Effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin

Huson, Mickey G., Strounina, Ekaterina V., Kealley, Catherine S., Rout, Manoj K., Church, Jeffrey S., Appelqvist, Ingrid A. M., Gidley, Michael J. and Gilbert, Elliot P. (2011) Effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin. Biomacromolecules, 12 6: 2092-2102. doi:10.1021/bm200080h


Author Huson, Mickey G.
Strounina, Ekaterina V.
Kealley, Catherine S.
Rout, Manoj K.
Church, Jeffrey S.
Appelqvist, Ingrid A. M.
Gidley, Michael J.
Gilbert, Elliot P.
Title Effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin
Journal name Biomacromolecules   Check publisher's open access policy
ISSN 1525-7797
1526-4602
Publication date 2011
Sub-type Article (original research)
DOI 10.1021/bm200080h
Volume 12
Issue 6
Start page 2092
End page 2102
Total pages 11
Place of publication Washington, DC, United States
Publisher American Chemical Society
Collection year 2012
Language eng
Formatted abstract The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility of soy glycinin powder were investigated using multiple techniques that probe over a range of length and time scales. In native glycinin, increased moisture resulted in a decrease in both the glass transition temperature and the denaturation temperature. The sensitivity of the glass transition temperature to moisture is shown to follow the Gordon-Taylor equation, while the sensitivity of the denaturation temperature to moisture is modeled using Flory's melting point depression theory. While denaturation resulted in a loss of long-range order, the principal conformational structures as detected by infrared aremaintained. The temperature range over which the glass to rubber transition occurred was extended on the high temperature side, leading to an increase in the midpoint glass transition temperature and suggesting that the amorphous regions of the newly disordered protein are less mobile. 13C NMR results supported this hypothesis.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
Centre for Advanced Imaging Publications
Centre for Nutrition and Food Sciences Publications
 
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Created: Wed, 14 Mar 2012, 17:17:59 EST by Professor Mike Gidley on behalf of Centre for Nutrition and Food Sciences