Wheat Gluten Polymer Structures: The Impact of Genotype, Environment, and Processing on Their Functionality in Various Applications
Author
Summary, in English
For a number of applications, gluten protein polymer structures are
of the highest importance in determining end-use properties. The
present article focuses on gluten protein structures in the wheat grain,
genotype- and environment-related changes, protein structures in
various applications, and their impact on quality. Protein structures in
mature wheat grain or flour are strongly related to end-use properties,
although influenced by genetic and environment interactions. Nitrogen
availability during wheat development and genetically determined
plant development rhythm are the most important parameters determining
the gluten protein polymer structure, although temperature
during plant development interacts with the impact of the mentioned
parameters. Glutenin subunits are the main proteins incorporated in
the gluten protein polymer in extracted wheat flour. During dough
mixing, gliadins are also incorporated through disulfide-sulfhydryl
exchange reactions. Gluten protein polymer size and complexity in
the mature grain and changes during dough formation are important
for breadmaking quality. When using the gluten proteins to produce
plastics, additional proteins are incorporated in the polymer through
disulfide-sulfhydryl exchange, sulfhydryl oxidation, â-eliminations
with lanthionine formation, and isopeptide formation. In promising
materials, the protein polymer structure is changed toward â-sheet
structures of both intermolecular and extended type and a hexagonal
close-packed structure is found. Increased understanding of gluten
protein polymer structures is extremely important to improve
functionality and end-use quality of wheat- and gluten-based products.
of the highest importance in determining end-use properties. The
present article focuses on gluten protein structures in the wheat grain,
genotype- and environment-related changes, protein structures in
various applications, and their impact on quality. Protein structures in
mature wheat grain or flour are strongly related to end-use properties,
although influenced by genetic and environment interactions. Nitrogen
availability during wheat development and genetically determined
plant development rhythm are the most important parameters determining
the gluten protein polymer structure, although temperature
during plant development interacts with the impact of the mentioned
parameters. Glutenin subunits are the main proteins incorporated in
the gluten protein polymer in extracted wheat flour. During dough
mixing, gliadins are also incorporated through disulfide-sulfhydryl
exchange reactions. Gluten protein polymer size and complexity in
the mature grain and changes during dough formation are important
for breadmaking quality. When using the gluten proteins to produce
plastics, additional proteins are incorporated in the polymer through
disulfide-sulfhydryl exchange, sulfhydryl oxidation, â-eliminations
with lanthionine formation, and isopeptide formation. In promising
materials, the protein polymer structure is changed toward â-sheet
structures of both intermolecular and extended type and a hexagonal
close-packed structure is found. Increased understanding of gluten
protein polymer structures is extremely important to improve
functionality and end-use quality of wheat- and gluten-based products.
Department/s
Publishing year
2013
Language
English
Pages
367-376
Publication/Series
Cereal Chemistry
Volume
90
Issue
4
Document type
Journal article
Publisher
American Association of Cereal Chemists
Topic
- Natural Sciences
- Physical Sciences
Status
Published
ISBN/ISSN/Other
- ISSN: 0009-0352