Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality

Crit Rev Food Sci Nutr. 2002;42(3):179-208. doi: 10.1080/10408690290825510.


The unique breadmaking properties of wheat are generally ascribed to the visco-elastic properties of its gluten proteins. While monomeric gluten proteins (gliadin) show viscous behavior, polymeric gluten proteins (glutenin) are elastic. The unique elasticity of glutenin results to a large extent from its polymeric nature. Glutenin is a highly heterogeneous mixture of polymers consisting of a number of different high- and low-molecular-weight glutenin subunits linked by disulfide bonds. Although glutenin obviously is the major polymeric protein in wheat, other polymeric proteins occur as well. Their importance in breadmaking may be underestimated. Nevertheless, variations in both quantity and quality of glutenin strongly determine variations in breadmaking performance. Structural features of different classes of glutenin subunits are described. Variations in glutenin quality may result from variations in its (1) structure, (2) size distribution, and (3) subunit composition. Some hypotheses on glutenin structure and current insights into the role of glutenin size distribution are evaluated. Finally, different ways in which variation in glutenin composition may directly or indirectly (by affecting glutenin structure and/or size distribution) influence glutenin quality are discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bread*
  • Flour
  • Gliadin / chemistry
  • Glutens / analogs & derivatives*
  • Glutens / chemistry*
  • Glycosylation
  • Molecular Weight
  • Particle Size
  • Plant Proteins / chemistry*
  • Polymers / chemistry
  • Rheology
  • Structure-Activity Relationship
  • Triticum* / chemistry
  • Triticum* / genetics
  • Viscosity


  • Plant Proteins
  • Polymers
  • Glutens
  • Gliadin
  • glutenin