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

• Published in: Applied Microbiology and Biotechnology Vol. 105; no. 1; pp. 197 - 210
• Main Authors: Bunterngsook, Benjarat, Mhuantong, Wuttichai, Kanokratana, Pattanop, Iseki, Yu, Watanabe, Takashi, Champreda, Verawat
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Science and Business Media LLC 01.01.2021; Springer Berlin Heidelberg; Springer; Springer Nature B.V
• Subjects: Bagasse; Biomass; Biomedical and Life Sciences; Biotechnologically Relevant Enzymes and Proteins; Biotechnology; Cellooligosaccharides; Cellulase; Cellulose; Chaetomium; Chaetomium thermophilum; endo-1,4-beta-glucanase; Enzymes; Filter paper; Genetic aspects; genomic libraries; glucose; Glycosidases; Glycoside hydrolase; glycosides; Homology; Hydrolase; hydrolysis; Identification and classification; Komagataella pastoris; Libraries; Life Sciences; Metagenome; Metagenomics; microbial communities; Microbial Genetics and Genomics; Microbiology; Microorganisms; Mixed Function Oxygenases; Mixed Function Oxygenases - genetics; Monooxygenase; Oxidases; Physiological aspects; Polysaccharides; protein content; Proteins; Saccharification; Saccharomycetales; Substrates; Sugar; Sugarcane; sugarcane bagasse; Synergism; Synergistic effect; Thermophilic microorganisms; Thailand; Saccharification; Biorefinery; Synergy; Lignocellulose; Lytic polysaccharide monooxygenase

Lytic polysaccharide monooxygenases (LPMOs) are auxiliary enzymes catalyzing oxidative cleavages of cellulose chains in crystalline regions, resulting in their increasing accessibility to the hydrolytic enzyme counterparts and hence higher released sugars from biomass saccharification. In this study...