Start Publications Structural-rheological characteristics of Chaplin E peptide at ...
KSV NIMA

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

Year: 2020

Journal: Int. J. Biol. Macromol., Volume 144, FEB 1, page 742–750

Authors: Dokouhaki, M; Prime, EL; Qiao, GG; Kasapis, S; Day, L; Gras, SL

Organizations: Australian GovernmentAustralian GovernmentCGIAR; ARC Dairy Innovation HubAustralian Research Council [IH2010005]; ARC Research Hub for Future FibresAustralian Research Council [IH140100018]

Keywords: Atomic force microscopy; Dilatational rheology; Canal viscometry; Chaplin E; Transmission electron microscopy; Foam stability

The Chaplin E peptide is a surface-active agent that can adsorb to the air/water interface and form interfacial films that display distinct interfacial properties as a function of pH. The similar to 2 nm thick homogeneous Chaplin E film formed under acidic conditions contains ordered structures that give a high dilatational elasticity. In contrast, the heterogeneous film formed under basic conditions contained fibrils resulting in a rough similar to 17 nm thick film with predominantly viscoelastic properties, probably due to the reduced intermolecular interactions. These fibrils were also susceptible to breakage, fragmenting into shorter fibrils, which gave a greater elasticity. The fibrils also lead to a greater shear viscosity compared to the ordered structures aligned within the Chaplin E film at pH 3.0. A higher stability was observed for the foam formed by the Chaplin E compared to the foam formed by beta-lactoglobulin, consistent with the greater rheological properties observed for the Chaplin E film at the interface. Our findings suggest that Chaplin E has potential to provide long time stability to dispersions in food, consumer goods or pharmaceutical applications, forming films with greater rheological properties and at least similar thickness to those formed by other surface-active proteins such as beta-casein and beta-lactoglobulin. (C) 2019 Elsevier B.V. All rights reserved.