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Background  Lytic polysaccharide monooxygenases (LPMOs) opened a new horizon for biomass deconstruction. They use a redox mechanism not yet fully understood and the range of substrates initially envisaged to be the crystalline polysaccharides is steadily expanding to non-crystalline ones.    Results  The enzyme  Kp LPMO10A from the actinomycete  Kitasatospora papulosa  was cloned and overexpressed in  Escherichia coli  cells in the functional form with native N-terminal. The enzyme can release oxidized species from chitin (C1-type oxidation) and cellulose (C1/C4-type oxidation) similarly to other AA10 members from clade II (subclade A). Interestingly,  Kp LPMO10A also cleaves isolated xylan (not complexed with cellulose, C4-type oxidation), a rare activity among LPMOs not described yet for the AA10 family. The synergistic effect of  Kp LPMO10A with Celluclast ®  and an endo-β-1,4-xylanase also supports this finding. The crystallographic elucidation of  Kp LPMO10A at 1.6 Å resolution along with extensive structural analyses did not indicate any evident difference with other characterized AA10 LPMOs at the catalytic interface, tempting us to suggest that these enzymes might also be active on xylan or that the ability to attack both crystalline and non-crystalline substrates involves yet obscure mechanisms of substrate recognition and binding.    Conclusions  This work expands the spectrum of substrates recognized by AA10 family, opening a new perspective for the understanding of the synergistic effect of these enzymes with canonical glycoside hydrolases to deconstruct ligno(hemi)cellulosic biomass.    Electronic supplementary material  The online version of this article (10.1186/s13068-019-1449-0) contains supplementary material, which is available to authorized users.

An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification