id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
10_1101-2020_04_24_059154	Hossain, Musaddique	Biochemical, structural insights of newly isolated AA16 family of Lytic Polysaccharide Monooxygenase (LPMO) from <em>Aspergillus fumigatus</em> and investigation of its synergistic effect using biomass	2021	30	.pdf	application/pdf	9146	1051	58	newly isolated AA16 family of Lytic Polysaccharide Monooxygenase (LPMO) from 9 study, we have biochemically and functionally characterized the new AA16 family of LPMO 48 characterization, biomass degradation activity of AfLPMO16, and cellulase cocktail 51 Keywords: A.fumigatus, Auxiliary activity, Cloning, Kinetics, LPMO, Lignocelluloses, 55 (unnamed domain) and later identified as C1-oxidizing LPMO active on cellulose [21]. The AfLPMO16 contains 19 amino acids long N-terminal signal peptide before His1 catalytic 147 interaction study suggests that the AfLPMO16 may also bind to cellulose [52]. AfLPMO16 showed efficient depolymerization activity on both CMC and PASC (Fig. 6a & 231 0.04 mg/ml to 0.06 mg/ml, reducing sugar quantified for AfLPMO16 treated biomass (Fig. 281 activity two-fold compared to the only cellulase treated biomass (Fig. 7c). 7c), where the only AfLPMO16 and only cellulase treated biomass hydrolysis activity is low 335 Biomass and cellulose hydrolysis by cellulase and AfLPMO16 429 	./cache/10_1101-2020_04_24_059154.pdf	./txt/10_1101-2020_04_24_059154.txt