Structure and molecular mobility of soy glycinin in the solid state

Kealley, Catherine S., Rout, Manoj K., Dezfouli, Mahshid Roohani, Strounina, Ekaterina, Whittaker, Andrew K., Appelqvist, Ingrid A. M., Lillford, Peter J., Gilbert, Elliot P. and Gidley, Michael J. (2008) Structure and molecular mobility of soy glycinin in the solid state. Biomacromolecules, 9 10: 2937-2946. doi:10.1021/bm800721d


Author Kealley, Catherine S.
Rout, Manoj K.
Dezfouli, Mahshid Roohani
Strounina, Ekaterina
Whittaker, Andrew K.
Appelqvist, Ingrid A. M.
Lillford, Peter J.
Gilbert, Elliot P.
Gidley, Michael J.
Title Structure and molecular mobility of soy glycinin in the solid state
Journal name Biomacromolecules   Check publisher's open access policy
ISSN 1525-7797
Publication date 2008-01-01
Year available 2008
Sub-type Article (original research)
DOI 10.1021/bm800721d
Open Access Status
Volume 9
Issue 10
Start page 2937
End page 2946
Total pages 10
Editor A-C. Albertsson
Place of publication USA
Publisher American Chemical Society
Language eng
Subject C1
030406 Proteins and Peptides
860199 Processed Food Products and Beverages (excl. Dairy Products) not elsewhere classified
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 transform 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.
Keyword Biochemistry & Molecular Biology
Chemistry, Organic
Polymer Science
Biochemistry & Molecular Biology
Chemistry
Polymer Science
BIOCHEMISTRY & MOLECULAR BIOLOGY
CHEMISTRY, ORGANIC
POLYMER SCIENCE
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Fri, 27 Mar 2009, 00:16:09 EST by Lesley-Jayne Jerrard on behalf of Centre For Magnetic Resonance