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 509705
Title Relative contributions of charge and surface coverage on pH-induced flocculation of protein-stabilized emulsions
Author(s) Delahaije, Roy J.B.M.; Hilgers, Roelant J.; Wierenga, Peter A.; Gruppen, Harry
Source Colloids and Surfaces. A: Physicochemical and Engineering Aspects 521 (2017). - ISSN 0927-7757 - p. 153 - 160.
Department(s) Food Chemistry Group
Publication type Refereed Article in a scientific journal
Publication year 2017
Keyword(s) Charge - Emulsion stability - Protein adsorption - Surface coverage - Zeta potential - β-lactoglobulin

To predict the stability of protein-stabilized emulsions against flocculation under different conditions (pH and concentration), a quantitative description of the effect of the relevant factors is essential. Typically, pH is considered to affect the protein charge (viz. zeta potential) and thereby the interactions between the emulsion droplets. In this study, it is shown that emulsion flocculation is not only determined by the interactions between the droplets (pH/charge), but also by the surface coverage (pH and protein concentration). Two distinct regimes of flocculation were identified. At zeta potentials of |9-27|mV, emulsions were stable against flocculation if the protein concentration was sufficiently high to fully cover the interface (C>Ccr). At a lower zeta potential (i.e. below a critical zeta potential ζcr of |9|mV), flocculation occurred even at high concentrations. In this regime, flocculation below ζcr was reversible at C>Ccr, while it was partly irreversible at Ccr, indicating a type of bridging flocculation at Ccr. This shows that emulsion flocculation can be estimated based on the relevant parameters (ζ and protein radius including the association behaviour of the protein).

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