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HMW 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 (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]

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]


  1. ^ H.-D. Belitz; W. Grosch; P. Schieberle (2004). Food Chemistry (3rd ed.). Springer. ISBN 978-3-540-64704-1.

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