Gluten wheat protein

Birzele B and Prange A (2003), Fusarium spp. and storage fungi in suboptimally stored wheat mycotoxins and influence on wheat gluten proteins. Mycotoxin Res., 19, 162-170. 

Blanch, E.W., Kasarda, D.D., Hecht, L., Nielsen, K., Barron, L.D. 2003. New insight into the solution structures of wheat gluten proteins from Raman optical activity. Biochemistry 42 5665-5673. 

Hernandez-Munoz, P., Kanavouras, A., Perry, K.W.N. and Gavara, R. 2003. Development and Characterization of Biodegradable Films Made from Wheat Gluten Protein Fractions../. Agric. Food Chem., 51, 7647-7654. 

Conclusions Wheat Gluten Proteins and Dough Viscoelasticity... 

G. Mamone, P. Ferranti, L. Chianese, L. Scaftui, F. Addeo, Qualitative and quantitative analysis of wheat gluten proteins by LC and ESI-MS, Rapid Conunun. Mass Spectrom., 14 (2000) 897. 

Quinoa flour does not have good baking properties like wheat gluten proteins. The wheat proteins are able to form a viscoelastic network when flour is mixed with water to form dough, and these viscoelastic properties allow the use of wheat to produce bread and other processed foods (Shewry et al., 2002). Quinoa bread has been made by including 10% of wheat flour (Chauhan et al., 1992a,b). However, the enzyme... 

Monolayer techniques have been used with much success to study the interaction of proteins with surfactants (11, 12, 13), ions and lipids (14), and other proteins (15). This paper investigates, through well-established procedures, the surface chemistry of monolayers of a major component of heterogeneous wheat gluten protein, gliadin, and explores these interactions with various surface-active agents. 

Figure 13.3 The classification and nomenclature of wheat gluten proteins separated by SDS-PAGE.

Figure 13.4 The major groups of wheat gluten proteins. The (o-gliadins and HMW subunits are defined as S-poor prolamins and HMW prolamins respectively. The a/P-gliadins, y-gliadins and LMW subunits are S-rich prolamins [12].

Shewry PR, Tatham AS, Forde J, Kreis M, Miflin BJ (1986). The classification and nomenclature of wheat gluten proteins a reassessment. J. Cereal ScL, 4 97-106. 

Cereals are an important protein source and are processed into bread, pasta and noodles, breakfast cereals, and fermented drink. For all these applications the quality is determined, to a greater or lesser extent, by the gluten proteins which account for about half of the total grain nitrogen. There are also opportunities to develop novel uses for cereal proteins in both the food and nonfood indns-tries. It is important to study the wheat gluten proteins, particularly the deamidated SWP (soluble wheat protein) in relation to their structure and function. 

Shewry, PR., Halford, N.G., Field, J.M., and Tatham, A.S. The structure and functionality of wheat gluten proteins. Proceedings of the 38th Australian Cereal Chemistry Conference, Sydney, NSW, Murray, L. ed.. Royal Australian Chemical Institute, Melbourne, VIC, Australia, 1989. 

Woychick, J.H., Boundy, J.A., and Dimler, R.J., Starch gel electrophoresis of wheat gluten proteins with concentrated urea. Arch. Biochem. Biophys. 94 477-482, 1961. 

By varying reaction condititnis, the optimum extent of esterification was obtained for each kind of proteins. Table 1 shows the highest esterification values obtained from an experimental design. Sunflower proteins underwent esterification in a larger extent than wheat gluten proteins. Only 25 % of the carboxyl groups of wheat gluten could be esterified with this experimental procedure. The different structure of proteins may account for this difference. 

Sunflower and wheat gluten proteins were successfully esterified by n-octanol. The grafting of hydrophobic groups to gluten and sunflower proteins decreased the solubility of die final inoduct obtained therefrom. 

Wheat gluten protein hydrolysates. See Hydrolyzed wheat gluten Wheat husk oil. See Wheat (Triticum vulgare) germ oil... 

Some cereal proteins are quite soluble in aqueous solution (albumins, globulins) but the functional proteins—prolamins and glutelins—are difficult to solubilize. This is important because, for example, we do not want wheat gluten proteins to be soluble in a dough system. However, in order to characterize proteins, it is usually necessary to have them in solution. Because the property of solubility is such an important one with respect to cereal proteins, we will dedicate this chapter to the topic. In keeping with the objectives of the book, we will attempt to approach the subject from the most general and fundamental basis. 

Preston, K. R. 1981. Effects of neutral salts upon wheat gluten protein properties. I. Relationships between the hydrophobic properties of gluten proteins and their extractability and turbidity in neutral salts. Cereal Chemistry 58 317-324. 

Shewry, P. R., A. S. Tatham, J. Forde, M. Kreis, and B. J. Miflin. 1986. The classification and nomenclature of wheat gluten proteins A reassessment. Journal of Cereal Science 4 97-106. 

The balance between viscosity and elasticity is close to optimum for wheat gluten protein at the water content used in dough-making. We have seen that the first requirement for a protein in dough to have viscoelastic properties is that its Tg be below the processing (usually ambient) temperature for the water content used. A second requirement for dough in an aerated product is that the molecular weight distribution (MWD) of the protein be optimal. 

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