Enhanced lignocellulosic biomass hydrolysis by oxidative lytic polysaccharide monooxygenases (LPMOs) GH61 from Gloeophyllum trabeum |
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| Institution: | 1. Department of Wood Science and Landscape Architechture, Chonnam National University, Gwangju 500-757, Republic of Korea;2. Department of Bioenergy Science and Technology, Chonnam National University, Gwangju 500-757, Republic of Korea;1. Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway;2. Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, Uppsala, Sweden;3. Borregaard AS, Sarpsborg, Norway;1. College of Food Science and Pharmaceutical Engineering, Zaozhuang University, Zaozhuang 277160, China;2. State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China;1. Enzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, Eastern Cape, South Africa;2. Forest Products Biotechnology Group, Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, British Columbia, V6T1Z4, Canada;1. Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin 300457, PR China;2. Tianjin Key Laboratory of Industrial Microbiology, Tianjin 300457, PR China;3. College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, PR China |
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| Abstract: | Lignocellulose is a renewable resource that is extremely abundant, and the complete enzymatic hydrolysis of lignocellulose requires a cocktail containing a variety of enzyme groups that act synergistically. The hydrolysis efficiency can be improved by introducing glycoside hydrolase 61 (GH61), a new enzyme that belongs to the auxiliary activity family 9 (AA9). GH61was isolated from Gloeophyllum trabeum and cleaves the glycosidic bonds on the cellulose surface via oxidation of various carbons. In this study, we investigated the properties of GH61. GtGH61 alone did not exhibit any notable activity, but the synergistic activity of GtGH61 with xylanase (GtXyl10G) or cellulase (GtCel5B) showed efficient bioconversion rates of 56 and 174% in pretreated kenaf (Hibiscus cannabinus L.) and oak (Quercus spp.), respectively. Furthermore, the GtGH61 activity was strongly accelerated in the presence of cobalt Co2+. Enzyme cocktails (GtXyl10G, GtCel5B, and GtGH61) increased the amount of sugar released by 7 and 6% for pretreated oak and kenaf, respectively, and the addition of Co2+ stimulated bioconversion by 12 and 11% in pretreated oak and kenaf, respectively. |
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| Keywords: | GH61 AA9 Lytic polysaccharide monooxygenase Lignocellulose bioconversion Bioethanol |
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