Aggregation of -Lactoglobulin Regulated by Glucosylation
Broersen, K. ; Elshof, E. ; Groot, J. de; Voragen, A.G.J. ; Hamer, R.J. ; Jongh, H.H.J. de - \ 2007
Journal of Agricultural and Food Chemistry 55 (2007)6. - ISSN 0021-8561 - p. 2431 - 2437.
heat-induced aggregation - amyloid formation - fibril formation - protein - glycoprotein - stability - hydrophobicity - glycosylation - calreticulin - denaturation
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