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 553924
Title Influence of the polydispersity of pH 2 and pH 3.5 beta-lactoglobulin amyloid fibril solutions on analytical methods
Author(s) Heyn, Timon R.; Garamus, Vasil M.; Neumann, Hendrikje R.; Uttinger, Maximilian J.; Guckeisen, Tobias; Heuer, Monique; Selhuber-Unkel, Christine; Peukert, Wolfgang; Keppler, Julia K.
Source European Polymer Journal 120 (2019). - ISSN 0014-3057
Department(s) Food Process Engineering
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) Amyloid aggregates - AUC - Beta-lactoglobulin - Building-blocks - Fibrils - Polydispersity - SAXS - Superposition effects - Whey-protein - Worm-like fibrils

It is well known that amyloid beta-lactoglobulin (BLG) fibril solutions contain a heterogeneous mixture of amyloid aggregates and non-amyloid material. However, few information are available on how strongly separated fractions of different morphologies (straight fibrils at pH 2 and worm-like aggregates at pH 3.5) vary with respect to physicochemical properties and building blocks as most analyses are conducted with unfractionized solutions where superposition effects occur. The pH-value shift resulted in an altered degree of acid hydrolysis which led to dissimilar building blocks of the aggregates (peptides at pH 2, non-hydrolyzed protein at pH 3.5). The respective separated amyloid and non-amyloid fractions showed significantly different size (SAXS, SEC, AUC) and charge properties (Zeta potential) than the whole samples. Strong superposition effects were evident with common analyses such as FTIR, TRP fluorescence and Thioflavin-T. At the same time, structural differences of pH 2 and pH 3.5 aggregates could be presented more clearly.

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