A.
    Appelqvist, I.
    Lillford, P.
    Gilbert, E.
    Gidley, M.
    Date
    2008
    Type
    Journal Article
    
    Metadata
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    Citation
    Kealley, C. and Rout, M. and Dezfouli, M. and Strounina, E. and Whittaker, A. and Appelqvist, I. and Lillford, P. et al. 2008. Structure and molecular mobility of soy glycinin in the solid state. Biomacromolecules. 9 (10): pp. 2937-2946.
    Source Title
    Biomacromolecules
    DOI
    10.1021/bm800721d
    ISSN
    1525-7797
    School
    Department of Medical Radiation Sciences
    URI
    http://hdl.handle.net/20.500.11937/7983
    Collection
    • Curtin Research Publications
    Abstract

    We report a multitechnique study of structural organization and molecular mobility for soy glycinin at a low moisture content (<30% w/ w) and relate these to its glass-to-rubber transition. Small-angle X-ray scattering (SAXS), differential scanning calorimetry (DSC), Fourier transfortn infrared (FTIR) spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy are used to probe structure and mobility on different length and time scales. NMR (~10-6 to 10-3 s) reveals transitions at a higher moisture content (> 17%) than DSC or SAXS, which sample for much longer times (~10 to 103 s) and where changes are detected at > 13% water content at 20 °C. The mobility transitions are accompanied by small changes in unit-cell parameters and IR band intensities and are associated with the enhanced motion of the polypeptide backbone. This study shows how characteristic features of the ordered regions of the protein (probed by SAXS and FTIR) and mobile segments (probed by NMR and DSC) can be separately monitored and integrated within a mobility transformation framework. © 2008 American Chemical Society.

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