Oxidative cleavage of polysaccharides by a termite-derived boosts the degradation of biomass by glycoside hydrolases.

Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in lignocellulose degradation, suggesting hereto unknown enzymatic activities in their digestome. Herein, we demonstrate that an ancient redox-active enzyme encoded by the lower termite , a Cu/Zn superoxide dismutase (SOD-1), plays a previously unknown role in plant biomass degradation.

Improving cellulases hydrolytic action: An expanded role for electron donors of lytic polysaccharide monooxygenases in cellulose saccharification.

Ascorbic acid (AscA) and gallic acid (GalA) are common electron donors and their boosting effect on lytic polysaccharide monooxygenases (LPMO) has been studied extensively. However, their influence on cellulase hydrolytic action has been ignored. In this work, the effect of AscA and GalA on cellulases hydrolytic action was evaluated.

Chemistry of lignin and hemicellulose structures interacts with hydrothermal pretreatment severity and affects cellulose conversion.

Understanding of how the plant cell walls of different plant species respond to pretreatment can help improve saccharification in bioconversion processes. Here, we studied the chemical and structural modifications in lignin and hemicellulose in hydrothermally pretreated poplar and wheat straw using wet chemistry and 2D heteronuclear single quantum coherence nuclear magnetic resonance (NMR) and their effects on cellulose conversion. Increased pretreatment severity reduced the levels of β─O─4 linkages with concomitant relatively increased levels of β─5 and β─β structures in the NMR spectra.

Removal of hard COD from acidic eucalyptus kraft pulp bleach plant effluent streams using oxidoreductases.

The bleach plant of a pulp and paper (P&P) mill presents a major source of wastewater containing toxic organic matter characterized as chemical oxygen demand (COD). Due to their high oxidizing power, oxidoreductases hold promise to be a key solution for the removal of dissolved organic material. Here, four oxidoreductases from different enzyme families were selected to treat bleach plant effluents.

On the roles of AA15 lytic polysaccharide monooxygenases derived from the termite Coptotermes gestroi.

Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes which catalyze the oxidative cleavage of polysaccharides. LPMOs belonging to family 15 in the Auxiliary Activity (AA) class from the Carbohydrate-Active Enzyme database are found widespread across the Tree of Life, including viruses, algae, oomycetes and animals. Recently, two AA15s from the firebrat Thermobia domestica were reported to have oxidative activity, one towards cellulose or chitin and the other towards chitin, signalling that AA15 LPMOs from insects potentially have different biochemical functions.