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 Daniel Alberto S{\'a}nchez and Maria Blanca Roncero and Pilar D{\'i}az and Josefina Mart{\'i}nez and F. I. Javier Pastor},
  journal={Carbohydrate polymers},

Lytic polysaccharide monooxygenases (LPMOs) facilitate cellulose nanofibrils production

This study demonstrates the potential use of LPMOs as a pretreatment in the NFC production process to facilitate disruption of wood cellulose fibers as a strategy to produce nanofibrillated cellulose (NFC).

Influence of the carbohydrate-binding module on the activity of a fungal AA9 lytic polysaccharide monooxygenase on cellulosic substrates

The role of the CBM from family 1 (CBM1) appended to the LPMO9H from Podospora anserina is probed to provide insights into the mechanism of action of fungal LPMOs on cellulose to produce nanocelluloses and biofuels.

Oxidized Product Profiles of AA9 Lytic Polysaccharide Monooxygenases Depend on the Type of Cellulose

Lytic polysaccharide monooxygenases (LPMOs) are essential for enzymatic conversion of lignocellulose-rich biomass in the context of biofuels and platform chemicals production. Considerable insight

Identification and characterization of a novel AA9-type lytic polysaccharide monooxygenase from a bagasse metagenome

The enzyme represented the first characterized LPMO from environmental metagenome and a potent auxiliary component for biomass saccharification and showed strong synergism to Accellerase on bagasse hydrolysis.

Two C1-oxidizing AA9 lytic polysaccharide monooxygenases from Sordaria brevicollis differ in thermostability, activity, and synergy with cellulase.

On account of its excellent thermostability and boosting effect on the enzymatic hydrolysis of delignified wheat straw, SbLPMO9A may have high application potential in biorefineries for lignocellulosic biomass.

A novel AA10 from Paenibacillus curdlanolyticus and its synergistic action on crystalline and complex polysaccharides

It is suggested that PcAA10A is a unique LPMO capable of cleaving and enhancing lignocellulosic biomass degradation, making it a good candidate for biotechnological applications.

Assessing the enzymatic effects of cellulases and LPMO in improving mechanical fibrillation of cotton linters

The combined enzymatic treatment with LPMO and cellulases boosted mechanical fibrillation of cotton linters, improving the NFC production and providing bioproducts with high transparency and high barrier properties.



Single-molecule study of oxidative enzymatic deconstruction of cellulose

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.

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.

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.

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.

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.

Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases.

Molecular simulation is used to examine the effect of oxidation on the structure of crystalline cellulose and suggests that oxidation of recalcitrant polysaccharides by LPMOs accelerates degradation not only by increasing the concentration of chain termini but also by reducing decrystallization work, and that product inhibition may be somewhat reduced as a result.

Discovery and industrial applications of lytic polysaccharide mono-oxygenases.

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.