Conformational changes to deamidated wheat gliadins and β-casein upon adsorption to oil–water emulsion interfaces

Role of interfacial protein membrane in oxidative stability of vegetable oil substitution emulsions applicable to nutritionally modified sausage

“…The physicochemical stability of a protein-based emulsion depends on the structure of adsorbed protein layers and whether other surfactants are present (Dickinson, 1992;Wong et al, 2012). The specific structure of the interfacial protein layer(s), thus, the emulsifying properties, is derived from the inherent structural characteristics of the protein, for example, a flexible structure with random coils in β-casein (Dickinson, Rolfe, & Dalgleish, 1988;Evers, Andersson, Lund, & Skepö, 2012), an elongated fibrous structure in myosin (Galluzzo & Regenstein, 1978b;Hong, Min, & Chin, 2012), and a compact globular structure in β-lactoglobulin (Zhai et al, 2011).…”

“…Considerable changes at the secondary and tertiary structural levels could occur on these proteins when they are brought to the surface of the fat globule through homogenization . On the other hand, for proteins with a high molecular mass and multiple subunits, such as soy β-conglycinin (Miriani, Keeratiu-rai, Corredig, Iametti, & Bonomi, 2011) and wheat gliadin (Wong et al, 2012), the compact molecular structure stabilized by disulfide bonds, hydrophobic contacts, and van der Waal's interactions limits their conformational rearrangement upon adsorption to the emulsion interface.…”

Interfacial peptide partitioning and undiminished antioxidative and emulsifying activity of oxidatively stressed soy protein hydrolysate in an O/W emulsion

“…Therefore, the amount of protein adsorbed at the water-oil interface and the structure of the adsorbed proteins could influence the stability of emulsions during storage. It has been reported that the conformational flexibility plays an important role in the ability of a protein to adsorb at a water-oil interface (Wong et al, 2012). Enzymatic hydrolysis has a great impact on protein emulsifying capacity due to significant alterations of protein structure by peptide chain cleavage.…”

From high milk protein powders to the rehydrated dispersions in variable ionic environments: A review

“…Behavior II: wetting stage, no swelling stage, and rehydration stage not observed (Adopted from Hussain et al, 2011b). resonance (NMR) (Bansal et al, 2006;Le Feunteun et al, 2012), Circular Dichroism (CD) (Creamer et al, 1981;Farrell et al, 2001;Wong et al, 2012), Raman spectroscopy (Ashton et al, 2010;Ashton et al, 2011), small ray-angle scattering (SAXS) (Mata et al, 2011;Zhai et al, 2012) and infrared spectroscopy (FTIR) (Gaiani et al, 2011;Hussain et al, 2011a;Sikand et al, 2011). Irrespective of a vast and important role of salts and casein in dairy industry (see Section 3), we find a dearth of literature corresponding to its effect on the secondary structure of this milk protein.…”