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 442717
Title Protein Concentration and Protein-Exposed Hydrophobicity as Dominant Parameters Determining the Flocculation of Protein-Stabilized Oil-in-Water Emulsions
Author(s) Delahaije, R.J.B.M.; Wierenga, P.A.; Nieuwenhuijzen, N.H. van; Giuseppin, M.L.F.; Gruppen, H.
Source Langmuir 29 (2013)37. - ISSN 0743-7463 - p. 11567 - 11574.
DOI http://dx.doi.org/10.1021/la401314a
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2013
Keyword(s) diffusing wave spectroscopy - beta-lactoglobulin - coalescence stability - disjoining pressure - drop size - adsorption - films - ph - interfaces - ovalbumin
Abstract DLVO theory is often considered to be applicable to the description of flocculation of protein-stabilized oil-in-water emulsions. To test this, emulsions made with different globular proteins (ß-lactoglobulin, ovalbumin, patatin, and two variants of ovalbumin) were compared under different conditions (pH and electrolyte concentration). As expected, flocculation was observed under conditions in which the zeta potential is decreased (around the isoelectric point and at high ionic strength). However, the extent of flocculation at higher ionic strength (>50 mM NaCl) decreased with increasing protein-exposed hydrophobicity. A higher exposed hydrophobicity resulted in a higher zeta potential of the emulsion droplets and consequently increased stability against flocculation. Furthermore, the addition of excess protein strongly increased the stability against salt-induced flocculation, which is not described by DLVO theory. In the protein-poor regime, emulsions showed flocculation at high ionic strength (>100 mM NaCl), whereas emulsions were stable against flocculation if excess protein was present. This research shows that the exposed hydrophobicity of the proteins and the presence of excess protein affect the flocculation behavior.
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