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Structure and dynamics of egg white ovalbumin adsorbed at the air/water interface

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Author: Kudryashova, E.V. · Meinders, M.B.J. · Visser, A.J.W.G. · Hoek, A. van · Jongh, H.H.J. de
Type:article
Date:2003
Source:European Biophysics Journal, 6, 32, 553-562
Identifier: 237238
doi: doi:10.1007/s00249-003-0301-3
Keywords: Nutrition · Food technology · Infrared reflection absorption spectroscopy · Protein structure · Surface compression · Surface layer · Time-resolved fluorescence anisotropy · egg white · ovalbumin · protein · water · absorption spectroscopy · adsorption · air · anisotropy · article · beta sheet · compression · dynamics · fluorescence · nonhuman · pressure · protein aggregation · protein folding · protein protein interaction · protein structure · Adsorption · Air · Colloids · Egg Proteins · Oligopeptides · Ovalbumin · Protein Conformation · Protein Structure, Secondary · Spectrometry, Fluorescence · Spectrophotometry, Infrared · Structure-Activity Relationship · Surface Properties · Surface Tension · Water

Abstract

The molecular properties of egg white ovalbumin adsorbed at the air/water interface were studied using infrared reflection absorption spectroscopy (IRRAS) and time-resolved fluorescence anisotropy (TRFA) techniques. Ovalbumin adsorbed at the air/ water interface adopts a characteristic partially unfolded conformation in which the content of the β-sheet is 10% lower compared to that of the protein in bulk solution. Adsorption to the interface leads to considerable changes in the rotational dynamics of ovalbumin. The results indicate that the end-over-end mobility of the ellipsoidal protein becomes substantially restricted. This is likely to reflect a preferential orientation of the protein at the interface. Continuous compression of surface layers of ovalbumin causes local aggregation of the protein, resulting in protein-network formation at the interface. The altered protein-protein interactions contribute to the strong increase in surface pressure observed.