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 490221
Title Interactions in protein mixtures. Part II: A virial approach to predict phase behavior
Author(s) Ersch, C.; Linden, E. van der; Martin, A.H.; Venema, P.
Source Food Hydrocolloids 52 (2016). - ISSN 0268-005X - p. 991 - 1002.
Department(s) Physics and Physical Chemistry of Foods
Publication type Refereed Article in a scientific journal
Publication year 2016
Abstract A virial theory was used to relate molecular interactions (in terms of second virial coefficients, B') and molecular size ratios to liquid–liquid phase separation. Application of the virial theory to binary hard sphere mixtures (additive and non-additive) confirmed the applicability of this simple approach towards predicting phase behavior based on two-particle interactions. Experimentally, second cross virial coefficients were obtained for dextran/gelatin, whey protein isolate (WPI)/gelatin mixtures and whey protein aggregate (WPA)/gelatin mixtures using membrane osmometry at varying ionic strength. From this, solvent conditions where interactions between proteins are dominated by electrostatics and solvent conditions where interactions are dominated by hard body interactions could be determined. Using experimentally obtained second virial coefficients, the liquid–liquid phase separation for gelatin/dextran mixtures was successfully predicted. Second cross virial coefficients for gelatin/whey protein isolate and for gelatin/whey protein aggregate could be related to the absence of phase separation in these mixtures. This could be related to a similar size of the proteins and their non-additive behavior at conditions where they mainly interact via hard body interactions.
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