Skip to main content
NCBI home page
Philosophical Transactions of the Royal Society B: Biological Sciences logoLink to Philosophical Transactions of the Royal Society B: Biological Sciences
. 2002 Feb 28;357(1418):133–142. doi: 10.1098/rstb.2001.1024

The structure and properties of gluten: an elastic protein from wheat grain.

Peter R Shewry 1, Nigel G Halford 1, Peter S Belton 1, Arthur S Tatham 1
PMCID: PMC1692935  PMID: 11911770

Abstract

The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain. These form a continuous proteinaceous matrix in the cells of the mature dry grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough. These viscoelastic properties underpin the utilization of wheat to give bread and other processed foods. One group of gluten proteins, the HMM subunits of glutenin, is particularly important in conferring high levels of elasticity (i.e. dough strength). These proteins are present in HMM polymers that are stabilized by disulphide bonds and are considered to form the 'elastic backbone' of gluten. However, the glutamine-rich repetitive sequences that comprise the central parts of the HMM subunits also form extensive arrays of interchain hydrogen bonds that may contribute to the elastic properties via a 'loop and train' mechanism. Genetic engineering can be used to manipulate the amount and composition of the HMM subunits, leading to either increased dough strength or to more drastic changes in gluten structure and properties.

Full Text

The Full Text of this article is available as a PDF (793.4 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BECKWEITH A. C., WALL J. S., DIMLER R. J. AMIDE GROUPS AS INTERACTION SITES IN WHEAT GLUTEN PROTEINS: EFFECTS OF AMIDE-ESTER CONVERSION. Arch Biochem Biophys. 1963 Dec;103:319–330. doi: 10.1016/0003-9861(63)90421-1. [DOI] [PubMed] [Google Scholar]
  2. Barro F., Rooke L., Békés F., Gras P., Tatham A. S., Fido R., Lazzeri P. A., Shewry P. R., Barceló P. Transformation of wheat with high molecular weight subunit genes results in improved functional properties. Nat Biotechnol. 1997 Nov;15(12):1295–1299. doi: 10.1038/nbt1197-1295. [DOI] [PubMed] [Google Scholar]
  3. Belton P. S., Colquhoun I. J., Grant A., Wellner N., Field J. M., Shewry P. R., Tatham A. S. FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin. Int J Biol Macromol. 1995 Apr;17(2):74–80. doi: 10.1016/0141-8130(95)93520-8. [DOI] [PubMed] [Google Scholar]
  4. Field J. M., Shewry P. R., Miflin B. J. Solubilisation and characterisation of wheat gluten proteins: correlations between the amount of aggregated proteins and baking quality. J Sci Food Agric. 1983 Apr;34(4):370–377. doi: 10.1002/jsfa.2740340409. [DOI] [PubMed] [Google Scholar]
  5. Field J. M., Tatham A. S., Shewry P. R. The structure of a high-Mr subunit of durum-wheat (Triticum durum) gluten. Biochem J. 1987 Oct 1;247(1):215–221. doi: 10.1042/bj2470215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gilbert S. M., Wellner N., Belton P. S., Greenfield J. A., Siligardi G., Shewry P. R., Tatham A. S. Expression and characterisation of a highly repetitive peptide derived from a wheat seed storage protein. Biochim Biophys Acta. 2000 Jun 15;1479(1-2):135–146. doi: 10.1016/s0167-4838(00)00059-5. [DOI] [PubMed] [Google Scholar]
  7. Keck B., Köhler P., Wieser H. Disulphide bonds in wheat gluten: cystine peptides derived from gluten proteins following peptic and thermolytic digestion. Z Lebensm Unters Forsch. 1995 Jun;200(6):432–439. doi: 10.1007/BF01193253. [DOI] [PubMed] [Google Scholar]
  8. Köhler P., Belitz H. D., Wieser H. Disulphide bonds in wheat gluten: further cystine peptides from high molecular weight (HMW) and low molecular weight (LMW) subunits of glutenin and from gamma-gliadins. Z Lebensm Unters Forsch. 1993 Mar;196(3):239–247. doi: 10.1007/BF01202740. [DOI] [PubMed] [Google Scholar]
  9. Köhler P., Belitz H. D., Wieser H. Disulphide bonds in wheat gluten: isolation of a cystine peptide from glutenin. Z Lebensm Unters Forsch. 1991 Mar;192(3):234–239. doi: 10.1007/BF01202885. [DOI] [PubMed] [Google Scholar]
  10. Miles M. J., Carr H. J., McMaster T. C., I'Anson K. J., Belton P. S., Morris V. J., Field J. M., Shewry P. R., Tatham A. S. Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):68–71. doi: 10.1073/pnas.88.1.68. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Napier J. A., Richard G., Turner M. F., Shewry P. R. Trafficking of wheat gluten proteins in transgenic tobacco plants: gamma-gliadin does not contain an endoplasmic reticulum-retention signal. Planta. 1997 Dec;203(4):488–494. doi: 10.1007/s004250050218. [DOI] [PubMed] [Google Scholar]
  12. Popineau Y., Deshayes G., Lefebvre J., Fido R., Tatham A. S., Shewry P. R. Prolamin aggregation, gluten viscoelasticity, and mixing properties of transgenic wheat lines expressing 1Ax and 1Dx high molecular weight glutenin subunit transgenes. J Agric Food Chem. 2001 Jan;49(1):395–401. doi: 10.1021/jf001015j. [DOI] [PubMed] [Google Scholar]
  13. Shwry P. R., Tatham A. S., Barro F., Barcelo P., Lazzeri P. Biotechnology of breadmaking: unraveling and manipulating the multi-protein gluten complex. Biotechnology (N Y) 1995 Nov;13(11):1185–1190. doi: 10.1038/nbt1195-1185. [DOI] [PubMed] [Google Scholar]
  14. Tao H. P., Adalsteins A. E., Kasarda D. D. Intermolecular disulfide bonds link specific high-molecular-weight glutenin subunits in wheat endosperm. Biochim Biophys Acta. 1992 Sep 4;1159(1):13–21. doi: 10.1016/0167-4838(92)90069-p. [DOI] [PubMed] [Google Scholar]
  15. Urry D. W. Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics. J Protein Chem. 1988 Feb;7(1):1–34. doi: 10.1007/BF01025411. [DOI] [PubMed] [Google Scholar]
  16. Van Dijk A. A., De Boef E., Bekkers A., Van Wijk L. L., Van Swieten E., Hamer R. J., Robillard G. T. Structure characterization of the central repetitive domain of high molecular weight gluten proteins. II. Characterization in solution and in the dry state. Protein Sci. 1997 Mar;6(3):649–656. doi: 10.1002/pro.5560060314. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Van Dijk A. A., Van Wijk L. L., Van Vliet A., Haris P., Van Swieten E., Tesser G. I., Robillard G. T. Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides. Protein Sci. 1997 Mar;6(3):637–648. doi: 10.1002/pro.5560060313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Wellner N., Belton P. S., Tatham A. S. Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of omega-gliadins. Biochem J. 1996 Nov 1;319(Pt 3):741–747. doi: 10.1042/bj3190741. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Philosophical Transactions of the Royal Society B: Biological Sciences are provided here courtesy of The Royal Society

RESOURCES