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Wheat Gluten Polymer Structures: The Impact of Genotype, Environment, and Processing on Their Functionality in Various Applications
Author(s) -
Johansson Eva,
Malik Ali Hafeez,
Hussain Abrar,
Rasheed Faiza,
Newson William R.,
Plivelic Tomas,
Hedenqvist Mikael S.,
Gällstedt Mikael,
Kuktaite Ramune
Publication year - 2013
Publication title -
cereal chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 100
eISSN - 1943-3638
pISSN - 0009-0352
DOI - 10.1094/cchem-08-12-0105-fi
Subject(s) - gluten , glutenin , chemistry , polymer , wheat gluten , protein quality , storage protein , plant protein , disulfide bond , protein aggregation , wheat flour , food science , biochemistry , chemical engineering , organic chemistry , gene , protein subunit , engineering
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 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, β‐eliminations with lanthionine formation, and isopeptide formation. In promising materials, the protein polymer structure is changed toward β‐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.