Team Leader (SynGBT)

Dr. Thomas Rexer
Dr. Thomas Rexer
Phone: +49 391 6110 375
Room: N0.03

Team (SynGBT)

Reza Mahour, MSc
Phone: +49 391 6110 371
Room: S0.11
Lisa Wenzel, M. Sc.
Lisa Wenzel, M. Sc.
Phone: +49 391 6110 229
Room: N0.04
Links: RG
Anja Bastian
Technical Assistant
Phone: +49 391 67 546 70
Room: G25-123

Cooperations

Martin-Luther-University Halle-Wittenberg, Chair of Downstream Processing

Analysis and Redesign of Biological Networks (ARB), MPI Magdeburg

Physical and Chemical Foundations of Process Engineering (PCF), MPI Magdeburg

Otto-von-Guericke University Magdeburg, Chair of Bioprocess Engineering

Completed Projects

German Federal Ministry of Education and Research (BMBF) project: "Aufbau einer Plattform zur in-vitro N-Glykosylierung von Proteinen unter Ausnutzung einer Kaskade isolierter Enzyme" in the BMBF funding programm "Biotechnologie 2020+", Call: "Basistechnologien" (grant identifier 031A156B)
Started: 11/2012. End: 04/2018.

Synthetic GlycoBioTechnology

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Synthetic Glycobiotechnology

Motivation

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.

References

1.
Mahour, R.; Klapproth, J.; Rexer, T.; Schildbach, A.; Klamt, S.; Pietzsch, M.; Rapp, E.; Reichl, U.: Establishment of a five-enzyme cell-free cascade for the synthesis of uridine diphosphate N-acetylglucosamine. Journal of Biotechnology 283, pp. 120 - 129 (2018)
2.
Rexer, T.; Schildbach, A.; Klapproth, J.; Schierhorn, A.; Mahour, R.; Pietzsch, M.; Rapp, E.; Reichl, U.: One pot synthesis of GDP-mannose by a multi-enzyme cascade for enzymatic assembly of lipid-linked oligosaccharides. Biotechnology and Bioengineering 115 (1), pp. 192 - 205 (2018)
 
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