HOPE
_{Harnessing the Oxidative Power of Enzymes}

HOPE – Harnessing the Oxidative Power of Enzymes was a strategic research project funded by the Novo Nordisk Foundation with the aim to address the pressing challenge of studying some of Nature’s most powerful oxidative enzymes, known as lytic polysaccharide monooxygenases or LPMOs.

These enzymes are important for converting biological material such as cellulose that is not easily degraded, into biofuels and chemicals. With the help of copper in its structure, the LPMOs can modify the cellulose fibers allowing other enzymes to access the material and release the sugar in the biomass. LPMOs are already used commercially today for converting plant waste to bioethanol.

A key element of the project involved establishing the Laboratory of Oxidative Enzymology at the Copenhagen Plant Science Center. The laboratory includes unique facilities with equipment to work under oxygen-free conditions and dedicated facilities for microbial and plant work.

The project was a partnership between The Department of Geosciences and Natural Resource Management, the Department of Plant and Environmental Sciences hosting the Copenhagen Plant Science Center, the Department of Chemistry and the Novo Nordisk Foundation Center for Protein Research at the University of Copenhagen and the Novo Nordisk Foundation Center for Biosustainability at the Technical University of Denmark.

2022

S. Banerjee, S. J. Muderspach, T. Tandrup, K. E. H. Frandsen, R. K. Singh, J. Ø. Ipsen, C. Hernandez-Rollan, M. H .H. Nørholm, M. J. Bjerrum, K. S. Johansen and L. L. Leggio (2022) Protonation state of an important histidine from high resolution structures of lytic polysaccharide monooxygenases. Biomolecules 2022, 12(2), 194; https://doi.org/10.3390/biom12020194

2021

R. Tokin, J. Ø. Ipsen, M. M. Poojary, P. E. Jensen, L. Olsson and K. S. Johansen (2021) Inhibition of LPMOs by fermented persimmon juice. Biomolecules. 2021 Dec; 11(12): 1890 10.3390/biom11121890

R. Tokin, K. E. R. Frandsen, J. Ørskov Ipsen, L. Lo Leggio, M. M. Poojary, J-G Berrin, S. Grisel, S. Brander, P. Erik Jensen and K. S. Johansen (2021) Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. New Phytologist. doi:  http://doi.org/10.1111/nph.17676 

S. Brander, S. Lausten, J. Ø. Ipsen, K. B. Falkenberg, A. B. Bertelsen, M. H. Nørholm, L. H. Østergaard and K. S. Johansen (2021) Colorimetric LPMO assay with direct implication for cellulolytic activity. Biotechnol Biofuels 14,51 doi: https://doi.org/10.1186/s13068-021-01902-4  

K.E.H. Frandsen, M. Haon, S. Grisel, B. Henrissat, L. Lo. Leggio and J-G. Berrin (2021) Identification of the molecular determinants driving the substrate specificity of fungal lytic polysaccharide monooxygenases (LPMOs), JBC, 296, 100086. doi: https://doi.org/10.1074/jbc.RA120.015545

Y.A. Theibich, S.P.A. Sauer, L. Lo. Leggio and E.D. Hedegård (2021) Estimating the accuracy of calculated electron paramagnetic resonance hyperfine couplings for a lytic polysaccharide monooxygenase. Comp. Struct. Biotech. J. 19, 555-567. doi: https://doi.org/10.1016/j.csbj.2020.12.014

Ipsen, J.Ø., Hallas-Møller, M., Brander, S., Leggio, L.L., Johansen, K.S. (2021). Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications. Biochem Soc Trans. BST20201031. doi: https://doi.org/10.1042/BST20201031

2020

Labourel, A., Frandsen, K. E. H., Zhang, F., Brouilly, N., Grisel, S., Haon, M., Ciano, L., Ropartz, D., Fanuel, M., Martin, F., Navarro, D., Rosso, M-N., Tandrup, T., Bissaro, B., Johansen, K. S., Zerva, A., Walton, P. H., Henrissat, B., Leggio, L. L., and Berrin J-G. (2020). A fungal family of lytic polysaccharide monooxygenase-like copper proteins. Nat Chem Biol 16, 345-350. doi: https://doi.org/10.1038/s41589-019-0438-8

Peciulyte, A., Xafenias, N., Galbe, M., Scott, B. R., Olsson, L., Johansen, K. S. (2020). Storage and handling of pretreated lignocellulose affects the redox chemistry during subsequent enzymatic saccharification. Bioresour. Bioprocess. 7, 64. doi: https://doi.org/10.1186/s40643-020-00353-3

Brander, S., Horvath, I., Ipsen, J.Ø., Peciulyte, A., Olsson, L., Hernández-Rollán, C., Nørholm, M. H. H., Mossin, S., Leggio, L. L., Probst, C., Thiele, D. J., and Johansen, K. S. (2020). Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace. Sci Rep 10, 16369. doi: https://doi.org/10.1038/s41598-020-73266-y

Garcia-Santamarina, S., Probst, C., Festa, R.A., Ding, C., Smith, A. D., Conklin, S. E., Brander, S., Kinch, L. N., Grishin, N. V., Franz, K. J., Riggs-Gelasco, P., Leggio, L. L., Johansen, K. S., and Thiele, D. J. (2020). A lytic polysaccharide monooxygenase-like protein functions in fungal copper import and meningitis. Nat Chem Biol 16, 337-344. doi: https://doi.org/10.1038/s41589-019-0437-9

Tokin, R., Ipsen, J. Ø., Westh, P., Johansen, K. S. (2020). The synergy between LPMOs and cellulases in enzymatic saccharification of cellulose is both enzyme- and substratedependent. Biotechnol Lett 42, 1975-1984. doi: https://doi.org/10.1007/s10529-020-02922-0

Tandrup, T., Tryfona, T., Frandsen, K. E. H., Johansen, K. S., Dupree, P., and Leggio, L. L. (2020). Oligosaccharide binding and thermostability of two related AA9 Lytic Polysaccharide Monooxygenases. Biochemistry 59 (36), 3347-3358. doi: https://doi.org/10.1021/acs.biochem.0c00312

2019

Frandsen, K. E. H, Tovborg, M., Jørgensen, C.I., Spodsberg, N., Rosso, M-N., Hemsworth, G. R., Garman, E. F., Grime, G. W., Poulsen, J-C. N., Batth, T. S., Miyauchi, S., Lipzen, A., Daum, C., Grigoriev, I. V., Johansen, K. S., Henrissat, B., Berrin, J-G., and Leggio, L. L. (2019). Insights into an unusual Auxiliary Activity 9 family member lacking the histidine brace motif of lytic polysaccharide monooxygenases. The Journal of Biological Chemistry 294, 17117-17130. doi: https://doi.org/10.1074/jbc.RA119.009223

Muderspach, S. J., Tandrup, T., Frandsen, K. E. H., Santoni, G., Poulsen, J-C. N., and Leggio, L. L. (2019). Further structural studies of the lytic polysaccharide monooxygenase AoAA13 belonging to the starch-active AA13 family. Amylase, 3 (1), 41-54. doi: https://doi.org/10.1515/amylase-2019-0004

2018

Tandrup, T., Frandsen, K. E. H., Johansen, K. S., Berrin, J.-G., and Leggio, L. L. (2018). Recent insights into lytic polysaccharide monooxygenases (LPMOs). Biochem Soc Trans 46 (6): 1431–1447. doi: https://doi.org/10.1042/BST20170549

Leggio, L.L., Weihe, C. D., Poulsen, J.-C. N., Sweeney, M., Rasmussen, F., Lin, J., De Maria, L., and Wogulis, M. (2018). Structure of a lytic polysaccharide monooxygenase from Aspergillus fumigatus and an engineered thermostable variant. Carbohydrate Research, 469, 55-59. doi: https://doi.org/10.1016/j.carres.2018.08.009

Publications by HOPE project members

This is a list of publications by members of HOPE, which are a result of other funding, but relevant to the overall objectives of HOPE.

2021

K. Mirzadeh, P.J. Shilling, R. Elfageih, H.L. Cui, M. Rennig, M.H.H. Nørholm and D.O. Daley (2020) Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region. Microbial Cell Factories, 19(1):85. https://doi.org/10.1186/s12934-020-01339-8

2018

Peciulyte, A., Samuelsson, L., Olsson, L., McFarland, K. C., Frickmann, J., Østergård, L., Halvorsen, R., Scott, B. R., and Johansen, K. S. (2018). Redox processes acidify and decarboxylate steam-pretreated lignocellulosic biomass and are modulated by LPMO and catalase. Biotechnol Biofuels 11, 165. doi: https://doi.org/10.1186/s13068-018-1159-z

Johansen, K. S. (2016). Oxidative Copper-Enzymes are the Key for Unlocking Recalcitrant Biopolymers. Doctoral dissertation.
Doctoral defence took place on Friday the 26th of January, 2018 at the University of Copenhagen, Frederiksberg, Denmark.

2017

Simmons, T. J., Frandsen, K. E. H., Ciano, L., Tryfona, T., Lenfant, N., Poulsen, J. C., Wilson, L. F. L., Tandrup, T., Tovborg, M., Schnorr, K., Johansen, K. S., Henrissat, B., Walton, P. H., Leggio, L. L., and Dupree, P. (2017). Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates. Nat commun 8, 1064. doi: https://doi.org/10.1038/s41467-017-01247-3