Sophanit Mekasha

Norwegian version of this page
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Visiting address Blindernveien 31 0371 Oslo
Postal address Postboks 1066 Blindern 0316 Oslo

Publications

  • Mekasha, Sophanit & Linke, Dirk (2021). Secretion Systems in Gram-Negative Bacterial Fish Pathogens. Frontiers in Microbiology. ISSN 1664-302X. 12. doi: 10.3389/fmicb.2021.782673. Full text in Research Archive
  • Støpamo, Fredrik Gjerstad; Kjendseth, Åsmund Røhr; Mekasha, Sophanit; Petrovic, Dejan; Varnai, Aniko & Eijsink, Vincent (2021). Characterization of a lytic polysaccharide monooxygenase from Aspergillus fumigatus shows functional variation among family AA11 fungal LPMOs. Journal of Biological Chemistry. ISSN 0021-9258. 297(6), p. 1–14. doi: 10.1016/j.jbc.2021.101421.
  • Mekasha, Sophanit; Tuveng, Tina R.; Vaaje-Kolstad, Gustav & Eijsink, Vincent G.H. (2021). Chromatographic assays for the enzymatic degradation of chitin. Bio-protocol. ISSN 2331-8325. 11(9). doi: 10.21769/BioProtoc.4014.
  • Skåne, Anna; Minniti, Giusi; Loose, Jennifer Sarah Maria; Mekasha, Sophanit; Bissaro, Bastien & Mathiesen, Geir [Show all 8 contributors for this article] (2021). The Fish Pathogen Aliivibrio salmonicida LFI1238 Can Degrade and Metabolize Chitin despite Gene Disruption in the Chitinolytic Pathway. Applied and Environmental Microbiology. ISSN 0099-2240. 87(19), p. 1–25. doi: 10.1128/AEM.00529-21.
  • Askarian, Fatemeh; Uchiyama, Satoshi; Masson, Helen; Sørensen, Henrik Vinther; Golten, Ole & Bunæs, Anne Cathrine [Show all 20 contributors for this article] (2021). The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection. Nature Communications. ISSN 2041-1723. 12, p. 1–19. doi: 10.1038/s41467-021-21473-0. Full text in Research Archive
  • Mekasha, Sophanit; Tuveng, Tina Rise; Askarian, Fatemeh; Choudhary, Swati; Schmith-Dannert, Claudia & Niebisch, Axel [Show all 9 contributors for this article] (2020). A trimodular bacterial enzyme combining hydrolytic activity with oxidative glycosidic bond cleavage efficiently degrades chitin. Journal of Biological Chemistry. ISSN 0021-9258. 295(27), p. 9134–9146. doi: 10.1074/jbc.RA120.013040. Full text in Research Archive
  • Vaaje-Kolstad, Gustav; Tuveng, Tina Rise; Mekasha, Sophanit & Eijsink, Vincent (2019). Enzymes for Modification of Chitin and Chitosan. In van den Broek, Lambertus A.M. & Boeriu, Carmen G. (Ed.), Chitin and Chitosan: Properties and Applications. John Wiley & Sons. ISSN 9781119450467. p. 189–228. doi: 10.1002/9781119450467.ch8.
  • Eijsink, Vincent; Petrovic, Dejan; Forsberg, Zarah; Mekasha, Sophanit; Kjendseth, Åsmund Røhr & Varnai, Aniko [Show all 8 contributors for this article] (2019). On the functional characterization of lytic polysaccharide monooxygenases (LPMOs). Biotechnology for Biofuels. ISSN 1754-6834. 12, p. 1–16. doi: 10.1186/s13068-019-1392-0. Full text in Research Archive
  • Mutahir, Zeeshan; Mekasha, Sophanit; Loose, Jennifer Sarah Maria; Abbas, Faiza; Vaaje-Kolstad, Gustav & Eijsink, Vincent [Show all 7 contributors for this article] (2018). Characterization and synergistic action of a tetra-modular lytic polysaccharide monooxygenase from Bacillus cereus. FEBS Letters. ISSN 0014-5793. 592(15), p. 2562–2571. doi: 10.1002/1873-3468.1318.
  • Bacik, JP; Mekasha, Sophanit; Forsberg, Zarah; Kovalevsky, AY; Vaaje-Kolstad, Gustav & Eijsink, Vincentius Gerardus Henricus [Show all 11 contributors for this article] (2017). Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation. Biochemistry. ISSN 0006-2960. 56(20), p. 2529–2532. doi: 10.1021/acs.biochem.7b00019.
  • Mekasha, Sophanit; Byman, Ida Roksvåg; Lynch, Catherine; Toupalová, Hana; Andera, Ladislav & Næs, Tormod [Show all 8 contributors for this article] (2017). Development of enzyme cocktails for complete saccharification of chitin using mono-component enzymes from Serratia marcescens. Process Biochemistry. ISSN 1359-5113. 56, p. 132–138. doi: 10.1016/j.procbio.2017.02.021. Full text in Research Archive
  • Tuveng, Tina Rise; Hagen, Live Heldal; Mekasha, Sophanit; Frank, Jeremy; Arntzen, Magnus Øverlie & Vaaje-Kolstad, Gustav [Show all 7 contributors for this article] (2017). Genomic, proteomic and biochemical analysis of the chitinolytic machinery of Serratia marcescens BJL200. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1865(4), p. 414–421. doi: 10.1016/j.bbapap.2017.01.007.
  • Mekasha, Sophanit; Toupalová, Hana; Linggadjaja, Eka; Tolani, Harish A.; Andera, Ladislav & Arntzen, Magnus Øverlie [Show all 9 contributors for this article] (2016). A novel analytical method for D-glucosamine quantification and its application in the analysis of chitosan degradation by a minimal enzyme cocktail. Carbohydrate Research. ISSN 0008-6215. 433, p. 18–24. doi: 10.1016/j.carres.2016.07.003.
  • Gaber, Yasser; Mekasha, Sophanit; Vaaje-Kolstad, Gustav; Eijsink, Vincent & Fraaije, Marco W. (2016). Characterization of a chitinase from the cellulolytic actinomycete Thermobifida fusca. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1864(9), p. 1253–1259. doi: 10.1016/j.bbapap.2016.04.010.
  • Forsberg, Zarah; Nelson, Cassandra E.; Dalhus, Bjørn; Mekasha, Sophanit; Loose, Jennifer & Crouch, Lucy I. [Show all 10 contributors for this article] (2016). Structural and functional analysis of a lytic polysaccharide monooxygenase important for efficient utilization of chitin in Cellvibrio japonicus. Journal of Biological Chemistry. ISSN 0021-9258. 291(14), p. 7300–7312. doi: 10.1074/jbc.M115.700161. Full text in Research Archive
  • Mekasha, Sophanit; Forsberg, Zarah; Dalhus, Bjørn; Bacik, John-Paul; Choudhary, Swati & Schmidt-Dannert, Claudia [Show all 8 contributors for this article] (2016). Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans. FEBS Letters. ISSN 0014-5793. 590(1), p. 34–42. doi: 10.1002/1873-3468.12025.
  • Bacik, John-Paul; Mekasha, Sophanit; Forsberg, Zarah; Kovalevsky, Andrey; Nix, Jay C. & Cuneo, Matthew J. [Show all 11 contributors for this article] (2015). Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. ISSN 1744-3091. 71(11), p. 1448–1452. doi: 10.1107/S2053230X15019743.
  • Forsberg, Zarah; Røhr, Åsmund Kjendseth; Mekasha, Sophanit; Andersson, K. Kristoffer; Eijsink, Vincent & Vaaje-Kolstad, Gustav [Show all 7 contributors for this article] (2014). Comparative study of two chitin-active and two cellulose-active AA10-type lytic polysaccharide monooxygenases. Biochemistry. ISSN 0006-2960. 53, p. 1647–1656. doi: 10.1021/bi5000433.

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  • Vaaje-Kolstad, Gustav; Tuveng, Tina Rise; Mekasha, Sophanit & Eijsink, Vincent (2019). Enzymes for Modification of Chitin and Chitosan. John Wiley & Sons. ISBN 9781119450467. 39 p.

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  • Petrikonyte, Patricija; Mekasha, Sophanit & Linke, Dirk (2023). Tenacibaculum maritimum virulence factors.
  • Mekasha, Sophanit; Tøndervik, Anne & Linke, Dirk (2023). Exploring virulence factors of Tenacibaculum maritimum.
  • Petrikonyte, Patricija; Mekasha, Sophanit & Linke, Dirk (2023). T. maritimum virulence factors.
  • Mekasha, Sophanit; Haslene-Hox, Hanne; Sperstad, Sigrid Bakken; Tøndervik, Anne & Linke, Dirk (2023). Exploring virulence factors of Tenacibaculum maritimum.
  • Petrikonyte, Patricija; Mekasha, Sophanit & Linke, Dirk (2023). Tenacibaculum maritimum virulence factors.
  • Mekasha, Sophanit & Linke, Dirk (2023). Virulence factors of the bacterial fish pathogen Tenacibaculum maritimum.
  • Mekasha, Sophanit; Petrikonytė, Patricija & Linke, Dirk (2023). Virulence factors of the bacterial fish pathogen Tenacibaculum maritimum.
  • Mekasha, Sophanit & Linke, Dirk (2022). Toxins and secretion systems in Gram-negative bacterial fish pathogens.
  • Mekasha, Sophanit & Linke, Dirk (2022). Toxins and secretion systems in Gram-negative bacterial fish pathogens. The case of T. maritimum.
  • Skåne, Anna; Arntzen, Magnus Øverlie; Mekasha, Sophanit; Mathiesen, Geir & Vaaje-Kolstad, Gustav (2019). The chitinolytic potential of the fish pathogen Aliivibrio (vibrio) salmonicida LFI123.
  • Mekasha, Sophanit; Tuveng, Tina Rise; Askarian, Fatemeh; Choudhary, Swati; Schmidt-Dannert, C & Niebisch, Axel [Show all 9 contributors for this article] (2019). A powerful single tri-modular bi-catalytic LPMO10/Chi18 enzyme is responsible for the growth of J. denitrificans 20603 on chitin.
  • Skåne, Anna; Minniti, Giusi; Loose, Jennifer Sarah Maria; Mekasha, Sophanit & Vaaje-Kolstad, Gustav (2019). The chitinolytic potential of the fish pathogen Aliivibrio salmonicida.
  • Forsberg, Zarah; Bissaro, Bastien; Courtade, Gaston; Mekasha, Sophanit; Loose, Jennifer Sarah Maria & Vaaje-Kolstad, Gustav [Show all 8 contributors for this article] (2018). Modularity as a tool to harness the power of LPMOs in polysaccharide conversion.
  • Mekasha, Sophanit; Byman, Ida Roksvåg; Lynch, Catherine; Toupalová, Hana; Anděra, Ladislav & Næs, Tormod [Show all 8 contributors for this article] (2017). Development of enzyme cocktails for complete saccharification of chitin using mono-component enzymes from Serratia marcescens.
  • Forsberg, Zarah; Nelson, CE; Dalhus, Bjørn; Mekasha, Sophanit; Loose, Jennifer & Røhr, Åsmund Kjendseth [Show all 9 contributors for this article] (2016). An LPMO important for efficient chitin utilization in Cellvibrio japonicus.
  • Tuveng, Tina Rise; Forsberg, Zarah; Nelson, CE; Dalhus, Bjørn; Mekasha, Sophanit & Loose, Jennifer [Show all 11 contributors for this article] (2016). Chitin degradation by Cellvibrio japonicus.
  • Mekasha, Sophanit; Forsberg, Zarah; Dalhus, Bjørn; Choudhary, Swati; Schmith-Dannert, Claudia & Vaaje-Kolstad, Gustav [Show all 7 contributors for this article] (2015). Structural and functional characterization of a chitin-active bicatalytic lytic polysaccharide monooxygenase/ glycoside hydrolase.
  • Forsberg, Zarah; Nelson, Cassandra E.; Dalhus, Bjørn; Loose, Jennifer; Mekasha, Sophanit & Røhr, Åsmund Kjendseth [Show all 9 contributors for this article] (2015). Structural and functional analysis of a lytic polysaccharide monooxygenase that is decisive for efficient utilization of recalcitrant polysaccharides by Cellvibrio japonicas.
  • Mekasha, Sophanit (2015). Structural and Functional Characterization of a Chitin-Active Bi-Catalytic Lytic Polysaccharide Monooxygenase/Glycoside Hydrolase from Jonesia denitrificans.
  • Toupalová, Hana; Mekasha, Sophanit; Vaaje-Kolstad, Gustav; Váchová, Lenka; Sedlackova, Petra & Eijsink, Vincent [Show all 7 contributors for this article] (2014). Breaking the chitin armour: preparation and use of natural and recombinant chitin-degrading enzymes.
  • Mekasha, Sophanit; Bunæs, Anne Cathrine; Vachova, L; Sedlackova, Petra; Andera, Ladislav & Vaaje-Kolstad, Gustav [Show all 7 contributors for this article] (2014). Saccharification of alpha-chitin using the chitinolytic machinery of Serratia marcescens.
  • Mekasha, Sophanit; Nakagawa, Y.; Bunæs, Anne Cathrine; Vachova, L; Sedlackova, Petra & Andera, Ladislav [Show all 9 contributors for this article] (2014). Optimization of alpa-chitin depolymerizatioon by designer enzyme cocktails and mechanical substrate pretreatment.
  • Mekasha, Sophanit; Bunæs, Anne Cathrine; Vachova, L; Sedlackova, Petra; Andera, Ladislav & Vaaje-Kolstad, Gustav [Show all 7 contributors for this article] (2013). Saccharification of a-chitin using the chitinolytic machinery of Serratia marcescens.
  • Mekasha, Sophanit; Bunæs, Anne Cathrine; Vachova, L; Sedlackova, Petra; Andera, Ladislav & Vaaje-Kolstad, Gustav [Show all 7 contributors for this article] (2013). Saccharification of a-chitin using the chitinolytic machinery of Serratia marcescens.
  • Mekasha, Sophanit (2017). Characterization and application of enzymes for saccharification of chitin. NMBU, KBM. ISSN 978-82-575-1421-1.
  • Mekasha, Sophanit (2013). Cloning, expression, purification and characterization of lytic polysaccharide monooxygenases from Streptomyces coelicolor (A3) and Jonesia denitrifiocans. Universitetet for miljø- og biovitenskap.

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Published Feb. 18, 2021 2:56 PM - Last modified Feb. 18, 2021 2:56 PM