Title
Reversible self-association of ovalbumin at air-water interfaces and the consequences for the exerted surface pressure
Author
Kudryashova, E.V.
Visser, A.J.W.G.
de Jongh, H.H.J.
TNO Kwaliteit van Leven
Publication year
2005
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.
Subject
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
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http://resolver.tudelft.nl/uuid:4c9d12cb-8fd2-4916-9f64-91f802784c39
DOI
https://doi.org/10.1110/ps.04771605
TNO identifier
238326
ISSN
0961-8368
Source
Protein Science, 14 (2), 483-493
Document type
article