FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern

Laura Nekiunaite, Dejan M. Petrović, Bjørge Westereng, Gustav Vaaje-Kolstad, Maher Abou Hachem, Anikó Várnai, Vincent G.H. Eijsink

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    Abstract

    Lytic polysaccharide monooxygenases (LPMOs) are important for the enzymatic conversion of biomass and seem to play a key role in degradation of the plant cell wall. In this study, we characterize an LPMO from the fungal plant pathogen Fusarium graminearum (FgLPMO9A) that catalyzes the mixed C1/C4 oxidative cleavage of cellulose and xyloglucan, but is inactive towards other (1,4)-linked β-glucans. Our findings indicate that FgLPMO9A has unprecedented broad specificity on xyloglucan, cleaving any glycosidic bond in the β-glucan main chain, regardless of xylosyl substitutions. Interestingly, we found that when incubated with a mixture of xyloglucan and cellulose, FgLPMO9A efficiently attacks the xyloglucan, whereas cellulose conversion is inhibited. This suggests that removal of hemicellulose may be the true function of this LPMO during biomass conversion.
    Original languageEnglish
    JournalF E B S Letters
    Volume590
    Issue number19
    Pages (from-to)3346-3356
    Number of pages11
    ISSN0014-5793
    DOIs
    Publication statusPublished - 2016

    Keywords

    • AA9
    • Cellulose
    • Fusarium graminearum
    • Lytic polysaccharide monooxygenase
    • Xyloglucan

    Cite this

    Nekiunaite, L., Petrović, D. M., Westereng, B., Vaaje-Kolstad, G., Abou Hachem, M., Várnai, A., & Eijsink, V. G. H. (2016). FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern. F E B S Letters, 590(19), 3346-3356. https://doi.org/10.1002/1873-3468.12385
    Nekiunaite, Laura ; Petrović, Dejan M. ; Westereng, Bjørge ; Vaaje-Kolstad, Gustav ; Abou Hachem, Maher ; Várnai, Anikó ; Eijsink, Vincent G.H. / FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern. In: F E B S Letters. 2016 ; Vol. 590, No. 19. pp. 3346-3356.
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    title = "FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern",
    abstract = "Lytic polysaccharide monooxygenases (LPMOs) are important for the enzymatic conversion of biomass and seem to play a key role in degradation of the plant cell wall. In this study, we characterize an LPMO from the fungal plant pathogen Fusarium graminearum (FgLPMO9A) that catalyzes the mixed C1/C4 oxidative cleavage of cellulose and xyloglucan, but is inactive towards other (1,4)-linked β-glucans. Our findings indicate that FgLPMO9A has unprecedented broad specificity on xyloglucan, cleaving any glycosidic bond in the β-glucan main chain, regardless of xylosyl substitutions. Interestingly, we found that when incubated with a mixture of xyloglucan and cellulose, FgLPMO9A efficiently attacks the xyloglucan, whereas cellulose conversion is inhibited. This suggests that removal of hemicellulose may be the true function of this LPMO during biomass conversion.",
    keywords = "AA9, Cellulose, Fusarium graminearum, Lytic polysaccharide monooxygenase, Xyloglucan",
    author = "Laura Nekiunaite and Petrović, {Dejan M.} and Bj{\o}rge Westereng and Gustav Vaaje-Kolstad and {Abou Hachem}, Maher and Anik{\'o} V{\'a}rnai and Eijsink, {Vincent G.H.}",
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    doi = "10.1002/1873-3468.12385",
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    Nekiunaite, L, Petrović, DM, Westereng, B, Vaaje-Kolstad, G, Abou Hachem, M, Várnai, A & Eijsink, VGH 2016, 'FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern', F E B S Letters, vol. 590, no. 19, pp. 3346-3356. https://doi.org/10.1002/1873-3468.12385

    FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern. / Nekiunaite, Laura; Petrović, Dejan M.; Westereng, Bjørge; Vaaje-Kolstad, Gustav; Abou Hachem, Maher ; Várnai, Anikó; Eijsink, Vincent G.H.

    In: F E B S Letters, Vol. 590, No. 19, 2016, p. 3346-3356.

    Research output: Contribution to journalLetterResearchpeer-review

    TY - JOUR

    T1 - FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern

    AU - Nekiunaite, Laura

    AU - Petrović, Dejan M.

    AU - Westereng, Bjørge

    AU - Vaaje-Kolstad, Gustav

    AU - Abou Hachem, Maher

    AU - Várnai, Anikó

    AU - Eijsink, Vincent G.H.

    PY - 2016

    Y1 - 2016

    N2 - Lytic polysaccharide monooxygenases (LPMOs) are important for the enzymatic conversion of biomass and seem to play a key role in degradation of the plant cell wall. In this study, we characterize an LPMO from the fungal plant pathogen Fusarium graminearum (FgLPMO9A) that catalyzes the mixed C1/C4 oxidative cleavage of cellulose and xyloglucan, but is inactive towards other (1,4)-linked β-glucans. Our findings indicate that FgLPMO9A has unprecedented broad specificity on xyloglucan, cleaving any glycosidic bond in the β-glucan main chain, regardless of xylosyl substitutions. Interestingly, we found that when incubated with a mixture of xyloglucan and cellulose, FgLPMO9A efficiently attacks the xyloglucan, whereas cellulose conversion is inhibited. This suggests that removal of hemicellulose may be the true function of this LPMO during biomass conversion.

    AB - Lytic polysaccharide monooxygenases (LPMOs) are important for the enzymatic conversion of biomass and seem to play a key role in degradation of the plant cell wall. In this study, we characterize an LPMO from the fungal plant pathogen Fusarium graminearum (FgLPMO9A) that catalyzes the mixed C1/C4 oxidative cleavage of cellulose and xyloglucan, but is inactive towards other (1,4)-linked β-glucans. Our findings indicate that FgLPMO9A has unprecedented broad specificity on xyloglucan, cleaving any glycosidic bond in the β-glucan main chain, regardless of xylosyl substitutions. Interestingly, we found that when incubated with a mixture of xyloglucan and cellulose, FgLPMO9A efficiently attacks the xyloglucan, whereas cellulose conversion is inhibited. This suggests that removal of hemicellulose may be the true function of this LPMO during biomass conversion.

    KW - AA9

    KW - Cellulose

    KW - Fusarium graminearum

    KW - Lytic polysaccharide monooxygenase

    KW - Xyloglucan

    U2 - 10.1002/1873-3468.12385

    DO - 10.1002/1873-3468.12385

    M3 - Letter

    VL - 590

    SP - 3346

    EP - 3356

    JO - F E B S Letters

    JF - F E B S Letters

    SN - 0014-5793

    IS - 19

    ER -