Glutenin (a type of glutelin) is a major

protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metab ...

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 mass In chemistry, the molar mass () (sometimes called molecular weight or formula weight, but see related quantities for usage) of a chemical substance ( element or compound) is defined as the ratio between the mass () and the amount of substance ...

es 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 Dough is a malleable, sometimes elastic paste made from flour (which itself is made from grains or from leguminous or chestnut crops). Dough is typically made by mixing flour with a small amount of water or other liquid and sometimes includes ...

. Wheat gluten proteins consist of two major fractions: the gliadins and the glutenins. Gliadins are

monomer A monomer ( ; ''mono-'', "one" + '' -mer'', "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or two- or three-dimensional network in a process called polymerization. Classification Chemis ...

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 multimeric aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds. 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. 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

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External links

family:"gliadin glutenin family"
- UniProt query Gluten Glycoproteins Seed storage proteins