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 327540
Title Mesostructure of fibrillar protein gels
Author(s) Veerman, C.; Sagis, L.M.C.; Linden, E. van der
Source In: Proceedings of the 3rd international symposium on Food rheology and structure. - Lappersdorf Germany : Kerschensteiner Verlag - ISBN 3905609193 - p. 385 - 388.
Event Lappersdorf Germany : Kerschensteiner Verlag - ISBN 3905609193 International symposium, 2003-02-09/2003-02-13
Department(s) Physics and Physical Chemistry of Foods
VLAG
Publication type Contribution in proceedings
Publication year 2003
Abstract We investigated the mesostructure of three different food proteins (ß-lactoglobulin (ß-lg), bovine serum albumin (BSA), and ovalbumin), after protein assembly at pH 2, using rheology and transmission electron microscopy (TEM). TEM micrographs showed fibrils with a contour length of about 2-7 µm for ß-lg, 100-300 nm for BSA, and 150-300 nm for ovalbumin. Using the results of rheological measurements, the critical percolation concentration (cp) was determined as a function of ionic strength. A decrease of cp with increasing ionic strength was found for all three proteins. All proteins studied in this work assemble into fibrils that form a homigeneoous isotropic network at low protein concentrations. The aggregation process was reversible for BSA, bus irreversible for ß-lg and ovalbumin, which may be due to the formation of intermolecular ß-sheets in these proteins. The linear decrese of cp with the Debye screening length is explained by an adjusted random contact model for charged semiflexible fibrils. Using this model we can estimate a persistence length for each of the proteins. The persistence length was 1.6 ± 0.4 µm for ß-lg, 16 ± 4 nm for BSA, and 300 ± 75 nm for ovalbumin.
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