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Morphology of frozen hydrated gluten...

Kontogiorgos, Vasileios.

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Morphology of frozen hydrated gluten networks as affected by ice structuring proteins.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Morphology of frozen hydrated gluten networks as affected by ice structuring proteins./
作者:	Kontogiorgos, Vasileios.
面頁冊數:	149 p.
附註:	Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7035.
Contained By:	Dissertation Abstracts International68-11B.
標題:	Agriculture, Food Science and Technology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR33608
ISBN:	9780494336083

Morphology of frozen hydrated gluten networks as affected by ice structuring proteins.
Kontogiorgos, Vasileios.

Morphology of frozen hydrated gluten networks as affected by ice structuring proteins. - 149 p.

Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7035.

Thesis (Ph.D.)--University of Guelph (Canada), 2007.

The present work constitutes an investigation of physicochemical properties of hydrated gluten and its industrial preparations in the presence or absence of ice structuring proteins (ISPs) at subzero temperatures.

ISBN: 9780494336083Subjects--Topical Terms:

1017813
Agriculture, Food Science and Technology.

Morphology of frozen hydrated gluten networks as affected by ice structuring proteins.
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245 1 0 $a Morphology of frozen hydrated gluten networks as affected by ice structuring proteins.
300 $a 149 p.
500 $a Source: Dissertation Abstracts International, Volume: 68-11, Section: B, page: 7035.
502 $a Thesis (Ph.D.)--University of Guelph (Canada), 2007.
520 $a The present work constitutes an investigation of physicochemical properties of hydrated gluten and its industrial preparations in the presence or absence of ice structuring proteins (ISPs) at subzero temperatures.
520 $a A highly active ISP preparation was isolated from cold acclimated winter wheat grass extract (AWWE). Enzymatic activity was detected and could be obliterated by heat treatment without any loss in recrystallization inhibition activity (RI). A single heat stable protein responsible for the RI activity was consequently isolated, which attains beta-sheet and random coil solution conformation. We identified it as belonging to the thaumatin-like protein group.
520 $a Calorimetric investigation of hydrated gluten at subzero temperature revealed two endothermic events. To interpret them, a novel microstructural model was proposed, which suggests that hydrated gluten forms nano-capillaries. By employing the Defay-Prigogine theory, one event was assigned to capillary-confined ice melting whereas the other to ice melting in the bulk. Furthermore, it was shown that it is impossible to assign a Tg value for hydrated frozen gluten, and therefore, the construction of state diagrams is not feasible at subzero temperatures for this material. It was also demonstrated that in the absence of a readily discemable T g temperature in gluten-ice composites, consideration of the melting point could provide a valid index of functional quality. ISPs were effective in controlling recrystallization both within the capillaries and in the bulk.
520 $a In order to bring the model system closer to potential food applications, flour-water mixtures were also investigated. Deterioration of the mechanical properties continued unabated for thirty days of aging with the ISPs being unable to offer protection against recrystallization at the concentration level studied. Furthermore, storage near the melting point of ice of the flour-water sample was found to accelerate the structural losses owing to increasing water mobility at this regime.
520 $a Fiber-like gluten network was not observed at all length scales studied. Gluten proteins form thin films that are arranged in sheets rather than in fibers. Ice crystal formation deteriorates the network by compressing its microstructural elements thus leading to rupture of adjacent sheets. Ice recrystallization leads to further deterioration with the ISPs being capable of controlling it to some extent.
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792 $a 2007
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