TY - JOUR
T1 - Light-stimulated T. thermophilus two-domain LPMO9H
T2 - Low-resolution SAXS model and synergy with cellulases
AU - Higasi, Paula M. R.
AU - Velasco, Josman A.
AU - Pellegrini, Vanessa O. A.
AU - de Araujo, Evandro A.
AU - Franca, Bruno Alves
AU - Keller, Malene B.
AU - Labate, Carlos A.
AU - Blossom, Benedikt M.
AU - Segato, Fernando
AU - Polikarpov, Igor
PY - 2021
Y1 - 2021
N2 - Lytic polysaccharide monooxygenases (LPMOs), monocopper enzymes that oxidatively cleave recalcitrant polysaccharides, have important biotechnological applications. Thermothelomyces thermophilus is a rich source of biomass-active enzymes, including many members from auxiliary activities family 9 LPMOs. Here, we report biochemical and structural characterization of recombinant TtLPMO9H which oxidizes cellulose at the C1 and C4 positions and shows enhanced activity in light-driven catalysis assays. TtLPMO9H also shows activity against xyloglucan. The addition of TtLPMO9H to endoglucanases from four different glucoside hydrolase families (GH5, GH12, GH45 and GH7) revealed that the product formation was remarkably increased when TtLPMO9H was combined with GH7 endoglucanase. Finally, we determind the first low resolution small-angle X-ray scattering model of the two-domain TtLPMO9H in solution that shows relative positions of its two functional domains and a conformation of the linker peptide, which can be relevant for the catalytic oxidation of cellulose and xyloglucan.
AB - Lytic polysaccharide monooxygenases (LPMOs), monocopper enzymes that oxidatively cleave recalcitrant polysaccharides, have important biotechnological applications. Thermothelomyces thermophilus is a rich source of biomass-active enzymes, including many members from auxiliary activities family 9 LPMOs. Here, we report biochemical and structural characterization of recombinant TtLPMO9H which oxidizes cellulose at the C1 and C4 positions and shows enhanced activity in light-driven catalysis assays. TtLPMO9H also shows activity against xyloglucan. The addition of TtLPMO9H to endoglucanases from four different glucoside hydrolase families (GH5, GH12, GH45 and GH7) revealed that the product formation was remarkably increased when TtLPMO9H was combined with GH7 endoglucanase. Finally, we determind the first low resolution small-angle X-ray scattering model of the two-domain TtLPMO9H in solution that shows relative positions of its two functional domains and a conformation of the linker peptide, which can be relevant for the catalytic oxidation of cellulose and xyloglucan.
KW - Cellulose
KW - Lytic polysaccharide monooxygenase
KW - CAZymes
U2 - 10.1016/j.carbpol.2021.117814
DO - 10.1016/j.carbpol.2021.117814
M3 - Journal article
C2 - 33712158
SN - 0144-8617
VL - 260
JO - Carbohydrate Polymers
JF - Carbohydrate Polymers
M1 - 117814
ER -