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 354354
Title Heat-induced whey protein isolate fibrils: Conversion, hydrolysis, and disulphide bond formation
Author(s) Bolder, S.G.; Vasbinder, A.; Sagis, L.M.C.; Linden, E. van der
Source International Dairy Journal 17 (2007). - ISSN 0958-6946 - p. 846 - 853.
Department(s) Physics and Physical Chemistry of Foods
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) beta-lactoglobulin - amyloid fibrils - gelation
Abstract Fibril formation of individual pure whey proteins and whey protein isolate (WPI) was studied. The heat-induced conversion of WPI monomers into fibrils at pH 2 and low ionic strength increased with heating time and protein concentration. Previous studies, using a precipitation method, size-exclusion method, or proton NMR spectroscopy, reported a wide range of values for the conversion. An alternative method was developed, namely centrifugal filtration, giving a consistent picture of the conversion. The present results help to explain the disparities reported in literature. No fibrils formed upon heating pure ¿-lactalbumin or pure BSA at pH 2, whereas fibrils formed in pure ß-lactoglobulin (ß-lg) and WPI solutions. Experiments indicate that ß-lg was the only whey protein involved in fibril formation. In all whey protein samples, hydrolysis occurred during heating at pH 2, as determined by HPLC and SDS-PAGE. When WPI fibrils formed at pH 2 were stored at pH 7 or 10, disulphide bonds were formed in the samples. Keywords: Heat-induced aggregation; Whey proteins; Fibrils; Conversion; HPLC; SDS-PAGE
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