title: Aggregation of beta-lactoglobulin regulated by glucosylation.
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 beta-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.
authors.affiliation: Wageningen Centre for Food Sciences, Diedenweg 20, P.O. Box 557, 6700 AN Wageningen, The Netherlands. broersen@mrc-lmb.cam.ac.uk
authors.forename: Kerensa
authors.initials: K
authors.lastname: Broersen
authors.forename: Marijke
authors.initials: M
authors.lastname: Elshof
authors.forename: Jolan
authors.initials: J
authors.lastname: De Groot
authors.forename: Alphons G J
authors.initials: AG
authors.lastname: Voragen
authors.forename: Rob J
authors.initials: RJ
authors.lastname: Hamer
authors.forename: Harmen H J
authors.initials: HH
authors.lastname: De Jongh
mesh_terms: D006031:Glycosylation; D006358:Hot Temperature; D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D055672:Static Electricity
chemical_list: D007782:Lactoglobulins