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