CRITICAL REVIEW - Interfacial Behaviour of Wheat Proteins

Structure and Orientation Changes of ω- and γ-Gliadins at the Air−Water Interface: A PM−IRRAS Spectroscopy and Brewster Angle Microscopy Study

“…Interfacial properties of WSP are essential to understand their biological self-assembly as well as the baking performance of gluten and wheat flour doughs. 18 Prolamins are synthesized, folded, and further accumulated in the aqueous environment of the endoplasmic reticulum of the endosperm cells where membrane surfaces are highly developed. In the wheat dough, prolamins are principally located in the bulk of the gluten network but also at the interface of the air bubbles incorporated by mixing and the carbon dioxide bubbles generated by yeast fermentation.…”

“…In the wheat dough, prolamins are principally located in the bulk of the gluten network but also at the interface of the air bubbles incorporated by mixing and the carbon dioxide bubbles generated by yeast fermentation. They are thus susceptible to participate to the stabilization of the alveolar structure of baked products 18 . Several studies have been performed at the air-water 19,20 and air-solid interfaces.…”

Interfacial Behavior of Wheat Puroindolines: Study of Adsorption at the Air–Water Interface from Surface Tension Measurement Using Wilhelmy Plate Method

“…Husband et al (25) have shown that both PIN-a and PIN-b have comparable foaming properties. The interfacial properties of puroindolines along with other wheat proteins are of great interest both from biological and technological points of view (28,29). The importance of interfacial properties of wheat proteins has been reviewed byÖrnebro et al (28) and the structure-function relationships of major lipid-binding proteins from cereal kernels have recently been reviewed by Douliez et al (29).…”

Nanomechanical force measurements of gliadin protein interactions

“…The proteins also show emulsifying activity, foaming, and film-forming ability. 24 The biomechanical properties of wheat gluten proteins are usually described as a combination of viscous flow (extensibility) and elasticity, which has been proposed to originate from the -turn conformation, related to the repetitive amino acid sequences, rich in proline, glycine, and glutamine. 25 Besides from the internal structural motifs, which govern elastic behavior, there are differences in the surface hydrophobicity of the -and !-gliadins, which affect interactions with other gliadin and glutenin molecules, leading to macroscopic effects on baking quality.…”

“…25 Besides from the internal structural motifs, which govern elastic behavior, there are differences in the surface hydrophobicity of the -and !-gliadins, which affect interactions with other gliadin and glutenin molecules, leading to macroscopic effects on baking quality. 24 In this work, the evolving technique of force spectroscopy has been brought to bear on the strength and nature of pairwise interactions between monomeric gliadin proteins, -, !-!, and -!. The mechanical deformation of these proteins, and their intrinsic structure, has been observed as a function of native and denaturant environments, and the intermolecular adhesion phenomena have been measured.…”