FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern. Issue 19 (18th September 2016)

• Record Type: Journal Article
• Authors: Nekiunaite, Laura; Petrović, Dejan M.; Westereng, Bjørge; Vaaje‐Kolstad, Gustav; Hachem, Maher Abou; Várnai, Anikó; Eijsink, Vincent G.H.
• Is Part Of: FEBS letters. Volume 590:Issue 19(2016)
• Page Start: 3346
• Page End: 3356
• Publication Date: 2016-09-18
• Subjects: AA9 -- cellulose -- Fusarium graminearum -- lytic polysaccharide monooxygenase -- xyloglucan; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12385
• Languages: English
• ISSNs: 0014-5793

Abstract

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 ( Fg LPMO9A) that catalyzes the mixed C1/C4 oxidative cleavage of cellulose and xyloglucan, but is inactive toward other (1, 4)‐linked β‐glucans. Our findings indicate that Fg LPMO9A 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, Fg LPMO9A 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. Abstract :