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 357174
Title Aggregation of -Lactoglobulin Regulated by Glucosylation
Author(s) Broersen, K.; Elshof, E.; Groot, J. de; Voragen, A.G.J.; Hamer, R.J.; Jongh, H.H.J. de
Source Journal of Agricultural and Food Chemistry 55 (2007)6. - ISSN 0021-8561 - p. 2431 - 2437.
DOI https://doi.org/10.1021/jf063178z
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) heat-induced aggregation - amyloid formation - fibril formation - protein - glycoprotein - stability - hydrophobicity - glycosylation - calreticulin - denaturation
Abstract A large number of proteins are glycosylated, either in vivo or as a result of industrial processing. Even though the effect of glycosylation on the aggregation of proteins has been studied extensively in the past, some reports show that the aggregation process is accelerated, whereas others found that the process is inhibited by glycosylation. This paper investigates the reasons behind these controversial results as well as the potential mechanism of the effect of glucosylation on aggregation using bovine -lactoglobulin as a model. Glucosylation was found to inhibit denaturant-induced aggregation, whereas heat-induced aggregation was accelerated. It was also found that the kinetic partitioning from an unfolded state was driven toward refolding for glucosylated protein, whereas aggregation was the preferred route for the nonglucosylated protein. Keywords: Aggregation; glucosylation; -lactoglobulin; hydrophobicity; electrostatic repulsion; unfolding/refolding
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