Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation
Lytic polysaccharide monooxygenase (LPMO) could oxidize and cleavage the glycosidic bonds of polysaccharides in lignocellulose, thereby promoting the hydrolysis of polysaccharide substrates by glycoside hydrolases and significantly improving the saccharification efficiency of lignocellulose. Brown-r...
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MDPI AG
2023-05-01
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| Series: | Fermentation |
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| Online Access: | https://www.mdpi.com/2311-5637/9/6/506 |
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| author | Fei Li Yang Liu Honglu Zhao Xuan Liu Hongbo Yu |
| author_facet | Fei Li Yang Liu Honglu Zhao Xuan Liu Hongbo Yu |
| author_sort | Fei Li |
| collection | DOAJ |
| description | Lytic polysaccharide monooxygenase (LPMO) could oxidize and cleavage the glycosidic bonds of polysaccharides in lignocellulose, thereby promoting the hydrolysis of polysaccharide substrates by glycoside hydrolases and significantly improving the saccharification efficiency of lignocellulose. Brown-rot fungi are typical degraders of lignocellulose and contain multiple LPMO genes of the AA14 family and AA9 family, however, the AA14 LPMO from brown-rot fungi was rarely reported. Herein, the transcriptomic analysis of <i>Serpula lacrymans</i> incubated in the presence of pine exhibited that an AA14 LPMO (<i>Sl</i>LPMO14A) was significantly upregulated and there were redox interactions between LPMOs and other enzymes (AA3, AA6, and hemicellulose degrading enzyme), indicating that <i>Sl</i>LPMO14A may be involved in the degradation of polysaccharides. Enzymatic profiling of <i>Sl</i>LPMO14A showed the optimal pH of 8.0 and temperature of 50 °C and it had higher reaction activity in the presence of 40% glycerol and acetonitrile. <i>Sl</i>LPMO14A could significantly improve the saccharification of pine and xylan-coated cellulose substrate to release glucose and xylose by cellulase and xylanase by disturbing the surface structure of lignocellulose based on environmental scanning electron microscope and atomic force microscopy analysis. |
| first_indexed | 2024-03-11T02:29:35Z |
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| institution | Directory Open Access Journal |
| issn | 2311-5637 |
| language | English |
| last_indexed | 2024-03-11T02:29:35Z |
| publishDate | 2023-05-01 |
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| spelling | doaj.art-3e710e587664406eab7bdc336b96eca52023-11-18T10:20:42ZengMDPI AGFermentation2311-56372023-05-019650610.3390/fermentation9060506Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose DegradationFei Li0Yang Liu1Honglu Zhao2Xuan Liu3Hongbo Yu4Department of Bioengineering, School of Chemistry and Chemical Engineering, Wuhan University of Science and Technology, Wuhan 430081, ChinaDepartment of Biotechnology, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, ChinaDepartment of Biotechnology, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, ChinaDepartment of Biotechnology, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, ChinaDepartment of Biotechnology, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, ChinaLytic polysaccharide monooxygenase (LPMO) could oxidize and cleavage the glycosidic bonds of polysaccharides in lignocellulose, thereby promoting the hydrolysis of polysaccharide substrates by glycoside hydrolases and significantly improving the saccharification efficiency of lignocellulose. Brown-rot fungi are typical degraders of lignocellulose and contain multiple LPMO genes of the AA14 family and AA9 family, however, the AA14 LPMO from brown-rot fungi was rarely reported. Herein, the transcriptomic analysis of <i>Serpula lacrymans</i> incubated in the presence of pine exhibited that an AA14 LPMO (<i>Sl</i>LPMO14A) was significantly upregulated and there were redox interactions between LPMOs and other enzymes (AA3, AA6, and hemicellulose degrading enzyme), indicating that <i>Sl</i>LPMO14A may be involved in the degradation of polysaccharides. Enzymatic profiling of <i>Sl</i>LPMO14A showed the optimal pH of 8.0 and temperature of 50 °C and it had higher reaction activity in the presence of 40% glycerol and acetonitrile. <i>Sl</i>LPMO14A could significantly improve the saccharification of pine and xylan-coated cellulose substrate to release glucose and xylose by cellulase and xylanase by disturbing the surface structure of lignocellulose based on environmental scanning electron microscope and atomic force microscopy analysis.https://www.mdpi.com/2311-5637/9/6/506LPMO<i>Serpula lacrymans</i>lignocellulose degradationsaccharification |
| spellingShingle | Fei Li Yang Liu Honglu Zhao Xuan Liu Hongbo Yu Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation Fermentation LPMO <i>Serpula lacrymans</i> lignocellulose degradation saccharification |
| title | Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation |
| title_full | Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation |
| title_fullStr | Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation |
| title_full_unstemmed | Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation |
| title_short | Lytic Polysaccharide Monooxygenases from <i>Serpula lacrymans</i> as Enzyme Cocktail Additive for Efficient Lignocellulose Degradation |
| title_sort | lytic polysaccharide monooxygenases from i serpula lacrymans i as enzyme cocktail additive for efficient lignocellulose degradation |
| topic | LPMO <i>Serpula lacrymans</i> lignocellulose degradation saccharification |
| url | https://www.mdpi.com/2311-5637/9/6/506 |
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