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I defined my MSc project based on the knowledge gap for the interaction between cyclodextrin and proteins and setup my supervisor team Kim L. Larsen, Daniel E. Ozten and Reinhard Wimmer. Here I chose NMR spectroscopy as the main method to study the inclusion complex formation between cyclodextrin and proteins due to its ability to give atomic level information. I obtained MSc in Biotechnology at Aalborg University (Denmark) in 2001 [1, 2, 3].
The main focus of my PhD project was acquiring a deeper insight into structure elucidation with NMR and I started to work on alginate C-5 epimerases 2002-2005 in a collaboration between Svein Valla at NTNU (Norwegian University of Science and Technology) and Reinhard Wimmer at Aalborg University [4, 5, 6]. Besides using NMR, I also focus on functional characterization of the alginate epimerases (using ITC, CD, FS and protein engineering) to understand ionic and substrate/product interaction, mode of action and role of the subunits in the alginate epimerases.
During my Post Doc at NTNU (2005-2007) I continued with structure elucidation and functional characterization on selenocysteine containing proteins using NMR spectroscopy under the supervision of Alex Dykyy at NTNU. Here I also had a key role in building up the NMR structure determination facilities at the NV-faculty NMR center NTNU and today I lead the NMR laboratory.
I was recruited as senior scientist on structure elucidation of proteins and carbohydrates by NMR in NOBIPOL (The Norwegian Biopolymer Laboratory) at NTNU (2007-2016). During this period, we started a collaboration with Vincent Eijsink with focus on structure and functional determination of lytic polysaccharide monooxygenases (LPMO) with NMR [7, 8, 9, 10, 11, 12]. Here we used NMR in many ways, not only to obtain the structure, but also to get functional insight into the LPMOs and their products. Besides the LPMO we also continued to work with alginate epimerases and became interested in the chemo-enzymatic functionalization of alginate and other carbohydrates as well as the characterization thereof [13, 14, 15, 16, 17, 18, 19, 20]. The versatility of NMR is also shown in our work following enzymatic or chemical transformation in the NMR tube [21, 22].
Today, I’m leading Biopolymer NMR group at NTNU and we focus on structure and functional characterization on polysaccharides, carbohydrate modifying enzymes, multidomain proteins and biomaterials.
- Wimmer R, Aachmann FL, Larsen KL, and Petersen SB. (2002) NMR diffusion as a novel tool for measuring the association constant between cyclodextrin and guest molecules. Carbohydr Res. 337, 841-9. DOI:10.1016/s0008-6215(02)00066-6 |
- Otzen DE, Knudsen BR, Aachmann F, Larsen KL, and Wimmer R. (2002) Structural basis for cyclodextrins' suppression of human growth hormone aggregation. Protein Sci. 11, 1779-87. DOI:10.1110/ps.0202702 |
- Aachmann FL, Otzen DE, Larsen KL, and Wimmer R. (2003) Structural background of cyclodextrin-protein interactions. Protein Eng. 16, 905-12. DOI:10.1093/protein/gzg137 |
- Aachmann FL, Svanem BI, Güntert P, Petersen SB, Valla S, and Wimmer R. (2006) NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase. J Biol Chem. 281, 7350-6. DOI:10.1074/jbc.M510069200 |
- Rozeboom HJ, Bjerkan TM, Kalk KH, Ertesvåg H, Holtan S, Aachmann FL, Valla S, and Dijkstra BW. (2008) Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii. J Biol Chem. 283, 23819-28. DOI:10.1074/jbc.M804119200 |
- Gawin A, Tietze L, Aarstad OA, Aachmann FL, Brautaset T, and Ertesvåg H. (2020) Functional characterization of three Azotobacter chroococcum alginate-modifying enzymes related to the Azotobacter vinelandii AlgE mannuronan C-5-epimerase family. Sci Rep. 10, 12470. DOI:10.1038/s41598-020-68789-3 |
- Aachmann FL, Sørlie M, Skjåk-Bræk G, Eijsink VG, and Vaaje-Kolstad G. (2012) NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. Proc Natl Acad Sci U S A. 109, 18779-84. DOI:10.1073/pnas.1208822109 |
- Westereng B, Agger JW, Horn SJ, Vaaje-Kolstad G, Aachmann FL, Stenstrøm YH, and Eijsink VG. (2013) Efficient separation of oxidized cello-oligosaccharides generated by cellulose degrading lytic polysaccharide monooxygenases. J Chromatogr A. 1271, 144-52. DOI:10.1016/j.chroma.2012.11.048 |
- Isaksen T, Westereng B, Aachmann FL, Agger JW, Kracher D, Kittl R, Ludwig R, Haltrich D, Eijsink VG, and Horn SJ. (2014) A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J Biol Chem. 289, 2632-42. DOI:10.1074/jbc.M113.530196 |
- Courtade G, Wimmer R, Røhr ÅK, Preims M, Felice AK, Dimarogona M, Vaaje-Kolstad G, Sørlie M, Sandgren M, Ludwig R, Eijsink VG, and Aachmann FL. (2016) Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. Proc Natl Acad Sci U S A. 113, 5922-7. DOI:10.1073/pnas.1602566113 |
- Courtade G, Forsberg Z, Heggset EB, Eijsink VGH, and Aachmann FL. (2018) The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation. J Biol Chem. 293, 13006-13015. DOI:10.1074/jbc.RA118.004269 |
- Courtade G, Ciano L, Paradisi A, Lindley PJ, Forsberg Z, Sørlie M, Wimmer R, Davies GJ, Eijsink VGH, Walton PH, and Aachmann FL. (2020) Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study. Proc Natl Acad Sci U S A. 117, 19178-19189. DOI:10.1073/pnas.2004277117 |
- Tøndervik A, Klinkenberg G, Aachmann FL, Svanem BI, Ertesvåg H, Ellingsen TE, Valla S, Skjåk-Bræk G, and Sletta H. (2013) Mannuronan C-5 epimerases suited for tailoring of specific alginate structures obtained by high-throughput screening of an epimerase mutant library. Biomacromolecules. 14, 2657-66. DOI:10.1021/bm4005194 |
- Rieder A, Grimmer S, Aachmann FL, Westereng B, Kolset SO, and Knutsen SH. (2013) Generic tools to assess genuine carbohydrate specific effects on in vitro immune modulation exemplified by β-glucans. Carbohydr Polym. 92, 2075-83. DOI:10.1016/j.carbpol.2012.11.092 |
- Arlov Ø, Aachmann FL, Sundan A, Espevik T, and Skjåk-Bræk G. (2014) Heparin-like properties of sulfated alginates with defined sequences and sulfation degrees. Biomacromolecules. 15, 2744-50. DOI:10.1021/bm500602w |
- Dalheim MØ, Vanacker J, Najmi MA, Aachmann FL, Strand BL, and Christensen BE. (2016) Efficient functionalization of alginate biomaterials. Biomaterials. 80, 146-156. DOI:10.1016/j.biomaterials.2015.11.043 |
- Omtvedt LA, Dalheim MØ, Nielsen TT, Larsen KL, Strand BL, and Aachmann FL. (2019) Efficient Grafting of Cyclodextrin to Alginate and Performance of the Hydrogel for Release of Model Drug. Sci Rep. 9, 9325. DOI:10.1038/s41598-019-45761-4 |
- Vikøren Mo I, Feng Y, Øksnes Dalheim M, Solberg A, Aachmann FL, Schatz C, and Christensen BE. (2020) Activation of enzymatically produced chitooligosaccharides by dioxyamines and dihydrazides. Carbohydr Polym. 232, 115748. DOI:10.1016/j.carbpol.2019.115748 |
- Mo IV, Dalheim MØ, Aachmann FL, Schatz C, and Christensen BE. (2020) 2,5-Anhydro-d-Mannose End-Functionalized Chitin Oligomers Activated by Dioxyamines or Dihydrazides as Precursors of Diblock Oligosaccharides. Biomacromolecules. 21, 2884-2895. DOI:10.1021/acs.biomac.0c00620 |
- Westereng B, Kračun SK, Leivers S, Arntzen MØ, Aachmann FL, and Eijsink VGH. (2020) Synthesis of glycoconjugates utilizing the regioselectivity of a lytic polysaccharide monooxygenase. Sci Rep. 10, 13197. DOI:10.1038/s41598-020-69951-7 |
- Khong TT, Aachmann FL, and Vårum KM. (2012) Kinetics of de-N-acetylation of the chitin disaccharide in aqueous sodium hydroxide solution. Carbohydr Res. 352, 82-7. DOI:10.1016/j.carres.2012.01.028 |
- Leth ML, Ejby M, Workman C, Ewald DA, Pedersen SS, Sternberg C, Bahl MI, Licht TR, Aachmann FL, Westereng B, and Abou Hachem M. (2018) Differential bacterial capture and transport preferences facilitate co-growth on dietary xylan in the human gut. Nat Microbiol. 3, 570-580. DOI:10.1038/s41564-018-0132-8 |