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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 491061
Title Towards predicting the stability of protein-stabilized emulsions
Author(s) Delahaije, R.J.B.M.; Gruppen, H.; Giuseppin, M.L.F.; Wierenga, P.A.
Source Advances in Colloid and Interface Science 219 (2015). - ISSN 0001-8686 - p. 1 - 9.
DOI https://doi.org/10.1016/j.cis.2015.01.008
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2015
Keyword(s) in-water emulsions - random sequential adsorption - equation-of-state - beta-lactoglobulin - light-scattering - latex-particles - quantitative description - exposed hydrophobicity - globular-proteins - diffusing wave
Abstract The protein concentration is known to determine the stability against coalescence during formation of emulsions. Recently, it was observed that the protein concentration also influences the stability of formed emulsions against flocculation as a result of changes in the ionic strength. In both cases, the stability was postulated to be the result of a complete (i.e. saturated) coverage of the interface. By combining the current views on emulsion stability against coalescence and flocculation with new experimental data, an empiric model is established to predict emulsion stability based on protein molecular properties such as exposed hydrophobicity and charge. It was shown that besides protein concentration, the adsorbed layer (i.e. maximum adsorbed amount and interfacial area) dominates emulsion stability against coalescence and flocculation. Surprisingly, the emulsion stability was also affected by the adsorption rate. From these observations, it was concluded that a completely covered interface indeed ensures the stability of an emulsion against coalescence and flocculation. The contribution of adsorption rate and adsorbed amount on the stability of emulsions was combined in a surface coverage model. For this model, the adsorbed amount was predicted from the protein radius, surface charge and ionic strength. Moreover, the adsorption rate, which depends on the protein charge and exposed hydrophobicity, was approximated by the relative exposed hydrophobicity (QH). The model in the current state already showed good correspondence with the experimental data, and was furthermore shown to be applicable to describe data obtained from literature.
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