Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin
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 t...
| Main Authors: | , , , , , , , |
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| Format: | Journal Article |
| Published: |
American Chemical Society
2011
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| Online Access: | http://hdl.handle.net/20.500.11937/18990 |
| _version_ | 1848749905717231616 |
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| author | Huson, M. Strounina, E. Kealley, Cat Rout, M. Church, J. Appelqvist, I. Gidley, M. Gilbert, E. |
| author_facet | Huson, M. Strounina, E. Kealley, Cat Rout, M. Church, J. Appelqvist, I. Gidley, M. Gilbert, E. |
| author_sort | Huson, M. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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 GordonTaylor 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 occurredwas 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. |
| first_indexed | 2025-11-14T07:28:22Z |
| format | Journal Article |
| id | curtin-20.500.11937-18990 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:28:22Z |
| publishDate | 2011 |
| publisher | American Chemical Society |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-189902017-02-28T01:35:23Z Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin Huson, M. Strounina, E. Kealley, Cat Rout, M. Church, J. Appelqvist, I. Gidley, M. Gilbert, E. 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 GordonTaylor 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 occurredwas 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. 2011 Journal Article http://hdl.handle.net/20.500.11937/18990 American Chemical Society restricted |
| spellingShingle | Huson, M. Strounina, E. Kealley, Cat Rout, M. Church, J. Appelqvist, I. Gidley, M. Gilbert, E. Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin |
| title | Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin |
| title_full | Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin |
| title_fullStr | Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin |
| title_full_unstemmed | Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin |
| title_short | Effects of Thermal Denaturation on the Solid-State Structure and Molecular Mobility of Glycinin |
| title_sort | effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin |
| url | http://hdl.handle.net/20.500.11937/18990 |