Differential activity of lytic polysaccharide monooxygenases on celluloses of different crystallinity. Effectiveness in the sustainable production of cellulose nanofibrils.

  title={Differential activity of lytic polysaccharide monooxygenases on celluloses of different crystallinity. Effectiveness in the sustainable production of cellulose nanofibrils.},
  author={Susana V. Valenzuela and Cristina Valls and Viviane Schink and D. S{\'a}nchez and M. B. Roncero and P. D{\'i}az and Josefina Mart{\'i}nez and F. Pastor},
  journal={Carbohydrate polymers},
A series of cellulosic substrates has been produced, treated with lytic polysaccharide monooxygenase (LPMO) from Streptomyces ambofaciens (SamLPMO10C), and analyzed by high performance anion exchange chromatography (HPAEC) with pulsed amperometric detection (PAD). The activity of the bacterial LPMO showed high variability depending on the origin and degree of crystallinity of the substrate. Additionally, we tested the effectiveness of SamLPMO10C in the nanofibrillation of flax, a high… Expand
Lytic polysaccharide monooxygenases (LPMOs) facilitate cellulose nanofibrils production
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A novel AA10 from Paenibacillus curdlanolyticus and its synergistic action on crystalline and complex polysaccharides
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Light-stimulated T. thermophilus two-domain LPMO9H: Low-resolution SAXS model and synergy with cellulases.
Lytic polysaccharide monooxygenases (LPMOs), monocopper enzymes that oxidatively cleave recalcitrant polysaccharides, have important biotechnological applications. Thermothelomyces thermophilus is aExpand
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A Thermostable Aspergillus fumigatus GH7 Endoglucanase Over-Expressed in Pichia pastoris Stimulates Lignocellulosic Biomass Hydrolysis.
In the context of avoiding the use of non-renewable energy sources, employing lignocellulosic biomass for ethanol production remains a challenge. Cellulases play an important role in this scenario:Expand
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Comparison of C4-oxidizing and C1/C4-oxidizing AA9 LPMOs in substrate adsorption, H2O2-driven activity and synergy with cellulase on celluloses of different crystallinity.
  • Kaixiang Chen, Xi Zhang, Liangkun Long, Shaojun Ding
  • Chemistry, Medicine
  • Carbohydrate polymers
  • 2021
Two types of AA9 LPMOs with different modularities and regioselectivities varied in cellulose adsorption, H2O2-driven activity and synergy with cellulase on celluloses of different crystallinity which could complement each other in lignocellulose degradation. Expand


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C1 and C4 oxidizing types of LPMO from Neurospora crassa bind to nanocrystalline cellulose with high preference for the very same substrate surfaces that are used by a processive cellulase to move along during hydrolytic cellulose degradation. Expand
Enzyme mediated nanofibrillation of cellulose by the synergistic actions of an endoglucanase, lytic polysaccharide monooxygenase (LPMO) and xylanase
The combination of endoglucanase, LPMO and xylanases was shown to facilitate nan ofibrillation, potentially reducing the need for mechanical refining while resulting in a pulp with a more uniform nanofibril composition. Expand
Efficient separation of oxidized cello-oligosaccharides generated by cellulose degrading lytic polysaccharide monooxygenases.
An evaluation of HPLC-based analytical tools for the simultaneous analysis of native and oxidized cello-oligosaccharides, which are products of enzymatic cellulose degradation, found HPAEC with pulsed amperometric detection (PAD) was superior for analysis of oxidized oligosac charides, combining the best separation with superior sensitivity. Expand
Analyzing Activities of Lytic Polysaccharide Monooxygenases by Liquid Chromatography and Mass Spectrometry.
The methods described constitute a suite of techniques for analyzing oxidized carbohydrate products, which can be applied to LPMOs as well as other carbohydrate-active redox enzymes. Expand
Fast purification method of functional LPMOs from Streptomyces ambofaciens by affinity adsorption.
The activity of SamLPMO10C expands the potential of the high valued LPMOs in lignocellulosic biomass valorization, reaffirming their promising role in cellulose deconstruction. Expand
An Oxidative Enzyme Boosting the Enzymatic Conversion of Recalcitrant Polysaccharides
An enzyme is described that acts on the surface of crystalline chitin, where it introduces chain breaks and generates oxidized chain ends, thus promoting further degradation by chit inases, demonstrating the existence of a hitherto unknown enzyme activity. Expand
Multifunctional cellulolytic auxiliary activity protein HcAA10-2 from Hahella chejuensis enhances enzymatic hydrolysis of crystalline cellulose
Results suggest that HcAA10-2 is a novel multifunctional modular AA10 protein possessing amorphogenesis, weak endoglucanase, and oxidative cleavage activities useful for efficient degradation of crystalline cellulose. Expand
Lytic polysaccharide monooxygenases disrupt the cellulose fibers structure
This work provides the first evidence of the direct oxidative action of LPMOs with the mechanical weakening of the cellulose ultrastructure. Expand
Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases.
In nature, polysaccharide glycosidic bonds are cleaved by hydrolytic enzymes for a vast array of biological functions. Recently, a new class of enzymes that utilize an oxidative mechanism to cleaveExpand
Discovery and industrial applications of lytic polysaccharide mono-oxygenases.
  • K. Johansen
  • Biology, Medicine
  • Biochemical Society transactions
  • 2016
LPMOs are widespread in both the fungal and the bacterial kingdoms, although the range of action of these enzymes remains to be elucidated, and based on the high abundance of LPMOs expressed by microbes involved in the decomposition of organic matter, the importance of L PMOs in the natural carbon-cycle is predicted to be significant. Expand