Glycans attached to proteins exert various important biological functions. They serve as recognition targets for glycan binding proteins, modulate the properties of proteins and can stabilize protein folding. One example of their biological significance is the binding of influenza viral particles to terminal sialic acid residues of glycans on the surface of epithelial cells
The importance of protein glycosylation for the biotech industry is highlighted by the fact that approximately 70% of therapeutic proteins, approved or in (pre-)clinical studies, are glycoproteins. However, there is still a lack of thorough scientific understanding of the structure-function relationships of glycans due to macro- and microheterogeneities of biological samples.
The Synthetic Glycobiotechnology group of the bioprocess engineering department develops process platforms for the efficient glycosylation of proteins. The complex design of these platforms integrates protein expression & purification, high-performance and high-resolution metabolite- and glycoanalytics as well as mathematical modelling of multienzyme networks. Therefore, the group closely cooperates with groups in-and outside the bioprocess department.