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Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme
Modification of kraft lignin (KL), traditionally uses harsh and energy-demanding physical and chemical processes. In this study, the potential of the bacterial laccase CotA (spore coating protein A) for oxidation of KL under mild conditions was assessed. Thereby, the efficiency of CotA to oxidize bo...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8658217/ https://www.ncbi.nlm.nih.gov/pubmed/34884966 http://dx.doi.org/10.3390/ijms222313161 |
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author | Mayr, Sebastian A. Subagia, Raditya Weiss, Renate Schwaiger, Nikolaus Weber, Hedda K. Leitner, Johannes Ribitsch, Doris Nyanhongo, Gibson S. Guebitz, Georg M. |
author_facet | Mayr, Sebastian A. Subagia, Raditya Weiss, Renate Schwaiger, Nikolaus Weber, Hedda K. Leitner, Johannes Ribitsch, Doris Nyanhongo, Gibson S. Guebitz, Georg M. |
author_sort | Mayr, Sebastian A. |
collection | PubMed |
description | Modification of kraft lignin (KL), traditionally uses harsh and energy-demanding physical and chemical processes. In this study, the potential of the bacterial laccase CotA (spore coating protein A) for oxidation of KL under mild conditions was assessed. Thereby, the efficiency of CotA to oxidize both softwood and hardwood KL of varying purity at alkaline conditions was examined. For the respective type of wood, the highest oxidation activity by CotA was determined for the medium ash content softwood KL (MA_S) and the medium ash content hardwood KL (MA_H), respectively. By an up to 95% decrease in fluorescence and up to 65% in phenol content coupling of the structural lignin units was indicated. These results correlated with an increase in viscosity and molecular weight, which increased nearly 2 and 20-fold for MA_H and about 1.3 and 6.0-fold for MA_S, respectively. Thus, this study confirms that the CotA laccase can oxidize a variety of KL at alkaline conditions, while the origin and purity of KL were found to have a major impact on the efficiency of oxidation. Under the herein tested conditions, it was observed that the MA_H KL showed the highest susceptibility to CotA oxidation when compared to the other hardwood KLs and the softwood KLs. Therefore, this could be a viable method to produce sustainable resins and adhesives. |
format | Online Article Text |
id | pubmed-8658217 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86582172021-12-10 Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme Mayr, Sebastian A. Subagia, Raditya Weiss, Renate Schwaiger, Nikolaus Weber, Hedda K. Leitner, Johannes Ribitsch, Doris Nyanhongo, Gibson S. Guebitz, Georg M. Int J Mol Sci Article Modification of kraft lignin (KL), traditionally uses harsh and energy-demanding physical and chemical processes. In this study, the potential of the bacterial laccase CotA (spore coating protein A) for oxidation of KL under mild conditions was assessed. Thereby, the efficiency of CotA to oxidize both softwood and hardwood KL of varying purity at alkaline conditions was examined. For the respective type of wood, the highest oxidation activity by CotA was determined for the medium ash content softwood KL (MA_S) and the medium ash content hardwood KL (MA_H), respectively. By an up to 95% decrease in fluorescence and up to 65% in phenol content coupling of the structural lignin units was indicated. These results correlated with an increase in viscosity and molecular weight, which increased nearly 2 and 20-fold for MA_H and about 1.3 and 6.0-fold for MA_S, respectively. Thus, this study confirms that the CotA laccase can oxidize a variety of KL at alkaline conditions, while the origin and purity of KL were found to have a major impact on the efficiency of oxidation. Under the herein tested conditions, it was observed that the MA_H KL showed the highest susceptibility to CotA oxidation when compared to the other hardwood KLs and the softwood KLs. Therefore, this could be a viable method to produce sustainable resins and adhesives. MDPI 2021-12-06 /pmc/articles/PMC8658217/ /pubmed/34884966 http://dx.doi.org/10.3390/ijms222313161 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Mayr, Sebastian A. Subagia, Raditya Weiss, Renate Schwaiger, Nikolaus Weber, Hedda K. Leitner, Johannes Ribitsch, Doris Nyanhongo, Gibson S. Guebitz, Georg M. Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme |
title | Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme |
title_full | Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme |
title_fullStr | Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme |
title_full_unstemmed | Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme |
title_short | Oxidation of Various Kraft Lignins with a Bacterial Laccase Enzyme |
title_sort | oxidation of various kraft lignins with a bacterial laccase enzyme |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8658217/ https://www.ncbi.nlm.nih.gov/pubmed/34884966 http://dx.doi.org/10.3390/ijms222313161 |
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