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Protein Science (2005), 14:483-493. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Reversible self-association of ovalbumin at air–water interfaces and the consequences for the exerted surface pressure

Elena V. Kudryashova1,2, Antonie J.W.G. Visser3 and Harmen H.J. De Jongh1,4

1 Wageningen Centre for Food Sciences, Wageningen, The Netherlands
2 Division of Chemical Enzymology, Chemistry Department, Moscow State University, 119899 Moscow, Russia
3 MicroSpectroscopy Centre, Laboratory of Biochemistry, Wageningen University, Wageningen, The Netherlands
4 TNO Nutrition and Food Research Institute, Zeist, The Netherlands

(RECEIVED March 25, 2004; FINAL REVISION May 12, 2004; ACCEPTED May 18, 2004)

In this study the relation between the ability of protein self-association and the surface properties at air–water interfaces is investigated using a combination of spectroscopic techniques. Three forms of chicken egg ovalbumin were obtained with different self-associating behavior: native ovalbumin, heat-treated ov-albumin—being a cluster of 12–16 predominantly noncovalently bound proteins, and succinylated ovalbu-min, as a form with diminished aggregation properties due to increased electrostatic repulsion. While the bulk diffusion of aggregated protein is clearly slower compared to monomeric protein, the efficiency of transport to the interface is increased, just like the efficiency of sticking to rather than bouncing from the interface. On a timescale of hours, the aggregated protein dissociates and adopts a conformation comparable to that of native protein adsorbed to the interface. The exerted surface pressure is higher for aggregated material, most probably because the deformability of the particle is smaller. Aggregated protein has a lower ability to desorb from the interface upon compression of the surface layer, resulting in a steadily increasing surface pressure upon reducing the available area for the surface layer. This observation is opposite to what is observed for succinylated protein that may desorb more easily and thereby suppresses the buildup of a surface pressure. Generally, this work demonstrates that modulating the ability of proteins to self-associate offers a tool to control the rheological properties of interfaces.

Keywords: ovalbumin; aggregation; air–water interface; IRRAS; FCS

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04771605.

Reprint requests to: Harmen H.J. de Jongh, Wageningen Centre for Food Sciences, Diedenweg 20, 6703 GW, Wageningen, The Netherlands; e-mail: harmen.dejongh{at}wur.nl; fax: 31-317-484893.


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