About us

  • The chitinolytic enzyme system of Serratia marcescens. Chitin is shown as densely packed polymer chains of GlcNAc (open circles). ChiB degrades the chains from their non-reducing ends (labeled ‘NR’) and ChiA from the reducing ends (labeled ‘R’); both enzymes use a processive mechanism  thus predominantly producing chitobiose (the repetitive unit in the substrate). ChiC makes random cuts in the more amorphous regions of the substrate opening these regions for attacks from ChiA and ChiB. Note that ChiC also has a CBM but that the position of this CBM is not clear due to lacking structural information. CBP21, originally described by Takeshi Watanabe and co-workers as a 21 kDa chitin-binding protein, is an LPMO that makes oxidative cuts in the most ordered and crystalline regions of the substrate yielding aldonic acids (GlcNAcA; filled circles) at the newly generated
downstream ends. Thus, the LPMO promotes the action of the chitinases (see here ). The chitobiase converts chitobiose and short chito-oligosaccharides to monomers. For more details on this system, see here .
    Photo
    http://www.jbc.org/content/280/31/28492.long

The group is led by group leader Professor Vincent Eijsink and deputy group leader Professor Gustav Vaaje-Kolstad. The group works on production, engineering, characterization and application of proteins and enzymes, in various contexts, such as biomass processing, bacterial pathogenicity, microbial ecology and vaccine development.

 

About us

Twenty years ago, the group worked primarily on two things: (1) the enzymology of chitin conversion & (2) developing lactic acid bacteria as vaccine carriers.

 

The vaccine research has been ongoing for many years, involving a few researchers and many MSc students, and has in recent years been supported by two consecutive grants from the Norwegian GlobVac programme. This work is led by Ass Prof. Geir Mathiesen.

 

The chitin work has drastically expanded in the past fifteen years, in part due to the discovery of a completely new enzyme activity that was first detected in our group in 2005 and that we described in detail in a landmark Science paper in 2010. These novel enzymes are today referred to as Lytic Polysaccharide Monooxygenases, or LPMOs. Since 2005, our enzyme work has been expanding to involve multiple industrial enzymes, including enzymes acting on proteins and, most importantly, enzymes acting on lignocellulosic biomass. The LPMOs caught, and are still catching, a lot of attention, since they are important for efficient bioprocessing of lignocelluosic biomass and since they are intriguing and abundant enzymes that likely have additional, hitherto undiscovered functions and whose catalytic function is only partly understood. For more information, see e.g. here:

 https://pubs.acs.org/doi/10.1021/acscatal.9b00246

https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-019-1392-0

 https://www.sciencedirect.com/science/article/pii/S0959440X18301441?via%3Dihub

 https://mmbr.asm.org/content/82/4/e00029-18.long

Today, we have a large portfolio of enzyme projects, varying from fundamental structure-function studies to applied projects focusing on bioprocess development. The main scientific driver in these projects is to unravel how Nature manages to break down highly recalcitrant materials such as shrimp shells, wood and straw. The main applied driver is the need for developing green technologies (i.e., enzyme- and fermentation-based) for valorizing of non-edible biomass, such as forest residues and straw, as well as chitin-rich materials such as shrimp shells.

 

In 2016 the more applied and bioprocess-oriented part of the PEP-group became an independent group led by Professor Svein Horn, called the Bioprocess Technology and Biorefining (BioRef) group. The BioRef and PEP groups regularly collaborate, for example within large projects such as Foods of Norway and Bio4Fuels.

 

During the past decade, we have developed multiple spin-off activities. Driven by Phil Pope, who joined the group in 2009, we have developed research in microbial ecology, in particular on biomass-processing microbial communities. Today, Phil leads his own group, the MEMO group (Microbial Ecology and Meta-Omics). While, today, both Phil and the MEMO group are formally based at another department, several MEMO members are located in the PEP group, especially those doing metaproteomics. There is a lot of collaboration.

 

Interestingly, -omics data indicate that chitinases, the first enzymes studied in our group, and LPMOs, discovered by our group in 2005/2010, both play a role in bacterial virulence. Thus, these enzymes putatively present totally new virulence factors and their study may lead to unravelling novel aspects of bacterial pathogenicity. These topics are pursued by Deputy Group leader Professor Gustav Vaaje-Kolstad and his team, who today are focusing on revealing alternative functions of enzymes originally thought only to be involved in biomass processing.

 

When it comes to advanced enzyme kinetics and biophysical studies of enzymes, we collaborate closely with Professor Morten Sørlie and researcher Åsmund Røhr Kjendseth in the Natural Product Chemistry and Organic Analysis group. Importantly, this collaboration will be central in the CUBE project, which is funded by an ERC Synergy grant that we received in 2019. In CUBE, which will run from 2020 to 2026, we aim at developing novel, LPMO-inspired catalysts.

 

As described above, the PEP group aims at combining high-level basic research with applied studies and innovation. Our main current funders are NMBU, The Research Council of Norway (NFR), The Novo-Nordisk Foundation, the Horizon 2020 program, Industry, and the ERC (Synergy grant).

 

For students, we can offer a wide variety of MSc projects, especially for students that do a 60 ECTS project, and we can tailor the projects according to the interest of the student. In their projects, students can learn about many (combinations of) topics, including:

  • Gene manipulation technologies
  • Protein expression and purification
  • Basic and advanced enzymology
  • Applied enzymology
  • Bioorganic analytics (various types of chromatography and mass spectrometry)
  • Omics technologies, in particular (meta-)proteomics
  • Protein structure, engineering and bioinformatics
  • Bioprocess development (normally in collaboration with Bioref)
  • Molecular microbiology
  • Cell biology

 

Available positions for PhD students and post-docs are announced at www.jobborge.no. If there are no announced positions, we cannot normally offer a position. However, if you have a strong CV and motivation to work on our topics, you are welcome to contact us. Do not send standard letters without a clear specific motivation for working with us; such letters will be discarded.

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Published 10. January 2020 - 12:09 - Updated 12. January 2020 - 21:30