Food Biophysics

, Volume 2, Issue 4, pp 125–132 | Cite as

Formation of Multilayers at the Interface of Oil-in-Water Emulsion via Interactions between Lactoferrin and β-Lactoglobulin

  • Aiqian Ye
  • Harjinder SinghEmail author


The interactions between negatively charged β-lactoglobulin and the positively charged lactoferrin at the droplet surface to form a multi-protein surface layer were examined. Addition of lactoferrin to the aqueous phase of emulsions formed with β-lactoglobulin at pH 7.0 caused an increase in the ζ-potential of emulsion droplets, and the ζ-potential became positive as the concentration of added lactoferrin was higher than 1% in the system. It is found that lactoferrin binds to adsorbed β-lactoglobulin at droplet surface probably via electrostatic interactions. The amount of lactoferrin at interface increased with increasing the concentration of added lactoferrin, but it decreased with a decrease in the pH. No lactoferrin was observed at interface at pH 3 and 4. By contrast, when β-lactoglobulin was added in the emulsions formed with lactoferrin at pH 7.0, the ζ-potential of emulsions changed from positive to negative as the concentration of added β-lactoglobulin increased. The amount of β-lactoglobulin at surface increased correspondingly with increasing the concentration of added β-lactoglobulin. However, in this case, β-lactoglobulin remained bound at interface even at pH 3 and 4 where both lactoferrin and β-lactoglobulin are positively charged. The association of lactoferrin or β-lactoglobulin with the surface proteins that have oppositely charge is probably mainly through electrostatic interactions between the two proteins. It appears that alternative layers of these proteins could be created at the droplet surface.


β-Lactoglobulin Lactoferrin emulsion ζ-Potential Multi-protein surface 



We gratefully acknowledge financial support from the New Zealand Foundation for Research, Science and Technology. We thank Dandan Chen, Jeniene Gilliland, and Michelle Tamehana for assistance with the experimental work.


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Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  1. 1.Riddet Centre, Massey UniversityPalmerston NorthNew Zealand

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