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Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)

Enzymatic polymerization of lignin is an environmentally-friendly and sustainable method that is investigated for its potential in opening-up new applications of one of the most abundant biopolymers on our planet. In this work, the laccase from Myceliophthora thermophila was successfully immobilized...

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Autores principales: Huber, Daniela, Pellis, Alessandro, Daxbacher, Andreas, Nyanhongo, Gibson S., Guebitz, Georg M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6431913/
https://www.ncbi.nlm.nih.gov/pubmed/30974557
http://dx.doi.org/10.3390/polym8080280
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author Huber, Daniela
Pellis, Alessandro
Daxbacher, Andreas
Nyanhongo, Gibson S.
Guebitz, Georg M.
author_facet Huber, Daniela
Pellis, Alessandro
Daxbacher, Andreas
Nyanhongo, Gibson S.
Guebitz, Georg M.
author_sort Huber, Daniela
collection PubMed
description Enzymatic polymerization of lignin is an environmentally-friendly and sustainable method that is investigated for its potential in opening-up new applications of one of the most abundant biopolymers on our planet. In this work, the laccase from Myceliophthora thermophila was successfully immobilized onto Accurel MP1000 beads (67% of protein bound to the polymeric carrier) and the biocatalyzed oxidation of Kraft lignin (KL) and lignosulfonate (LS) were carried out. Fluorescence intensity determination, phenol content analysis and size exclusion chromatography were performed in order to elucidate the extent of the polymerization reaction. The collected results show an 8.5-fold decrease of the LS samples’ fluorescence intensity after laccase-mediated oxidation and a 12-fold increase of the weight average molecular weight was obtained.
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spelling pubmed-64319132019-04-02 Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL) Huber, Daniela Pellis, Alessandro Daxbacher, Andreas Nyanhongo, Gibson S. Guebitz, Georg M. Polymers (Basel) Article Enzymatic polymerization of lignin is an environmentally-friendly and sustainable method that is investigated for its potential in opening-up new applications of one of the most abundant biopolymers on our planet. In this work, the laccase from Myceliophthora thermophila was successfully immobilized onto Accurel MP1000 beads (67% of protein bound to the polymeric carrier) and the biocatalyzed oxidation of Kraft lignin (KL) and lignosulfonate (LS) were carried out. Fluorescence intensity determination, phenol content analysis and size exclusion chromatography were performed in order to elucidate the extent of the polymerization reaction. The collected results show an 8.5-fold decrease of the LS samples’ fluorescence intensity after laccase-mediated oxidation and a 12-fold increase of the weight average molecular weight was obtained. MDPI 2016-08-03 /pmc/articles/PMC6431913/ /pubmed/30974557 http://dx.doi.org/10.3390/polym8080280 Text en © 2016 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Huber, Daniela
Pellis, Alessandro
Daxbacher, Andreas
Nyanhongo, Gibson S.
Guebitz, Georg M.
Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)
title Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)
title_full Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)
title_fullStr Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)
title_full_unstemmed Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)
title_short Polymerization of Various Lignins via Immobilized Myceliophthora thermophila Laccase (MtL)
title_sort polymerization of various lignins via immobilized myceliophthora thermophila laccase (mtl)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6431913/
https://www.ncbi.nlm.nih.gov/pubmed/30974557
http://dx.doi.org/10.3390/polym8080280
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