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|Title:||Application of small-angle scattering to study the effects of moisture content on a native soy protein.|
|Keywords:||Small angle scattering|
|Citation:||Kealley, C. S., Elcombe, M. M., Wuhrer, R., & Gilbert, E. P. (2008). Application of small-angle scattering to study the effects of moisture content on a native soy protein. Journal of Applied Crystallography, 41, 628-633. doi:10.1107/S0021889808012648|
|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 similar to-4 indicates that the interface between the 'dry' protein powder and the surrounding medium at a length-scale of at least 3 mm down to similar 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, Wiley-Blackwell.|
|Gov't Doc #:||1384|
|Appears in Collections:||Journal Articles|
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