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| Natura: | Artículo científico |
| Lingua: | en |
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Proceedings of the National Academy of Sciences of the United States of America
2025
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| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/39854233/ |
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| _version_ | 1868266252618694656 |
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| author | Liang, Congying Lin, Lu Xu, Tao Kang, Guoqiang Liu, Zhi-Hua Li, Bing-Zhi |
| author_facet | Liang, Congying Lin, Lu Xu, Tao Kang, Guoqiang Liu, Zhi-Hua Li, Bing-Zhi Liang, Congying Lin, Lu Xu, Tao Kang, Guoqiang Liu, Zhi-Hua Li, Bing-Zhi |
| collection | PubMed - marine biology |
| contents | The ligninolytic catalytic network reveals the importance of auxiliary enzymes in lignin biocatalysts. Liang, Congying Lin, Lu Xu, Tao Kang, Guoqiang Liu, Zhi-Hua Li, Bing-Zhi Lignin Pseudomonas putida Peroxidases Bacterial Proteins Biocatalysis Oxidation-Reduction Lignin degradation by biocatalysts is a key strategy to develop a plant-based sustainable carbon economy and thus alleviate global climate change. This process involves synergy between ligninases and auxiliary enzymes. However, auxiliary enzymes within secretomes, which are composed of thousands of enzymes, remain enigmatic, although several ligninolytic enzymes have been well characterized. Moreover, it is a challenge to understand synergistic lignin degradation via a diverse array of enzymes, especially in bacterial systems. In this study, the coexpression network of the periplasmic proteome uncovers potential accessory enzymes for B-type dye-decolorizing peroxidases (DypBs) in A514. The catalytic network of the DypBs-based multienzyme complex is characterized. DypBs couple with quinone reductases and nitroreductase to participate in quinone redox cycling. They work with superoxide dismutase to induce Fenton reaction for lignin oxidation. A synthetic enzyme cocktail (SEC), recruiting 15 enzymes, was consequently designed with four functions. It overcomes the limitation of lignin repolymerization, exhibiting a capacity comparable to that of the native periplasmic secretome. Importantly, we reveal the synergistic mechanism of a SEC-A514 cell system, which incorporates the advantages of in vitro enzyme catalysis and in vivo microbial catabolism. Chemical analysis shows that this system significantly reduces the molecular weight of lignin, substantially extends the degradation spectra for lignin functional groups, and efficiently metabolizes lignin derivatives. As a result, 25% of lignin is utilized, and its average molecular weight is reduced by 27%. Our study advances the knowledge of bacterial lignin-degrading multienzymes and provides a viable lignin degradation strategy. |
| format | Artículo científico |
| id | pubmed_39854233 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Proceedings of the National Academy of Sciences of the United States of America |
| record_format | pubmed |
| spellingShingle | The ligninolytic catalytic network reveals the importance of auxiliary enzymes in lignin biocatalysts. Liang, Congying Lin, Lu Xu, Tao Kang, Guoqiang Liu, Zhi-Hua Li, Bing-Zhi Lignin Pseudomonas putida Peroxidases Bacterial Proteins Biocatalysis Oxidation-Reduction The ligninolytic catalytic network reveals the importance of auxiliary enzymes in lignin biocatalysts. Liang, Congying Lin, Lu Xu, Tao Kang, Guoqiang Liu, Zhi-Hua Li, Bing-Zhi Lignin Pseudomonas putida Peroxidases Bacterial Proteins Biocatalysis Oxidation-Reduction Lignin degradation by biocatalysts is a key strategy to develop a plant-based sustainable carbon economy and thus alleviate global climate change. This process involves synergy between ligninases and auxiliary enzymes. However, auxiliary enzymes within secretomes, which are composed of thousands of enzymes, remain enigmatic, although several ligninolytic enzymes have been well characterized. Moreover, it is a challenge to understand synergistic lignin degradation via a diverse array of enzymes, especially in bacterial systems. In this study, the coexpression network of the periplasmic proteome uncovers potential accessory enzymes for B-type dye-decolorizing peroxidases (DypBs) in A514. The catalytic network of the DypBs-based multienzyme complex is characterized. DypBs couple with quinone reductases and nitroreductase to participate in quinone redox cycling. They work with superoxide dismutase to induce Fenton reaction for lignin oxidation. A synthetic enzyme cocktail (SEC), recruiting 15 enzymes, was consequently designed with four functions. It overcomes the limitation of lignin repolymerization, exhibiting a capacity comparable to that of the native periplasmic secretome. Importantly, we reveal the synergistic mechanism of a SEC-A514 cell system, which incorporates the advantages of in vitro enzyme catalysis and in vivo microbial catabolism. Chemical analysis shows that this system significantly reduces the molecular weight of lignin, substantially extends the degradation spectra for lignin functional groups, and efficiently metabolizes lignin derivatives. As a result, 25% of lignin is utilized, and its average molecular weight is reduced by 27%. Our study advances the knowledge of bacterial lignin-degrading multienzymes and provides a viable lignin degradation strategy. |
| title | The ligninolytic catalytic network reveals the importance of auxiliary enzymes in lignin biocatalysts. |
| topic | Lignin Pseudomonas putida Peroxidases Bacterial Proteins Biocatalysis Oxidation-Reduction |
| url | https://pubmed.ncbi.nlm.nih.gov/39854233/ |