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dc.contributor.authorKealley, Cat
dc.contributor.authorElcombe, M.
dc.contributor.authorWuhrer, R.
dc.contributor.authorGilbert, E.
dc.identifier.citationKealley, 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.titleApplication of small-angle scattering to study the effects of moisture content on a native soy protein
dc.typeJournal Article
dcterms.source.titleJournal of Applied Crystallography
curtin.departmentDepartment of Medical Radiation Sciences
curtin.accessStatusFulltext not available

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