Title
Structure and dynamics of egg white ovalbumin adsorbed at the air/water interface
Author
Kudryashova, E.V.
Meinders, M.B.J.
Visser, A.J.W.G.
van Hoek, A.
de Jongh, H.H.J.
Publication year
2003
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.
Subject
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
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http://resolver.tudelft.nl/uuid:425367e3-c4df-4f1d-99da-8eaf43e273e6
DOI
https://doi.org/10.1007/s00249-003-0301-3
TNO identifier
237238
ISSN
0175-7571
Source
European Biophysics Journal, 32 (6), 553-562
Document type
article