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Reversible self-association of ovalbumin at air-water interfaces and the consequences for the exerted surface pressure

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Author: Kudryashova, E.V. · Visser, A.J.W.G. · Jongh, H.H.J.de
Type:article
Date:2005
Institution: TNO Kwaliteit van Leven
Source:Protein Science, 2, 14, 483-493
Identifier: 238326
doi: doi:10.1110/ps.04771605
Keywords: Nutrition · Food technology · Aggregation · Air-water interface · FCS · IRRAS · Ovalbumin · monomer · ovalbumin · succinic acid derivative · water · adsorption · air water interface · article · covalent bond · desorption · diffusion · dissociation · egg · electricity · flow kinetics · fluorescence correlation spectroscopy · heat treatment · infrared reflection absorption spectroscopy · priority journal · protein aggregation · protein assembly · protein conformation · protein modification · spectroscopy · surface property · surface tension · Adsorption · Air · Animals · Boron Compounds · Chickens · Electrostatics · Heat · Kinetics · Microscopy, Fluorescence · Ovalbumin · Ovum · Pressure · Protein Conformation · Protein Structure, Secondary · Proteomics · Rheology · Spectrometry, Fluorescence · Spectroscopy, Fourier Transform Infrared · Surface Properties · Time Factors · Water · Gallus gallus

Abstract

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 ovalbumin-being a cluster of 12-16 predominantly noncovalently bound proteins, and succinylated ovalbumin, 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.