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

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dc.contributor.authorHuson, MGen_AU
dc.contributor.authorStrounina, EVen_AU
dc.contributor.authorKealley, CSen_AU
dc.contributor.authorRout, MKen_AU
dc.contributor.authorChurch, JSen_AU
dc.contributor.authorAppelqvist, IAMen_AU
dc.contributor.authorGidley, MJen_AU
dc.contributor.authorGilbert, EPen_AU
dc.date.accessioned2012-01-12T04:25:53Zen_AU
dc.date.available2012-01-12T04:25:53Zen_AU
dc.date.issued2011-06-01en_AU
dc.date.statistics2012-01-12en_AU
dc.description.abstractThe 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 are maintained. 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. C-13 NMR results supported this hypothesis. © 2011, American Chemical Societyen_AU
dc.identifier.citationHuson, M. G., Strounina, E. V., Kealley, C. S., Rout, M. K., Church, J. S., Appelqvist, I. A. M., Gidley, M. J., & Gilbert, E. P. (2011). Effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin. Biomacromolecules, 12(6), 2092-2102. doi:10.1021/bm200080hen_AU
dc.identifier.govdoc3887en_AU
dc.identifier.issn1525-7797en_AU
dc.identifier.issue6en_AU
dc.identifier.journaltitleBiomacromoleculesen_AU
dc.identifier.pagination2092-2102en_AU
dc.identifier.urihttp://dx.doi.org/10.1021/bm200080hen_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/3990en_AU
dc.identifier.volume12en_AU
dc.language.isoenen_AU
dc.publisherAmerican Chemical Societyen_AU
dc.subjectProtein denaturationen_AU
dc.subjectCrystal structureen_AU
dc.subjectMobilityen_AU
dc.subjectNuclear magnetic resonanceen_AU
dc.subjectProteinsen_AU
dc.subjectGlycineen_AU
dc.titleEffects of thermal denaturation on the solid-state structure and molecular mobility of glycininen_AU
dc.typeJournal Articleen_AU
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