Aggregation of β-lactoglobulin regulated by glucosylation

article





Broersen, K.

Elshof, M.

Groot, J.de

Voragen, A.G.J.

Hamer, R.J.

Jongh, H.H.J.de
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 β-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. © 2007 American Chemical Society.
Topics






















Food technologyβ-lactoglobulinAggregationElectrostatic repulsionGlucosylationHydrophobicityUnfolding/refoldingLactoglobulinChemistryElectricityGlycosylationHeatKineticsProtein denaturationProtein foldingElectrostaticsGlycosylationHeatKineticsLactoglobulinsProtein DenaturationProtein FoldingBovinae
TNO Identifier
239900
Repository link
https://resolver.tno.nl/uuid:2373e731-738b-4535-b6e1-8dde0019308d
ISSN
00218561
Source
Journal of Agricultural and Food Chemistry, 55(6), pp. 2431-2437.
Pages
2431-2437
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