Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 479693
Title Quantitative description of the parameters affecting the adsorption behaviour of globular proteins
Author(s) Delahaije, R.J.B.M.; Gruppen, H.; Giuseppin, M.L.F.; Wierenga, P.A.
Source Colloids and Surfaces. B: Biointerfaces 123 (2014). - ISSN 0927-7765 - p. 199 - 206.
DOI https://doi.org/10.1016/j.colsurfb.2014.09.015
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2014
Keyword(s) air-water-interface - bovine serum-albumin - beta-lactoglobulin - rheological properties - air/water interface - surface rheology - kinetics - ovalbumin - charge - denaturation
Abstract The adsorption behaviour of proteins depends significantly on their molecular properties and system conditions. To study this relation, the effect of relative exposed hydrophobicity, protein concentration and ionic strength on the adsorption rate and adsorbed amount is studied using ß-lactoglobulin, ovalbumin and lysozyme. The curves of surface elastic modulus versus surface pressure of all three proteins, under different conditions (i.e. concentration and ionic strength) superimposed. This showed that the interactions between the adsorbed proteins are similar and that the adsorbed proteins retain their native state. In addition, the adsorption rate (kadsorb) was shown to scale with the relative hydrophobicity and ionic strength. Moreover, the adsorbed amount was shown to be dependent on the protein charge and the ionic strength. Based on these results, a model is proposed to predict the maximum adsorbed amount (Gmax). The model approximates the adsorbed amount as a close-packed monolayer using a hard-sphere approximation with an effective protein radius which depends on the electrostatic repulsion. The theoretical adsorbed amount was in agreement with experimental Gmax (±10%).
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