1.14.99.54	analysis	a fast, robust, and sensitive spectrophotometric activity assay based on a peroxidase activity of LPMO, using 2,6-dimethoxyphenol and H2O2. The high molar absorption coefficient of the formed Product coerulignone displays a high molar absorption coefficinet that makes the assay sensitive and allows reliable activity measurements of LPMO in concentrations of approx. 0.5-50 mg/l	744556	
1.14.99.54	analysis	assay based on adsorption of the fluorescent dye SYTO-62, adapted to identify and localize LPMO-catalyzed formation of carboxyl groups on a cellulose surface model substrate which provides amorphous and crystalline regions alternating on a nano-flat cellulose surface	-, 740733	
1.14.99.54	degradation	cellulose conversion by cellobiohydrolase Cel7A from Trichoderma longibrachiatum alone is enhanced from 46 to 54% by the addition of isoform AA9A. Conversion by a mixture of Cel7A, endoglucanase, and beta-glucosidase is increased from 79 to 87% using pretreated bacterial microcrystalline cellulose with AA9A for 72 h. Individual AA9A molecules exhibit intermittent random movement along, across, and penetrating into the ribbon-like microfibril structure of bacterial microcrystalline cellulose, concomitant with the release of a small amount of oxidized sugars and the splitting of large cellulose ribbons into fibrils with smaller diameters	744555	
1.14.99.54	synthesis	construction of a cassette vector containing the XylS/Pm system that can easily be used for exchanging LPMO coding genes with or without signal sequences. The cassette reliably produces mature (translocated) LPMOs under controlled conditions. The signal sequence of LPMO10A from Serratia marcescens gives highest levels of recombinant protein production and translocation	744631	
1.14.99.54	degradation	design of dockerin-fused lytic polysaccharide monooxygenases. The resulting chimeras exhibit activity levels on microcrystalline cellulose similar to that of the wild-type enzymes. The dockerin moieties of the chimeras are functional and specifically bind to their corresponding cohesin partner. The chimeric lytic polysaccharide monooxygenases are able to self-assemble in designer cellulosomes alongside an endo- and an exo-cellulase also converted to the cellulosomal mode. The resulting complexes show a 1.7fold increase in the release of soluble sugars from cellulose, compared with the free enzymes, and a 2.6fold enhancement compared with free cellulases without lytic polysaccharide monooxygenase enhancement	739541	
1.14.99.54	analysis	development of a beta-glucosidase-assisted method to quantify the release of C1-oxidized glucooligosaccharides from cellulose	744131	
1.14.99.54	analysis	feeding the dissolved reagents into the reaction system during measurements with obtaining a simultaneous response in the oxygen consumption rate allows in situ monitoring the LPMO inhibition and activation by EDTA and Cu2+ ions as well as studying other effects on the enzymatic reaction	744633	
1.14.99.54	degradation	in combination with endoglucanase and beta-glucosidase, Cel61A shows the ability to release more than 36% of the pretreated soy spent flake glucose	744632	
1.14.99.54	degradation	in combination with endoglucanase and beta-glucosidase, Pte6 shows the ability to release more than 36% of the pretreated soy spent flake glucose	744632	
1.14.99.54	degradation	in presence of a Trichoderma reesei CL847 cocktail composed of mainly cellulases and xylanases, a boost of glucose release from poplar and pine is observed upon addition of AA14B enzyme to the cocktail	745847	
1.14.99.54	degradation	in presence of a Trichoderma reesei CL847 cocktail composed of mainly cellulases and xylanases, a boost of glucose release from poplar and pine is observed upon addition of AA14B enzyme to the cocktail. Addition of AA14A to a GH11 xylanase increases the release of xylooligomers from birchwood cellulosic fibers by 40%	745847	
1.14.99.54	degradation	In the presence of an electron source, LPMO increases the activity of a commercial cellulase on filter paper, and the xylanase activity of xylanase Xyn10A on beechwood xylan. Mixtures of 60% Celluclast 1.5 L, 20% Xyn10A and 20% LPMO increase the total reducing sugar production from pretreated wheat straw by 54%, while the conversions of glucan to glucose and xylan to xylose are increased by 40 and 57%, respectively	-, 744804	
1.14.99.54	degradation	lytic polysaccharide monooxygenase is able to cleave cellulose acetates with a degree of acetylation of up to 1.4	744639	
1.14.99.54	degradation	oxidative activity of Cel61A displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose, by 27%	744815	
1.14.99.54	degradation	the intrinsic physicochemical characteristics of Kraft pulp fibers (e.g. cellulose accessibility/degree of polymerization/crystallinity/charge) are positively enhanced by the synergistic cooperation of endoglucanase, LPMO and xylanase. LPMO addition results in the oxidative cleavage of the pulps, increasing the negative charge on the cellulose fibers, although gross fiber properties (fiber length, width and morphology) are relatively unchanged. This improves cellulose nanofibrilliation while stabilizing the nanofibril suspension, without sacrificing nanocellulose thermostability	746487	
1.14.99.54	degradation	treatment with CelS2 reduces nonproductive binding of cellobiohydrolase onto cellulose surface	-, 740287