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Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation
Even though the discovery of lytic polysaccharide monooxygenases (LPMOs) has fundamentally shifted our understanding of biomass degradation, most of the current studies focused on their roles in carbohydrate oxidation. However, no study demonstrated if LPMO could directly participate to the process...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520884/ https://www.ncbi.nlm.nih.gov/pubmed/37766973 http://dx.doi.org/10.1016/j.isci.2023.107870 |
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author | Sun, Su Li, Fei Li, Muzi Zhang, Wenqian Jiang, Zhenxiong Zhao, Honglu Pu, Yunqiao Ragauskas, Arthur J. Dai, Susie Y. Zhang, Xiaoyu Yu, Hongbo Yuan, Joshua S. Xie, Shangxian |
author_facet | Sun, Su Li, Fei Li, Muzi Zhang, Wenqian Jiang, Zhenxiong Zhao, Honglu Pu, Yunqiao Ragauskas, Arthur J. Dai, Susie Y. Zhang, Xiaoyu Yu, Hongbo Yuan, Joshua S. Xie, Shangxian |
author_sort | Sun, Su |
collection | PubMed |
description | Even though the discovery of lytic polysaccharide monooxygenases (LPMOs) has fundamentally shifted our understanding of biomass degradation, most of the current studies focused on their roles in carbohydrate oxidation. However, no study demonstrated if LPMO could directly participate to the process of lignin degradation in lignin-degrading microbes. This study showed that LPMO could synergize with lignin-degrading enzymes for efficient lignin degradation in white-rot fungi. The transcriptomics analysis of fungi Irpex lacteus and Dichomitus squalens during their lignocellulosic biomass degradation processes surprisingly highlighted that LPMOs co-regulated with lignin-degrading enzymes, indicating their more versatile roles in the redox network. Biochemical analysis further confirmed that the purified LPMO from I. lacteus CD2 could use diverse electron donors to produce H(2)O(2), drive Fenton reaction, and synergize with manganese peroxidase for lignin oxidation. The results thus indicated that LPMO might uniquely leverage the redox network toward dynamic and efficient degradation of different cell wall components. |
format | Online Article Text |
id | pubmed-10520884 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-105208842023-09-27 Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation Sun, Su Li, Fei Li, Muzi Zhang, Wenqian Jiang, Zhenxiong Zhao, Honglu Pu, Yunqiao Ragauskas, Arthur J. Dai, Susie Y. Zhang, Xiaoyu Yu, Hongbo Yuan, Joshua S. Xie, Shangxian iScience Article Even though the discovery of lytic polysaccharide monooxygenases (LPMOs) has fundamentally shifted our understanding of biomass degradation, most of the current studies focused on their roles in carbohydrate oxidation. However, no study demonstrated if LPMO could directly participate to the process of lignin degradation in lignin-degrading microbes. This study showed that LPMO could synergize with lignin-degrading enzymes for efficient lignin degradation in white-rot fungi. The transcriptomics analysis of fungi Irpex lacteus and Dichomitus squalens during their lignocellulosic biomass degradation processes surprisingly highlighted that LPMOs co-regulated with lignin-degrading enzymes, indicating their more versatile roles in the redox network. Biochemical analysis further confirmed that the purified LPMO from I. lacteus CD2 could use diverse electron donors to produce H(2)O(2), drive Fenton reaction, and synergize with manganese peroxidase for lignin oxidation. The results thus indicated that LPMO might uniquely leverage the redox network toward dynamic and efficient degradation of different cell wall components. Elsevier 2023-09-09 /pmc/articles/PMC10520884/ /pubmed/37766973 http://dx.doi.org/10.1016/j.isci.2023.107870 Text en © 2023. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Sun, Su Li, Fei Li, Muzi Zhang, Wenqian Jiang, Zhenxiong Zhao, Honglu Pu, Yunqiao Ragauskas, Arthur J. Dai, Susie Y. Zhang, Xiaoyu Yu, Hongbo Yuan, Joshua S. Xie, Shangxian Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
title | Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
title_full | Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
title_fullStr | Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
title_full_unstemmed | Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
title_short | Lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
title_sort | lytic polysaccharide monooxygenase synergized with lignin-degrading enzymes for efficient lignin degradation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520884/ https://www.ncbi.nlm.nih.gov/pubmed/37766973 http://dx.doi.org/10.1016/j.isci.2023.107870 |
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