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Fg LPMO 9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern
Author(s) -
Nekiunaite Laura,
Petrović Dejan M.,
Westereng Bjørge,
VaajeKolstad Gustav,
Hachem Maher Abou,
Várnai Anikó,
Eijsink Vincent G.H.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12385
Subject(s) - xyloglucan , cellulose , polysaccharide , hemicellulose , glycosidic bond , glucan , chemistry , cell wall , biochemistry , enzyme
Lytic polysaccharide monooxygenases ( LPMO s) 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 LPMO 9A) 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 LPMO 9A 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 LPMO 9A 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.