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

journal contribution
posted on 2020-02-01, 00:00 authored by M Dokouhaki, Emma PrimeEmma Prime, G G Qiao, S Kasapis, L Day, S L Gras
© 2019 Elsevier B.V. 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 ~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 ~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 β-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 β-casein and β-lactoglobulin.

History

Journal

International Journal of Biological Macromolecules

Volume

144

Pagination

742 - 750

Publisher

Elsevier

Location

Amsterdam, The Netherlands

ISSN

0141-8130

eISSN

1879-0003

Language

eng

Publication classification

C1 Refereed article in a scholarly journal; C Journal article

Copyright notice

2020, Elsevier