Gliadin proteins

Sensitivity to the protein gliadin, present in gluten, results in coeliac disease. 

FIGURE 2.12 Response surface model predictions of the effects of HA protein (gliadin) and HA polyphenol (TA) on the haze intensity in a model system at fixed levels of pH and alcohol. Reprinted with permission from Siebert et at. (1996a). Copyright 1996 American Chemical Society. 

FIGURE 2.14 Particle sizes measured with 100 ( ), 200 ( ), 300 (A), 400 ( ), and 500 ( ) mg/L protein (gliadin) concentrations added to 40 mg/L TA. Reprinted with permission from Siebert and Lynn (2000). Copyright 2000 American Society of Brewing Chemists. 

Gliadin. Gliadin is that portion of the gluten proteins that is soluble in 70% aqueous ethanol. It comprises approximately 35 to 40% of the flour proteins. Gliadin imparts the viscous component to the viscoelastic properties of gluten. 

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. 

In the forementioned laboratories, we started with a new strategy based on phase separation in order to prepare natural particles. Simple or complex coacervation methods involving proteins or protein and polysaccharide mixtures3 were used to create new matrices dedicated to controlled release applications. The colloidal carriers produced were in the micrometre or nanometre size range depending on the substrates or the methods used. Wheat proteins, gliadins, were implicated in simple coacervation to produce nanospheres. Controlled release experiments with model compounds were conducted in order to evaluate... 

PC loadings and their absolute values in the data reduction techniques has been proposed. This procedure has been successfully used for the smdy of the effect of carboxymethyl-P-cyclodextrin on the hydrophobicity parameters of steroidal drugs measured by TLC, and for the assessment of the binding characteristics of environmental pollutants to the wheat protein, gliadin, investigated by HPLC. 

The situation has recently been clarified considerably by the finding that the removal of wheat and rye flour from the diet of children with coeliac disease has resulted in rapid improvement, both clinically and biochem-ically, and that deterioration followed the reintroduction into the diet of wheat flour or wheat gluten, but wheat starch had no effect. As reported by Weyers, van de Kamer, and Dicke at the First International Congress on Dietetics at Amsterdam, the decisive factor is the protein gliadin. 

Table 1.37. Emulsifying property of various proteins Gliadin (1.4°/o Ala)...

The most obvious features when scanning a solution of proteins are the denaturation peaks. For instance, if bovine serum albumin (BSA) with and without fatty acids in aqueous solution is heated, and not subjected to too high a temperature, nearly reversible endothermic peaks are obtained [77]. This is the case for many globular proteins of animal and plant origin, such as lactoglobulin and the wheat proteins gliadin and glutenin [78,79]. 

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