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 505371
Title Controlling the ratio between native-like, non-native-like, and aggregated β-lactoglobulin after heat treatment
Author(s) Delahaije, Roy J.B.M.; Gruppen, Harry; Eijk-Van Boxtel, Evelien L. Van; Cornacchia, Leonardo; Wierenga, Peter A.
Source Journal of Agricultural and Food Chemistry 64 (2016)21. - ISSN 0021-8561 - p. 4362 - 4370.
DOI https://doi.org/10.1021/acs.jafc.6b00816
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) aggregation - concentration - denaturation - ionic strength - pH - refolding - structure - temperature - unfolding
Abstract

The amount of heat-denatured whey protein is typically determined by pH 4.6 precipitation. Using this method, a significant amount of nondenatured protein was reported even after long heating times. Apparently, a fraction of the unfolded protein refolds into the "native" state rather than form aggregates. This fact is known and has been explained using kinetic models. How the conditions affect the refolding and aggregation is, however, not fully understood. Therefore, this study investigates the unfolding, refolding, and aggregation process of β-lactoglobulin using circular dichroism and size-exclusion chromatography to characterize different folding variants and to quantify their content. The proteins remaining in solution at pH 4.6 were confirmed to be native-like. The nonaggregated fraction contains proteins with a native-like and two types of non-native-like conformations. The nonaggregated fraction increased with decreasing temperature (60-90 °C) and concentration (1-50 g/L) and increasing electrostatic repulsion (pH 7-8; 0-50 mM). The native-like fraction in the nonaggregated fraction was independent of pH, ionic strength, and concentration but increased with decreasing temperature.

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