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	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	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	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	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