Repository hosted by TU Delft Library

Home · Contact · About · Disclaimer ·

Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces

Publication files not online:

Author: Wierenga, P.A. · Meinders, M.B.J. · Egmond, M.R. · Voragen, A.G.J. · Jongh,
Institution: TNO Kwaliteit van Leven
Source:Journal of Physical Chemistry B, 35, 109, 16946-16952
Identifier: 238707
doi: doi:10.1021/jp050990g
Keywords: Nutrition · Food technology · Adsorption · Air · Chemical analysis · Colloids · Electric charge · Electrostatics · Hydrophobicity · Interfaces (materials) · Saturation (materials composition) · Water · Adsorption kinetics · Air-water interface · Electrostatic charge · Energy barrier · Surface pressure · Proteins · ovalbumin · water · adsorption · air · article · chemistry · flow kinetics · kinetics · protein secondary structure · protein tertiary structure · Adsorption · Air · Kinetics · Ovalbumin · Protein Structure, Secondary · Protein Structure, Tertiary · Rheology · Water


In this study a set of chemically engineered variants of ovalbumin was produced to study the effects of electrostatic charge on the adsorption kinetics and resulting surface pressure at the air-water interface. The modification itself was based on the coupling of succinic anhydride to lysine residues on the protein surface. After purification of the modified proteins, five homogeneous batches were obtained with increasing degrees of modification and ζ-potentials ranging from -19 to -26 mV (-17 mV for native ovalbumin). These batches showed no changes in secondary, tertiary, or quaternary structure compared to the native protein. However, the rate of adsorption as measured with ellipsometry was found to decrease with increasing net charge, even at the initial stages of adsorption. This indicates an energy barrier to adsorption. With the use of a model based on the random sequential adsorption model, the energy barrier for adsorption was calculated and found to increase from 4.1 kT to 6.1 kT when the protein net charge was increased from -12 to -26. A second effect was that the increased electrostatic repulsion resulted in a larger apparent size of the adsorbed proteins, which went from 19 to 31 nm2 (native and highest modification, respectively), corresponding to similar interaction energies at saturation. The interaction energy was found to determine not only the saturation surface load but also the surface pressure as a function of the surface load. This work shows that, in order to describe the functionality of proteins at interfaces, they can be described as hard colloidal particles. Further, it is shown that the build-up of protein surface layers can be described by the coulombic interactions, exposed protein hydrophobicity, and size. © 2005 American Chemical Society.