TY - JOUR
T1 - Investigating lytic polysaccharide monooxygenase-assisted wood cell wall degradation with microsensors
AU - Chang, Hucheng
AU - Gacias Amengual, Neus
AU - Botz, Alexander
AU - Schwaiger, Lorenz
AU - Kracher, Daniel
AU - Scheiblbrandner, Stefan
AU - Csarman, Florian
AU - Ludwig, Roland
N1 - Funding Information:
We thank Wolfgang Schuhmann for valuable discussions and support in setting up the SECM and Monika Debreczeny for help with the confocal laser scanning microscope. We thank Christopher Schulz for providing the material and protocol for the polyurethane coating. This work was supported by European Research Council through European Union’s Horizon 2020 research and innovation program (ERC Consolidator Grant OXIDISE) under grant agreement no. 726396.
Publisher Copyright:
© 2022, The Author(s).
PY - 2022/12
Y1 - 2022/12
N2 - Lytic polysaccharide monooxygenase (LPMO) supports biomass hydrolysis by increasing saccharification efficiency and rate. Recent studies demonstrate that H2O2 rather than O2 is the cosubstrate of the LPMO-catalyzed depolymerization of polysaccharides. Some studies have questioned the physiological relevance of the H2O2-based mechanism for plant cell wall degradation. This study reports the localized and time-resolved determination of LPMO activity on poplar wood cell walls by measuring the H2O2 concentration in their vicinity with a piezo-controlled H2O2 microsensor. The investigated Neurospora crassa LPMO binds to the inner cell wall layer and consumes enzymatically generated H2O2. The results point towards a high catalytic efficiency of LPMO at a low H2O2 concentration that auxiliary oxidoreductases in fungal secretomes can easily generate. Measurements with a glucose microbiosensor additionally demonstrate that LPMO promotes cellobiohydrolase activity on wood cell walls and plays a synergistic role in the fungal extracellular catabolism and in industrial biomass degradation.
AB - Lytic polysaccharide monooxygenase (LPMO) supports biomass hydrolysis by increasing saccharification efficiency and rate. Recent studies demonstrate that H2O2 rather than O2 is the cosubstrate of the LPMO-catalyzed depolymerization of polysaccharides. Some studies have questioned the physiological relevance of the H2O2-based mechanism for plant cell wall degradation. This study reports the localized and time-resolved determination of LPMO activity on poplar wood cell walls by measuring the H2O2 concentration in their vicinity with a piezo-controlled H2O2 microsensor. The investigated Neurospora crassa LPMO binds to the inner cell wall layer and consumes enzymatically generated H2O2. The results point towards a high catalytic efficiency of LPMO at a low H2O2 concentration that auxiliary oxidoreductases in fungal secretomes can easily generate. Measurements with a glucose microbiosensor additionally demonstrate that LPMO promotes cellobiohydrolase activity on wood cell walls and plays a synergistic role in the fungal extracellular catabolism and in industrial biomass degradation.
UR - http://www.scopus.com/inward/record.url?scp=85140206630&partnerID=8YFLogxK
U2 - 10.1038/s41467-022-33963-w
DO - 10.1038/s41467-022-33963-w
M3 - Article
C2 - 36271009
AN - SCOPUS:85140206630
SN - 2041-1723
VL - 13
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 6258
ER -