Biochemical and Functional Properties of Wheat Gliadins: A Review

REFERENCES

• Altenbach, S., Vensel, W.H. and Dupont, F.M. (2010). Analysis of expressed sequence tags from a single wheat cultivar facilitates interpretation of tandem mass spectrometry data and discrimination of gamma gliadin proteins that may play different functional roles in flour. BMC Plant Biol. 10:1–14.
   PubMed Web of Science ®Google Scholar
• Anderson, O.D., Hisa, C.C., Adalsteins, A.E., Lew, E.J. L. and Kasarda, D.D. (2001). Identification of several new classes of low-molecular-weight wheat gliadin-related proteins and genes. Theor. Appl. Genet. 103:307–315.
   Web of Science ®Google Scholar
• Anderson, O.D., Litts, J.C. and Greene, F.C. (1997). The α-gliadin gene family: 1. Characterization of ten new wheat α-gliadin genomic clones, evidence for limited sequence conservation of flanking DNA, and southern analysis of the gene family. Theor. Appl. Genet. 95:50–58.
   Web of Science ®Google Scholar
• Ang, S., Kogulanathan, J., Morris, G.A., Kok, M.S., Shewry, P.R., Tatham, A.S., Adams, G.G., Rowe, A.J. and Harding, S.E. (2010). Structure and heterogeneity of gliadin: A hydrodynamic evaluation. Eur. Biophys. J. Biophys. 39:255–261.
   PubMed Web of Science ®Google Scholar
• Anjum, F.M., Khan, M.R., Din, A., Saeed, M., Pasha, I. and Arshad, A.U. (2007). Wheat gluten: High molecular weight glutenin subunits-structure, genetics, and relation to dough elasticity. J. Food Sci. 72:56–63.
   PubMed Web of Science ®Google Scholar
• Autran, J.C. and Galterio, G. (1989). Associations between electrophoretic composition of protein, quality characteristics and agronomic attributes of durum wheat. II. Protein-quality associations. J. Cereal Sci. 9:195–215.
   Google Scholar
• Banc, A., Desbat, B., Renard, D., Popineau, Y., Mangavel, C. and Navailles, L. (2009). Exploring the interactions of gliadins with model membranes: Effect of confined geometry and interfaces. Biopolymers. 91:610–622.
   PubMed Web of Science ®Google Scholar
• Bean, S.R. and Lookhart, G.L. (2000). Ultrafast capillary electrophoretic analysis of cereal storage proteins and its applications to protein characterisation and cultivar differentiation. J. Agric. Food Chem. 48:344–353.
   PubMed Web of Science ®Google Scholar
• Bietz, J.A. (1983). Reversed-phase high-performance liquid chromatography of cereal endosperm proteins. J. Chromatogr. 255:219–238.
   PubMed Web of Science ®Google Scholar
• Bietz, J.A., Huebner, F.R., Sanderson, J.E. and Wall, J.S. (1977). Wheat gliadin homology revealed through N-terminal amino acid sequence analysis. Cereal Chem. 54:1070–1083.
   Web of Science ®Google Scholar
• Branlard, G. and Dardevet, M. (1985). Diversity of grain protein and bread wheat quality. I. Correlation between gliadin bands and flour quality characteristics. J. Cereal Sci. 3:329–343.
   Web of Science ®Google Scholar
• Brezhneva, T.A., Upelniek, V.P. and Pukhalsky, V.A. (2010). Genetic control of gliadin components in wheat Triticum spelta L. Russ. J. Genet. 46:562–565.
   Web of Science ®Google Scholar
• Brown, J.W. S. and Flavell, R.B. (1981). Fractionation of wheat gliadin and glutenin subunits by two-dimensional electrophoresis and the role of group 6 and group 2 chromosomes in gliadins synthesis. Theor. Appl. Genet. 59:349–359.
   PubMed Web of Science ®Google Scholar
• Bushuk, W. and Zillman, R.R. (1978). Wheat cultivars identification by gliadin electrophoregrams. I. Apparatus method and nomenclature. Can. J. Plant Sci. 58:505–515.
   Web of Science ®Google Scholar
• Camafeita, E., Solis, J., Alfonso, P., Lopez, J.A., Sorell, L. and Mendez, E. (1998). Selective identification by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry of different types of gluten in foods containing cereal mixtures. J. Chromatogr. 823:299–306.
   Web of Science ®Google Scholar
• Cassidy, B.G., Dvorak, J. and Anderson, O.D. (1998). The wheat low-molecular-weight glutenin genes: Characterization of six new genes and progress in understanding gene family structure. Theor. Appl. Genet. 96:743–750.
   Web of Science ®Google Scholar
• Charbonnier, L. (1974). Isolation and characterization of ω-gliadin fractions. Biochim. Biophys. Acta. 359:142–151.
   PubMed Web of Science ®Google Scholar
• Clarke, B.C., Phongkham, T., Gianibelli, M.C., Beasley, H. and Bekes, F. (2003). The characterization and mapping of a family of LMW-gliadin genes: Effects on dough properties and bread volume. Theor. Appl. Genet. 106:629–635.
   PubMed Web of Science ®Google Scholar
• Cornish, G.B., Bekes, F., Eagles, H.A. and Payne, P.I. (2006). Prediction of dough properties for bread wheats. In: Gliadin and Glutenin: The Unique Balance of Wheat Quality, pp. 243–280. Wrigley, C.W., Bekes, F. and Bushuk, W. Eds., American Association of Cereal Chemists, St Paul, MN.
   Google Scholar
• Cunsolo V., Foti, S., Saletti, R., Gilbert, S., Tatham, A.S. and Shewry, P.R. (2003). Structural studies of glutenin subunits 1Dy10 and 1Dy12 by matrix-assisted laser desorption/ionisation mass spectrometry and high-performance liquid chromatography/electrospray ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 17:442–454.
   PubMed Web of Science ®Google Scholar
• D′Ovidio, R. and Masci, S. (2004). The low-molecular-weight glutenin subunits of wheat gluten. J. Cereal Sci. 39:321–339.
   Web of Science ®Google Scholar
• Damidaux, R., Autran, J.C., Grignac, P. and Feillet, P. (1978). Evidence of relationships useful for breeding between the electrophoretic pattern of gliadins and the viscoelastic properties of the gluten in Triticum durum Desf. C.R. Hebd. Seances Acad. Sci. Ser. D. Sci. Nat. 287:701–704.
   Web of Science ®Google Scholar
• Darewicz, M., Dziuba, J. and Minkiewicz, P. (2008). Celiac disease- background, molecular, bioinformatics and analytical aspects. Food Rev. Int. 24:311–329.
   Web of Science ®Google Scholar
• Du Cros, D.L., Wrigley, C.W. and Hare, R.A. (1982). Prediction of durum-wheat quality from gliadin-protein composition. Austr. J. Agr. Res. 33:429–442.
   Google Scholar
• DuPont, F., Vensel, W.H., Chan, R. and Kasarda, D.D. (2000). Characterization of the 1B-type omega gliadins from Triticum aestivum cultivar Butte. Cereal Chem. 77:607–614.
   Web of Science ®Google Scholar
• Ewart, J.A. D. (1983). Slow triple β-gliadin from Cappelle-Desprez. J. Sci. Food Agric. 34:653–656.
   Web of Science ®Google Scholar
• Ferranti, P., Mamone, G., Picariello, G. and Addeo, F. (2007). Mass spectrometry analysis of gliadins in celiac disease. J. Mass Spectrom. 42:1531–1548.
   PubMed Web of Science ®Google Scholar
• Fido, R.J., Bekes, F., Gras, P.W. and Tatham, A.S. (1997). Effects of α-, β-, γ- and ω-gliadins on the dough mixing properties of wheat flour. J. Cereal Sci. 26:271–277.
   Web of Science ®Google Scholar
• Foulk, J.A. and Bunn, J.M. (2001). Physical and barrier properties of developed bilayer protein films. Appl. Eng. Agric. 17:635–641.
   Google Scholar
• Francin-Allami, M., Saumonneau, A., Lavenant, L., Bouder, A., Sparkes, I., Hawes, C. and Popineau, Y. (2011). Dynamic trafficking of wheat gamma-gliadin and of its structural domains in tobacco cells, studied with fluorescent protein fusions. J. Exp. Bot. 62:4507–4520.
   PubMed Web of Science ®Google Scholar
• Friedli, G.L. (1996). Interaction of Deamidated Soluble Wheat Protein (SWP) with other Food Proteins and Metals. PhD thesis, University of Surrey.
   Google Scholar
• Fuad, T. and Prabhasankar, P. (2010). Role of ingredients in pasta product quality: A review on recent developments. Crit. Rev. Food Sci. Nutr. 50:787–798.
   PubMed Web of Science ®Google Scholar
• Gianibelli, M.C., Larroque, O.R., MacRitchie, F. and Wrigley, C.W. (2001). Biochemical, genetic, and molecular characterization of wheat endosperm proteins. Online available at. AACC. http://www.aaccnet.org/cerealchemistry/freearticle/ gianibelli.pdf, 1–20.
   Google Scholar
• Gianibelli, M.C., Masci, S., Larroque, O.R., Lafiandra, D. and MacRitchie, F. (2002). Biochemical characterisation of a novel polymeric protein subunit from bread wheat (Triticum aestivum L.). J. Cereal Sci. 35:265–276.
   Web of Science ®Google Scholar
• Gomez, A., Ferrero, C., Calvelo, A., Anon, M.C. and Puppo, M.C. (2011). Effect of mixing time on structural and rheological properties of wheat flour dough for breadmaking. Int. J. Food Prop. 14:583–598.
   Web of Science ®Google Scholar
• Hamer, R. J. and van Vliet, T. (2000). Understanding the structure and properties of gluten: An overview. In: Wheat Gluten, pp. 125–131. Shewry, P. R. and Tatham, A. S., Eds, Royal Society of Chemistry, Cambridge.
   Google Scholar
• Hisa, C.C. and Anderson, O.D. (2001). Isolation and characterization of wheat ω-gliadin genes. Theor. Appl. Genet. 103:37–44.
   Web of Science ®Google Scholar
• Huebner, F.R. and Bietz, J.A. (1986). Assessment of the potential breadmaking quality of hard wheats by reversed-phase high performance liquid chromatography of gliadins. J. Cereal Sci. 4:379–388.
   Google Scholar
• Kasarda, D.D., Autran, J.C., Lew, E.J. L., Nimmo, C.C. and Shewry, P.R. (1983). N-terminal amino acid sequences of ω-gliadins and ω-secalins: Implications for the evolution of prolamin genes. Biochim. Biophys. Acta. 747:138–150.
   Web of Science ®Google Scholar
• Kasarda, D.D., Bernardin, J.E. and Nimmo, C.C. (1976). Wheat proteins. In: Advances in Cereal Science and Technology, pp. 158–236. Pomeranz, Y., Eds., St. Paul, MN.
   Google Scholar
• Khan, M.R., Anjum, F.M., Din, A., Hussain, S., Shabbir, M.A. and Nadeem, M. (2010). Immunochemical characteristics of wheat proteins. Food Agr. Immunol. 21:279–294.
   Web of Science ®Google Scholar
• Khatkar, B.S. (1996). Dynamic Rheological and Functional Properties of Wheat Gluten Proteins. Ph.D. Thesis. University of Reading. UK.
   Google Scholar
• Khatkar, B.S., Bell, A.E. and Schofield, J.D. (1995). The dynamic rheological properties of glutens and gluten subfractions from wheats of good and poor bread-making quality. J Cereal Sci. 22:29–44.
   Web of Science ®Google Scholar
• Khatkar, B.S., Fido, R.J., Tatham, A.S. and Schofield, J.D. (2002a). Functional properties of wheat gliadins: 1. Effects on mixing characteristics and bread making quality. J. Cereal Sci. 35:299–306.
   Web of Science ®Google Scholar
• Khatkar, B.S., Fido, R.J., Tatham, A.S. and Schofield, J.D. (2002b). Functional properties of wheat gliadins: 2. Effects on dynamic rheological properties of wheat gluten. J. Cereal Sci. 35:307–313.
   Web of Science ®Google Scholar
• Klindworth, D.L., Hareland, G.A., Elias, E.M. and Xu, S.S. (2005). Agronomic and quality characteristics of 1AS.1AL-1DL translocation lines of durum wheat carrying glutenin allele Glu-D1d. Crop Sci. 45:77–84.
   Google Scholar
• Kuragano, T., Kimura, H. and Wada, Y. (1991). Effects of gliadin and glutenin on physical properties of cookies. Journal of Home Economics of Japan. 42:45–52.
   Google Scholar
• Lan, W.X., Lan, X.J., Wei, Y.M., Pu, Z.E. and Zheng, Y.L. (2009). Quality evaluation of gliadins from Zhengmai 9023×99E18 in wheat. Journal of Plant Sciences. 4:1–9.
   Google Scholar
• Lefebvre, J. and Mahmoudi, N. (2007). The pattern of the linear viscoelastic behaviour of wheat flour dough as delineated from the effects of water content and high molecular weight glutenin subunits composition. J Cereal Sci. 45:49–58.
   Web of Science ®Google Scholar
• Lookhart, G.L. and Albers, L.D. (1988). Correlations between reversed-phase high-performance liquid chromatography and acid- and sodium dodecyl sulfate-polyacrylamide gel electrophoretic data on prolamins from wheat sister lines differing widely in baking quality. Cereal Chem. 65:222–227.
   Web of Science ®Google Scholar
• MacRitchie, F. (1984). Baking quality of wheat flours. Adv. Food Res. 29:201–277.
   Google Scholar
• MacRitchie, F. (1987). Evaluation of contributions from wheat protein fractions to dough mixing and breadmaking. J. Cereal Sci. 6:259–268.
   Web of Science ®Google Scholar
• Metakovsky, E.V., Branlard, G., Chernakov, V.M., Upelniek, V.P., Redaelli, R. and Pogna, N.E. (1997). Recombination mapping of some chromosome 1A-, 1B-, 1D-, and 6B-controlled gliadins and low-molecular-weight glutenin subunits in common wheat. Theor. Appl. Genet. 94:788–795.
   Web of Science ®Google Scholar
• Molberg, O., McAdam, S., Lundin, K.E., Kristiansen, C., Arentz-Hansen H., Kett, K. and Sollid, L.M. (2001). T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase. Eur. J. Immunol. 31:1317–1323.
   PubMed Web of Science ®Google Scholar
• Mondal, S., Hays, D.B., Alviola, N.J., Mason, R.E., Tilley, M., Waniska, R.D. and Bean, S.R. (2009). Functionality of gliadin proteins in wheat flour tortillas. J. Agric. Food Chem. 57:1600–1605.
   PubMed Web of Science ®Google Scholar
• Muccilli, V., Cunsolo, V., Saletti, R., Foti, S., Margiotta, B., Scossa, F., Masci, S. and Lafiandra, D. (2010). Characterisation of a specific class of typical low molecular weight glutenin subunits of durum wheat by a proteomic approach. J. Cereal Sci. 51:134–139.
   Web of Science ®Google Scholar
• Muller, S. and Wieser, H. (1997). The location of disulphide bonds in monomeric gamma-gliadins. J. Cereal Sci. 26:169–176.
   Google Scholar
• Muller, S.W. and Wieser, H. (1995). The location of disulphide bonds in α-type gliadins. J. Cereal Sci. 22:21–27.
   Web of Science ®Google Scholar
• Navnidhi. (2010). Molecular and Functional Characterisation of Wheat Varieties for Flat Bread (Chapatti) Quality. Ph.D. Thesis. GJ University of Science and Technology, India.
   Google Scholar
• Ohm, J., Hareland, G., Simsek, S., Seabourn, B., Maghirang, E. and Dowell, F. (2010). Molecular weight distribution of proteins in hard red spring wheat: Relationship to quality parameters and intrasample uniformity. Cereal Chem. 87:553–560.
   Web of Science ®Google Scholar
• Ojaghi, J. and Akhundova, E. (2010). Genetic diversity of gliadin pattern, morphological traits and baking quality in doubled haploid wheat. Afr. J. Biotechnol. 9:956–966.
   Web of Science ®Google Scholar
• Ornebro, J., Nylander, T., Eliasson, A.C., Shewry, P.R., Tatham, A.S. and Gilbert, S.M. (2001). Adsorption of the high molecular weight glutenin subunit 1Dx5 compared to the 58-kDa central repetitive domain and α-gliadins. J. Cereal Sci. 34:141–150.
   Web of Science ®Google Scholar
• Osborne, T.B. (1907). The protein of the wheat kernel. Publication No. 84, Carnegie Institute: Washington, DC.
   Google Scholar
• Paananen, A., Tappura, K., Tatham, A.S., Fido, R., Shewry, P.R., Miles, M. and McMaster, T.J. (2006). Nanomechanical force measurements of gliadin protein interactions. Biopolymers 63:658–667.
   Web of Science ®Google Scholar
• Park, S.H., Bean, S.R., Chung, O.K. and Seib, P.A. (2006). Levels of protein and protein composition in hard winter wheat flours and the relationship to breadmaking. Cereal Chem. 83:418–423.
   Web of Science ®Google Scholar
• Payne, P.I. (1987). Genetics of wheat storage proteins and the effect of allelic variation on bread-making quality. Annu. Rev. Plant Physiol. 38:141–153.
   Web of Science ®Google Scholar
• Payne, P.I. and Lawrence, G.J. (1983). Catalogue of alleles for the complex gene loci Glu-A1, Glu-B1 and Glu-D1 which code for higher molecular weight subunits of glutenin in hexaploid wheat. Cereal Res Comm. 11:29–35.
   Google Scholar
• Pedersen, L. and Jorgensen, J.R. (2007). Variation in rheological properties of gluten from three biscuit wheat cultivars in relation to nitrogen fertilization. J. Cereal Sci. 46:132–138.
   Web of Science ®Google Scholar
• Pena, R.J., Trethowan, R., Pfeiffer, W.H. and Van Ginkel, M. (2002). Quality (end-use) improvement in wheat: Compositional, genetic, and environmental factors. J. Crop Prod. 1–37.
   Google Scholar
• Piergiovanni, A.R. and Volpe, N. (2003). Capillary electrophoresis of gliadins as a tool in the discrimination and characterization of hulled wheats (Triticum dicoccon schrank and T-spelta L.). Cereal Chem. 80:269–273.
   Web of Science ®Google Scholar
• Popineau, Y. and Pineau, F. (1987). Investigation of surface hydrophobicities of purified gliadins by hydrophobic interaction chromatography, reversed-phase high performance chromatography and apolar ligand binding. J. Cereal Sci. 5:215–231.
   Google Scholar
• Prabhasankar, P. (2002). Electrophoretic and immunochemical characteristics of wheat protein fractions and their relationships to chapatti making quality. Food Chem. 78:81–84.
   Web of Science ®Google Scholar
• Qi, P.F., Wei, Y.M., Chen, Q., Ouellet, T., Ai, J., Chen, G.Y., Li, W. and Zheng, Y.L. (2011). Identification of novel α-gliadin genes. Genome. 54:244–252.
   PubMed Web of Science ®Google Scholar
• Ram, B.P. and Nigam, N.G. (1981). Puffing and textural characteristics of chapatti in relation to varietal differences in gluten composition. J. Food Sci. 47:231–233.
   Web of Science ®Google Scholar
• Rao, H.P. (1993). Chapatti and related products. In: Encyclopedia of Food Science, Food Technology and Nutrition, pp. 795–801. Macrae, R., Robinson, R.K. and Sadler, M.J. Eds., Academic Press, London.
   Google Scholar
• Rashed, M.A., Abou-Deif, M.H., Sallam, M.A. A., Rizkalla, A.A. and Ramadan, W.A. (2007). Identification and prediction of the flour quality of bread wheat by gliadin electrophoresis. J. Appl. Sci. Res. 3:1393–1399.
   Google Scholar
• Redaelli, R., Pogna, N.E. and Ng, P.K. W. (1997). Effect of prolamins encoded by chromosomes 1B and 1D on the rheological properties of dough in near isogenic lines of bread wheat. Cereal Chem. 74:102–107.
   Web of Science ®Google Scholar
• Rodrigues, M.M. F., Martins, M.M. and Costa, M.L. B. (2005). Thermal properties of gluten proteins of two soft wheat varieties. Food Chem. 93:459–465.
   Web of Science ®Google Scholar
• Rodriguez-Nogales, J.M., Garcia, M.C. and Marina, M.L. (2006). High performance liquid chromatography and capillary electrophoresis for the analysis of maize proteins. J. Separ. Sci. 29:197–210.
   PubMed Web of Science ®Google Scholar
• Sewa, R., Jain, N., Dawar, V., Singh, R.P. and Sheoran, J. (2005). Analysis of acid-PAGE gliadin pattern of Indian wheats (Triticum aestivum L.) representing different environments and periods. Crop Sci. 45:1256–1263.
   Web of Science ®Google Scholar
• Sharma, A., Rao, V.S., Bhagwat, S.G. and Bapat, M.M. (2004). Elongation curve for evaluating chapatti making quality of whole wheat flour and its relation with other quality parameters. J. Food Sci. Tech. 41:160–164.
   Web of Science ®Google Scholar
• Shewry, P.R. (2009). Wheat. J. Exp. Bot. 60:1537–1553.
   PubMed Web of Science ®Google Scholar
• Shewry, P.R. and Tatham, A.S. (1997). Disulphide bonds in wheat gluten proteins. J. Cereal Sci. 25:207–227.
   Web of Science ®Google Scholar
• Shewry, P.R. and Tatham, A.S. (2000). Wheat gluten. Paper presented at: 7th International Workshop Gluten (University of Bristol).
   Google Scholar
• Shewry, P.R., Tatham, A.S., Forde, J., Kreis, M. and Miffin, B.J. (1986). The classification and nomenclature of wheat gluten proteins: A reassessment. J. Cereal Sci. 4:97–106.
   Web of Science ®Google Scholar
• Singh, H. and MacRitchie, F. (2001). Application of polymer science to properties of gluten. J. Cereal Sci. 33:231–243.
   Web of Science ®Google Scholar
• Singh, M. and Khatkar, B.S. (2005). Structural and functional properties of wheat storage proteins: A review. J. Food Sci. Technol. 42:455–471.
   Web of Science ®Google Scholar
• Singh, S., Singh, N. and MacRitchie, F. (2011). Relationship of polymeric proteins with pasting, gel dynamic and dough empirical-rheology in different Indian wheat varieties. Food Hydrocolloid. 25:19–24.
   Web of Science ®Google Scholar
• Siriamornpun, S., Wootton, M., Cox, J.M., Bekes, F. and Wrigley, C.W. (2001). Capillary electrophoresis of wheat gliadin proteins and its potential for wheat varietal identification using patter matching software. Aust. J. Agric. Res. 52:839–843.
   Google Scholar
• Sollid, L.M. (2000). Molecular basis of celiac disease. Ann. Rev. Immunol. 18:53–81.
   PubMed Web of Science ®Google Scholar
• Song, Y. and Zheng, Q. (2008). Influence of gliadin removal on strain hardening of hydrated wheat gluten during equibiaxial extensional deformation. J. Cereal Sci. 48:58–67.
   Web of Science ®Google Scholar
• Sorensen, H.A., Sperotto, M.M., Petersen, M., Kesmir, C., Radzikowski, L., Jacobsen, S. and Sondergaard, I. (2002). Variety identification of wheat using mass spectrometry with neural networks and the influence of mass spectra processing prior to neural network analysis. Rapid Commun. Mass Spectrom. 16:1232–1237.
   PubMed Web of Science ®Google Scholar
• Sozinov, A.A. and Poperelya, F.A. (1982). Polymorphism of prolamines and variability of grain quality. Plant Foods Hum. Nutr. 31:243–249.
   Web of Science ®Google Scholar
• Sreevamulu, G., Banerjee, R., Bhardwaj, A. and Vaishnav, P.P. (2003). Understanding the functionality of wheat high molecular weight glutenin subunits (HMW-GS) in chapatti making quality. In: The gluten proteins, pp. 162–165. Lafiandra, D., Masci, S. and D'ovidio, R., Eds, Royal Society of Chemistry, Cambridge.
   Google Scholar
• Srivastava, A., Rao, U.J. S. P. and Rao, P.H. (2003). Studies on protein and its high-molecular-weight subunit composition in relation to chapati-making quality of Indian wheat cultivars. J. Sci. Food. Agric. 83:225–231.
   Web of Science ®Google Scholar
• Tatham, A.S., Masson, P. and Popineau, Y. (1990). Conformational studies of peptides derived by enzymatic hydrolysis of a γ-type gliadin. J. Cereal Sci. 11:1–13.
   Google Scholar
• Tatham, A.S., Miflin, B.J. and Shewry, P.R. (1985). The β-turn conformation in wheat gluten proteins: Relationship to gluten elasticity. Cereal Chem. 62:405–412.
   Web of Science ®Google Scholar
• Tatham, A.S. and Shewry, P.R. (1985). The conformation of wheat gluten proteins: The secondary structures and thermal stabilities of α-, β-, γ- and ω-Gliadins. J. Cereal Sci. 3:103–113.
   Web of Science ®Google Scholar
• Tatham, A.S. and Shewry, P.R. (1995). The S-poor prolamins of wheat, barley and rye. J. Cereal Sci. 22:1–16.
   Web of Science ®Google Scholar
• Uthayakumaran, S., Gras, P.W., Stoddard, F.L. and Bekes, F. (1999). Effect of varying protein content and glutenin-to-gliadin ratio on the functional properties of wheat dough. Cereal Chem. 76:389–394.
   Web of Science ®Google Scholar
• Uthayakumaran, S. and Lukow, O.M. (2005). Improving wheat for bread and tortilla production by manipulating glutenin-to-gliadin ratio. J. Sci. Food. Agric. 85:2111–2118.
   Web of Science ®Google Scholar
• Uthayakumaran, S., Tomoskozi, S., Tatham, A.S., Savage, A.W. J., Gianibell, M.C., Stoddard, F.L. and Bekes, F. (2001). Effects of gliadin fractions on functional properties of wheat dough depending on molecular size and hydrophobicity. Cereal Chem. 78:138–141.
   Web of Science ®Google Scholar
• Van Lonkhuijsen, H.J., Hamer, R.J. and Schreuder, C. (1992). Influence of specific gliadins on the breadmaking quality of wheat. Cereal Chem. 69:174–177.
   Web of Science ®Google Scholar
• Veraverbeke, W.S. and Delcour, J.A. (2002). Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality. Crit. Rev. Food Sci. Nutr. 42:179–208.
   PubMed Web of Science ®Google Scholar
• Weegels, P.L., Hamer, R.J. and Schofield, J.D. (1996). Functional properties of wheat glutenins. J. Cereal Sci. 23:1–17.
   Web of Science ®Google Scholar
• Weegels, P.L., Marseille, J.P., Bosveld, P. and Hamer, R.J. (1994). Large-scale separation of gliadins and their breadmaking quality. J. Cereal Sci. 20:253–264.
   Web of Science ®Google Scholar
• Wellner, N., Bianchini, D., Mills, E.N. C. and Belton, P.S. (2003). Effect of selected hofmeister anions on the secondary structure and dynamics of wheat prolamins in gluten. Cereal Chem. 80:596–600.
   Web of Science ®Google Scholar
• Wellner, N., Mills, E.N. C., Brownsey, G., Wilson, R.H., Brown, N., Freeman, J., Halford, N.G., Shewry, P.R. and Belton, P.S. (2005). Changes in protein secondary structure during gluten deformation studied by dynamic Fourier transform infrared spectroscopy. Biomacromolecules. 6:255–61.
   PubMed Web of Science ®Google Scholar
• Wesley, A.S., Lukow, O.M., Ames, N., Kovacs, M.I. P., McKenzie, R.I. H. and Brown, D. (1999). Effect of single substitution of glutenin or gliadin proteins on flour quality of Alpha 16, a Canada Prairie Spring wheat breeders line. Cereal Chem. 76:743–747.
   Web of Science ®Google Scholar
• Wieser, H. (2007). Chemistry of gluten proteins. Food Microbiol. 24:115–119.
   PubMed Web of Science ®Google Scholar
• Wieser, H. and Kieffer, R. (2001). Correlations of the amount of gluten protein types to the technological properties of wheat flours determined on a micro-scale. J. Cereal Sci. 34:19–27.
   Web of Science ®Google Scholar
• Wrigley, C., Bekes, F. and Bushuk, W. (2006). Gliadin and Glutenin: The Unique Balance of Wheat Quality. AACC International. MN.
   Google Scholar
• Wrigley, C.W., Robinson, P.J. and Williams, W.T. (1981). Association between electrophoretic patterns of gliadin proteins and quality characteristics of wheat cultivars. J. Sci. Food Agric. 23:433–442.
   Web of Science ®Google Scholar
• Wrigley, C.W., Robinson, P.J. and Williams, W.T. (1982). Association between individual gliadin proteins and quality, agronomic and morphological attributes of wheat cultivars. Aust. J. Agr. Res. 33:409–418.
   Google Scholar
• Wrigley, C.W. and Shepherd, K.W. (1973). Electrofocusing of grain proteins from wheat genotypes. Ann. New York Acad. Sci. 209:154–162.
   PubMed Web of Science ®Google Scholar
• Wu, F., Han, Z.X., Liu, Y., Pan, Z.F., Deng, G.B. and Yu, M.Q. (2007). Unique gliadin patterns in Chinese winter wheat cultivars. Plant Breeding. 126:498–502.
   Web of Science ®Google Scholar
• Zilic S., Barac, M., Pesic, M., Dodig, D. and Ignjatovic-Micic, D. (2011). Characterization of proteins from grain of different bread and durum wheat genotypes. Int. J. Mol. Sci. 12:5878–5894.
   PubMed Web of Science ®Google Scholar