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Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy
Kraft lignin, a side-stream from the pulp and paper industry, can be modified by laccases for the synthesis of high added-value products. This work aims to study different laccase sources, including a bacterial laccase from Streptomyces ipomoeae (SiLA) and a fungal laccase from Myceliophthora thermo...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9920240/ https://www.ncbi.nlm.nih.gov/pubmed/36771814 http://dx.doi.org/10.3390/polym15030513 |
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author | García-Fuentevilla, Luisa Domínguez, Gabriela Martín-Sampedro, Raquel Hernández, Manuel Arias, María E. Santos, José I. Ibarra, David Eugenio, María E. |
author_facet | García-Fuentevilla, Luisa Domínguez, Gabriela Martín-Sampedro, Raquel Hernández, Manuel Arias, María E. Santos, José I. Ibarra, David Eugenio, María E. |
author_sort | García-Fuentevilla, Luisa |
collection | PubMed |
description | Kraft lignin, a side-stream from the pulp and paper industry, can be modified by laccases for the synthesis of high added-value products. This work aims to study different laccase sources, including a bacterial laccase from Streptomyces ipomoeae (SiLA) and a fungal laccase from Myceliophthora thermophila (MtL), for kraft lignin polymerization. To study the influence of some variables in these processes, a central composite design (CCD) with two continuous variables (enzyme concentration and reaction time) and three levels for each variable was used. The prediction of the behavior of the output variables (phenolic content and molecular weight of lignins) were modelled by means of response surface methodology (RSM). Moreover, characterization of lignins was performed by Fourier-transform infrared (FTIR) spectroscopy and different nuclear magnetic resonance (NMR) spectroscopy techniques. In addition, antioxidant activity was also analyzed. Results showed that lignin polymerization (referring to polymerization as lower phenolic content and higher molecular weight) occurred by the action of both laccases. The enzyme concentration was the most influential variable in the lignin polymerization reaction within the range studied for SiLA laccase, while the most influential variable for MtL laccase was the reaction time. FTIR and NMR characterization analysis corroborated lignin polymerization results obtained from the RSM. |
format | Online Article Text |
id | pubmed-9920240 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-99202402023-02-12 Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy García-Fuentevilla, Luisa Domínguez, Gabriela Martín-Sampedro, Raquel Hernández, Manuel Arias, María E. Santos, José I. Ibarra, David Eugenio, María E. Polymers (Basel) Article Kraft lignin, a side-stream from the pulp and paper industry, can be modified by laccases for the synthesis of high added-value products. This work aims to study different laccase sources, including a bacterial laccase from Streptomyces ipomoeae (SiLA) and a fungal laccase from Myceliophthora thermophila (MtL), for kraft lignin polymerization. To study the influence of some variables in these processes, a central composite design (CCD) with two continuous variables (enzyme concentration and reaction time) and three levels for each variable was used. The prediction of the behavior of the output variables (phenolic content and molecular weight of lignins) were modelled by means of response surface methodology (RSM). Moreover, characterization of lignins was performed by Fourier-transform infrared (FTIR) spectroscopy and different nuclear magnetic resonance (NMR) spectroscopy techniques. In addition, antioxidant activity was also analyzed. Results showed that lignin polymerization (referring to polymerization as lower phenolic content and higher molecular weight) occurred by the action of both laccases. The enzyme concentration was the most influential variable in the lignin polymerization reaction within the range studied for SiLA laccase, while the most influential variable for MtL laccase was the reaction time. FTIR and NMR characterization analysis corroborated lignin polymerization results obtained from the RSM. MDPI 2023-01-18 /pmc/articles/PMC9920240/ /pubmed/36771814 http://dx.doi.org/10.3390/polym15030513 Text en © 2023 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 García-Fuentevilla, Luisa Domínguez, Gabriela Martín-Sampedro, Raquel Hernández, Manuel Arias, María E. Santos, José I. Ibarra, David Eugenio, María E. Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy |
title | Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy |
title_full | Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy |
title_fullStr | Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy |
title_full_unstemmed | Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy |
title_short | Enzyme-Catalyzed Polymerization of Kraft Lignin from Eucalyptus globulus: Comparison of Bacterial and Fungal Laccases Efficacy |
title_sort | enzyme-catalyzed polymerization of kraft lignin from eucalyptus globulus: comparison of bacterial and fungal laccases efficacy |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9920240/ https://www.ncbi.nlm.nih.gov/pubmed/36771814 http://dx.doi.org/10.3390/polym15030513 |
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