Wheat Gluten Polymer Structures: The Impact of Genotype, Environment, and Processing on Their Functionality in Various Applications
(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:
https://lup.lub.lu.se/record/4178266
- author
- Johansson, Eva ; Malik, Ali H. ; Hussain, Abrar ; Rasheed, Faiza ; Newson, William R. ; Plivelic, Tomás LU ; Hedenqvist, Mikael S. ; Gällstedt, Mikael and Kuktaite, Ramune
- organization
- publishing date
- 2013
- 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
- 2016-04-01 13:05:50
- date last changed
- 2022-04-21 19:34:29
@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}},
doi = {{10.1094/CCHEM-08-12-0105-FI}},
volume = {{90}},
year = {{2013}},
}