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Ultrastructure of consecutively extracted and flocculated gliadins and glutenins
Year:
1998
Source of publication :
Journal of Cereal Science
Authors :
Shomer, Ilan
;
.
Vasiliver, Rosa
;
.
Volume :
27
Co-Authors:
Shomer, I., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Lookhart, G.L., USDA-ARS, U.S. Grain Mktg. Research Laboratory, Manhattan, KS 66502, United States
Vasiliver, R., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Bean, S., Dept. of Grain Science and Industry, Kansas State University, Manhattan, KS 66506, United States
Facilitators :
From page:
27
To page:
36
(
Total pages:
10
)
Abstract:
Gliadin and glutenin are characterized by specific ultrastructures, which depend on variety and separation conditions. Gliadins, extracted with 80% ethanol, of Israeli spring wheat 'Ariel' appeared as spherical bodies within an amorphous perforated matrix. The gliadins of a commercial sample of U.S. hard red winter wheat were deposited in bundles of bodies of concentric membrane-like units during water dialysis and they tended to separate while heating at 120°C. Acetic-acid-extracted glutenins heated at 120°C appeared as amorphous compact agglomerated particles beside dispersed aggregates, fibril-like patterns and oil-like bodies. The extracted glutenins, which were dialysed vs water, appeared as dispersed or aggregated particles beside oil-like bodies embedded in and/or encapsulated by coagulated protein. Differences were found in high-performance capillary electrophoresis patterns of both gliadins and glutenins between the Israeli spring wheat 'Ariel' and the good baking quality U.S. hard red winter wheat 'Karl 92'; indicating that the structural differences are a result of different proteins and differences in the physicochemical properties of the proteins. © 1998 Academic Press Limited.
Note:
Related Files :
Capillary electrophoresis
Gliadin
gluten
Microstructure
transmission electron microscopy
ultrastructure
Show More
Related Content
More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28303
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:38
Scientific Publication
Ultrastructure of consecutively extracted and flocculated gliadins and glutenins
27
Shomer, I., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Lookhart, G.L., USDA-ARS, U.S. Grain Mktg. Research Laboratory, Manhattan, KS 66502, United States
Vasiliver, R., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Bean, S., Dept. of Grain Science and Industry, Kansas State University, Manhattan, KS 66506, United States
Ultrastructure of consecutively extracted and flocculated gliadins and glutenins
Gliadin and glutenin are characterized by specific ultrastructures, which depend on variety and separation conditions. Gliadins, extracted with 80% ethanol, of Israeli spring wheat 'Ariel' appeared as spherical bodies within an amorphous perforated matrix. The gliadins of a commercial sample of U.S. hard red winter wheat were deposited in bundles of bodies of concentric membrane-like units during water dialysis and they tended to separate while heating at 120°C. Acetic-acid-extracted glutenins heated at 120°C appeared as amorphous compact agglomerated particles beside dispersed aggregates, fibril-like patterns and oil-like bodies. The extracted glutenins, which were dialysed vs water, appeared as dispersed or aggregated particles beside oil-like bodies embedded in and/or encapsulated by coagulated protein. Differences were found in high-performance capillary electrophoresis patterns of both gliadins and glutenins between the Israeli spring wheat 'Ariel' and the good baking quality U.S. hard red winter wheat 'Karl 92'; indicating that the structural differences are a result of different proteins and differences in the physicochemical properties of the proteins. © 1998 Academic Press Limited.
Scientific Publication
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