Structural-rheological characteristics of Chaplin E peptide at the air/water interface; a comparison with β-lactoglobulin and β-casein.

摘要: The Chaplin E peptide is a surface-active agent that can adsorb to the air/water interface and form interfacial films display distinct properties as function of pH. ~2 nm thick homogeneous film formed under acidic conditions contains ordered structures give high dilatational elasticity. In contrast, heterogeneous basic contained fibrils resulting in rough ~17 nm with predominantly viscoelastic properties, probably due reduced intermolecular interactions. These were also susceptible breakage, fragmenting into shorter fibrils, which gave greater lead shear viscosity compared aligned within at pH 3.0. A higher stability was observed for foam by β-lactoglobulin, consistent rheological interface. Our findings suggest has potential provide long time dispersions food, consumer goods or pharmaceutical applications, forming least similar thickness those other proteins such β-casein β-lactoglobulin.