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 351424
Title Fibril assembly in whey protein mixtures
Author(s) Bolder, S.G.
Source Wageningen University. Promotor(en): Erik van der Linden, co-promotor(en): Leonard Sagis. - [S.l.] : S.n. - ISBN 9789085045212 - 116
Department(s) Physics and Physical Chemistry of Foods
VLAG
Publication type Dissertation, internally prepared
Publication year 2007
Keyword(s) wei-eiwit - gelering - reologie - optica - whey protein - gelation - rheology - optics
Categories Food Physics
Abstract The objective of this thesis was to study fibril assembly in mixtures of whey proteins. The effect of the composition of the protein mixture on the structures and the resulting phase behaviour was investigated. The current work has shown that beta-lactoglobulin is responsible for the fibril assembly in whey protein mixtures upon heating at pH 2 and low ionic strength. To determine the efficiency of fibril formation, a method was developed to measure the conversion of whey protein monomers into fibrils. This method was used to study the effect of heating time, protein concentration, and stirring and seeding on the formation of fibrils in whey protein isolate solutions. The results have provided a better understanding of the mechanism of fibril formation and a model for fibril formation is proposed, including an activation, nucleation, growth, and termination step. Based on the method to measure the conversion two fast assays were found to determine the fibril concentration quantitatively. These two fast assays can be used for studying the kinetics of protein assembly in general, once they have been calibrated for a certain protein.
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