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Wheat Gluten Polymer Structures: The Impact of Genotype, Environment, and Processing on Their Functionality in Various Applications

Johansson, Eva; Malik, Ali H.; Hussain, Abrar; Rasheed, Faiza; Newson, William R.; Plivelic, Tomás LU ; Hedenqvist, Mikael S.; Gällstedt, Mikael and Kuktaite, Ramune (2013) In Cereal Chemistry 90(4). p.367-376
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cereal Chemistry
volume
90
issue
4
pages
367 - 376
publisher
American Association of Cereal Chemists
external identifiers
  • wos:000326404700010
  • scopus:84881419665
ISSN
0009-0352
DOI
10.1094/CCHEM-08-12-0105-FI
language
English
LU publication?
yes
id
a0d4f070-c4e8-46bf-9f6c-351f3edde054 (old id 4178266)
date added to LUP
2013-11-29 11:03:26
date last changed
2019-02-20 05:09:12
@article{a0d4f070-c4e8-46bf-9f6c-351f3edde054,
  abstract     = {For a number of applications, gluten protein polymer structures are<br/><br>
of the highest importance in determining end-use properties. The<br/><br>
present article focuses on gluten protein structures in the wheat grain,<br/><br>
genotype- and environment-related changes, protein structures in<br/><br>
various applications, and their impact on quality. Protein structures in<br/><br>
mature wheat grain or flour are strongly related to end-use properties,<br/><br>
although influenced by genetic and environment interactions. Nitrogen<br/><br>
availability during wheat development and genetically determined<br/><br>
plant development rhythm are the most important parameters determining<br/><br>
the gluten protein polymer structure, although temperature<br/><br>
during plant development interacts with the impact of the mentioned<br/><br>
parameters. Glutenin subunits are the main proteins incorporated in<br/><br>
the gluten protein polymer in extracted wheat flour. During dough<br/><br>
mixing, gliadins are also incorporated through disulfide-sulfhydryl<br/><br>
exchange reactions. Gluten protein polymer size and complexity in<br/><br>
the mature grain and changes during dough formation are important<br/><br>
for breadmaking quality. When using the gluten proteins to produce<br/><br>
plastics, additional proteins are incorporated in the polymer through<br/><br>
disulfide-sulfhydryl exchange, sulfhydryl oxidation, â-eliminations<br/><br>
with lanthionine formation, and isopeptide formation. In promising<br/><br>
materials, the protein polymer structure is changed toward â-sheet<br/><br>
structures of both intermolecular and extended type and a hexagonal<br/><br>
close-packed structure is found. Increased understanding of gluten<br/><br>
protein polymer structures is extremely important to improve<br/><br>
functionality and end-use quality of wheat- and gluten-based products.},
  author       = {Johansson, Eva and Malik, Ali H. and Hussain, Abrar and Rasheed, Faiza and Newson, William R. and Plivelic, Tomás and Hedenqvist, Mikael S. and Gällstedt, Mikael and Kuktaite, Ramune},
  issn         = {0009-0352},
  language     = {eng},
  number       = {4},
  pages        = {367--376},
  publisher    = {American Association of Cereal Chemists},
  series       = {Cereal Chemistry},
  title        = {Wheat Gluten Polymer Structures: The Impact of Genotype, Environment, and Processing on Their Functionality in Various Applications},
  url          = {http://dx.doi.org/10.1094/CCHEM-08-12-0105-FI},
  volume       = {90},
  year         = {2013},
}