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{{Short description|Protein family}}
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'''Glutenin''' (a type of [[glutelin]]) is the major [[protein]] within [[wheat flour]], making up 47% of the total protein content. The glutenins are protein aggregates of high-[[molecular mass|molecular-mass]] (HMW) and low-molecular-mass (LMW) [[Protein subunit|subunits]] with [[molar mass]]es from about 200,000 to a few million, which are stabilized by intermolecular [[disulfide bond]]s, [[hydrophobic interaction]]s and other forces. Glutenin is responsible for the strength and elasticity of [[dough]].<ref>{{cite book |author1=H.-D. Belitz |author2=W. Grosch |author3=P. Schieberle |year=2004 |title=Food Chemistry |edition=3rd |publisher=[[Springer Science+Business Media|Springer]] |isbn=978-3-540-64704-1}}</ref>
{{More citations needed|date=June 2017}}
{{Pfam box
|Name=HMW Glutenin
|InterPro=IPR001419
|Pfam=PF03157
|Symbol=Glutenin
}}
⚫
'''Glutenin''' (a type of [[glutelin]]) is a major [[protein]] within [[wheat flour]], making up 47% of the total protein content. The glutenins are protein aggregates of high-[[molecular mass|molecular-mass]] (HMW) and low-molecular-mass (LMW) [[Protein subunit|subunits]] with [[molar mass]]es from about 200,000 to a few million, which are stabilized by intermolecular [[disulfide bond]]s, [[hydrophobic interaction]]s and other forces. Glutenin is responsible for the strength and elasticity of [[dough]].<ref>{{cite book | vauthors = Belitz HD, Grosch W, Schieberle P |year=2004 |title=Food Chemistry |edition=3rd |publisher=[[Springer Science+Business Media|Springer]] |isbn=978-3-540-64704-1}}</ref>


Wheat gluten proteins consist of two major fractions: the gliadins and the glutenins. [[Gliadin]]s are monomeric proteins, which can be separated into four groups: alpha-, beta-, gamma- and omega-gliadins. Glutenins occur as multimeric aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds. In wheat, omega- and gamma-gliadins are encoded by genes at the Gli-1 loci located on the short arms of group-1 chromosomes, while alpha- and beta-gliadin-encoding genes are located on the short arms of group-6 chromosomes. LMW glutenins are encoded by genes at the Glu-3 loci that are closely linked to the Gli-1 loci. HMW glutenins are encoded by genes at the Glu-1 loci found on the long arms of group-1 chromosomes. Each Glu-1 locus consists of two tightly linked genes encoding one x-type and one y-type HMW glutenin, with polymorphism giving rise to a number of different [[allele]]s at each locus. The y-type genes at the Glu-A1 locus are not expressed in hexaploid wheat. Due to the very close linkage between the x- and y-type genes, HMW glutenins are classified into alleles according to the x- and y-type subunits expressed.
Wheat [[gluten]] proteins consist of two major fractions: the gliadins and the glutenins. [[Gliadin]]s are [[monomer]]ic proteins, which can be separated into four groups: alpha-, beta-, gamma- and omega-gliadins. They are structurally similar to LMW glutenins. Glutenins occur as [[multimer]]ic aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds.{{citation needed|date=September 2017}} The way the glutenins form their disulfide bond network is predicted to be regulated by the hydrophobicity in the peptide sections where their cysteins are located, explaining why the gliadins are monomeric despite sharing similar conserved cysteine motifs as the LMW-glutenins.<ref>{{cite journal | vauthors = Markgren J, Hedenqvist M, Rasheed F, Skepö M, Johansson E | title = Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations | journal = Biomolecules | volume = 10 | issue = 8 | pages = 1095 | date = July 2020 | pmid = 32717949 | doi = 10.3390/biom10081095 | s2cid = 220841839 | doi-access = free }}</ref>


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Breadmaking qualities are largely dependent on the number and composition of HMW glutenin subunits. It has been demonstrated that alleles Glu-A1b (Ax2∗) and Glu-D1d (Dx5 + Dy10) are normally associated with superior end-use quality, especially dough strength.{{citation needed|date=September 2017}}
Considerable efforts have been made to understand the relationship of gliadin and glutenin composition to the [[rheology|rheological]] properties of wheat dough. It is now well understood that the properties of various wheat storage proteins have a major effect on dough rheological properties. The gliadin and glutenin components contribute to dough quality either in an independent manner (additive genetic effects) or in interactive manner ([[epistatic]] effects). It was suggested{{By whom|date=February 2015}} that the apparent effects of gliadins on dough quality should be attributed to the LMW glutenins due to the close linkage of the Gli-1 and Glu-3 loci. Generally, HMW glutenins have been found to be more important than gliadins and LMW glutenins for dough rheological properties.

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Breadmaking qualities are largely dependent on the number and composition of HMW glutenin subunits. It has been demonstrated that alleles Glu-A1b (Ax2∗) and Glu-D1d (Dx5 + Dy10) are normally associated with superior end-use quality, especially dough strength.


== References ==
== References ==
{{reflist}}
{{reflist}}

== External links ==
* [https://www.uniprot.org/uniprot/?query=family:%22gliadin%2Fglutenin+family%22&sort=score family:"gliadin glutenin family"] - UniProt query


[[Category:Gluten]]
[[Category:Gluten]]

Latest revision as of 22:00, 5 July 2024

HMW Glutenin
Identifiers
SymbolGlutenin
PfamPF03157
InterProIPR001419
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Glutenin (a type of glutelin) is a major protein within wheat flour, making up 47% of the total protein content. The glutenins are protein aggregates of high-molecular-mass (HMW) and low-molecular-mass (LMW) subunits with molar masses from about 200,000 to a few million, which are stabilized by intermolecular disulfide bonds, hydrophobic interactions and other forces. Glutenin is responsible for the strength and elasticity of dough.[1]

Wheat gluten proteins consist of two major fractions: the gliadins and the glutenins. Gliadins are monomeric proteins, which can be separated into four groups: alpha-, beta-, gamma- and omega-gliadins. They are structurally similar to LMW glutenins. Glutenins occur as multimeric aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds.[citation needed] The way the glutenins form their disulfide bond network is predicted to be regulated by the hydrophobicity in the peptide sections where their cysteins are located, explaining why the gliadins are monomeric despite sharing similar conserved cysteine motifs as the LMW-glutenins.[2]

Breadmaking qualities are largely dependent on the number and composition of HMW glutenin subunits. It has been demonstrated that alleles Glu-A1b (Ax2∗) and Glu-D1d (Dx5 + Dy10) are normally associated with superior end-use quality, especially dough strength.[citation needed]

References

[edit]
  1. ^ Belitz HD, Grosch W, Schieberle P (2004). Food Chemistry (3rd ed.). Springer. ISBN 978-3-540-64704-1.
  2. ^ Markgren J, Hedenqvist M, Rasheed F, Skepö M, Johansson E (July 2020). "Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations". Biomolecules. 10 (8): 1095. doi:10.3390/biom10081095. PMID 32717949. S2CID 220841839.
[edit]
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