Kjendseth Lab
Norwegian University of Life Sciences (NMBU) · Faculty of Chemistry, Biotechnology and Food Science (KBM)
Åsmund Røhr Kjendseth leads the Kjendseth Lab at NMBU’s Faculty of Chemistry, Biotechnology and Food Science, where he also serves as Head of Education and Leader for the Chemistry research group (~20 members). We combine robotics, spectroscopy, and computation to understand how redox enzymes activate oxygen and remodel biomass — and to engineer resilient biocatalysts.
Research focus
- Redox chemistry and reaction pathways of copper and flavin enzymes
- Spectroscopic probes (EPR, UV-Vis) for enzyme intermediates and oxygen activation
- Computational workflows integrating quantum-chemical and molecular simulations with experiment
- AI-driven enzyme engineering on HPC infrastructure
Highlights
- Principal Investigator on the FRIPRO-funded COOFIX programme and co-PI on the ERC Synergy grant CUBE.
- Builds a multidisciplinary team spanning automation, spectroscopy, structural biology, and computational chemistry.
news
| Jan 13, 2026 | Our study on how redox robustness has shaped LPMO evolution is now published in PNAS (doi:10.1073/pnas.2521617123). Led by Iván Ayuso-Fernández with contributions from across the team and edited by Harry Gray at Caltech. |
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| Aug 05, 2025 | New publication out in Biochemistry detailing the activity of a cryptic Pseudomonas aeruginosa prophage endolysin (doi:10.1021/acs.biochem.5c00142). Great work by Per Kristian Thorén Edvardsen, Andrea Nikoline Englund, and collaborators across KBM and beyond. |
| Jul 01, 2025 | Our structure–function analysis of an understudied LPMO type with unique redox properties and substrate specificity is now published in ACS Catalysis (2025). Great work by Kelsi Hall and the team. |
| May 01, 2025 | New paper in FEBS Letters revealing how cyanide and buffer ions differentially inhibit LPMOs, shedding light on functional variation across the enzyme family. |
| Feb 07, 2025 | Åsmund shared recent spectroscopy results and computational insights during the Hylleraas Centre seminar in Oslo, highlighting how experiments guide our understanding of LPMO redox chemistry. (Source: Hylleraas Centre event listing.) |
selected publications
- Biophys. J.The rotamer of the second-sphere histidine in AA9 lytic polysaccharide monooxygenase is pH dependentBiophysical Journal, 2024
- ACS Catal.Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate SpecificityACS Catalysis, 2025
- Nat. Commun.Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO)Nature Communications, 2024