Application of small-angle scattering to study the effects of moisture content on a native soy protein
|dc.identifier.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.|
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.
|dc.title||Application of small-angle scattering to study the effects of moisture content on a native soy protein|
|dcterms.source.title||Journal of Applied Crystallography|
|curtin.department||Department of Medical Radiation Sciences|
|curtin.accessStatus||Fulltext not available|
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