Journal article
Structural-rheological characteristics of Chaplin E peptide at the air/water interface; a comparison with β-lactoglobulin and β-casein.
Mina Dokouhaki, Emma L Prime, Greg G Qiao, Stefan Kasapis, Li Day, Sally L Gras
Int J Biol Macromol | Elsevier Inc. | Published : 2020
Abstract
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 great..
View full abstractGrants
Awarded by Australian Research Council
Funding Acknowledgements
The authors wish to acknowledge the Electron Microscopy Unit of The University of Melbourne, for assistance with electron microscopy, specifically Dr. Simon Crawford. The authors would also like to acknowledge the Australian Government for providing the Australian Postgraduate Award (APA) and International Postgraduate Research Scholarship (IPRS) for Mina Dokouhaki and thank the Particulate Fluids Processing Centre (PFPC), The Bio21 Molecular Science and Biotechnology Institute and RMIT Food Research and Innovation Centre for access to equipment. Sally Gras is supported by The ARC Dairy Innovation Hub (IH2010005). Emma Prime is supported by The ARC Research Hub for Future Fibres (IH140100018).