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

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...

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Main Authors: Kealley, Cat, Elcombe, M., Wuhrer, R., Gilbert, E.
Format: Journal Article
Published: 2008
Online Access:http://hdl.handle.net/20.500.11937/31911
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author Kealley, Cat
Elcombe, M.
Wuhrer, R.
Gilbert, E.
author_facet Kealley, Cat
Elcombe, M.
Wuhrer, R.
Gilbert, E.
author_sort Kealley, Cat
building Curtin Institutional Repository
collection Online Access
description 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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spelling curtin-20.500.11937-319112018-03-29T09:09:14Z Application of small-angle scattering to study the effects of moisture content on a native soy protein Kealley, Cat Elcombe, M. Wuhrer, R. Gilbert, E. 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. 2008 Journal Article http://hdl.handle.net/20.500.11937/31911 10.1107/S0021889808012648 restricted
spellingShingle Kealley, Cat
Elcombe, M.
Wuhrer, R.
Gilbert, E.
Application of small-angle scattering to study the effects of moisture content on a native soy protein
title Application of small-angle scattering to study the effects of moisture content on a native soy protein
title_full Application of small-angle scattering to study the effects of moisture content on a native soy protein
title_fullStr Application of small-angle scattering to study the effects of moisture content on a native soy protein
title_full_unstemmed Application of small-angle scattering to study the effects of moisture content on a native soy protein
title_short Application of small-angle scattering to study the effects of moisture content on a native soy protein
title_sort application of small-angle scattering to study the effects of moisture content on a native soy protein
url http://hdl.handle.net/20.500.11937/31911