Exploring PEGylated and immobilized laccases for catechol polymerization

Laccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We...

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Autores principales: Su, Jing, Noro, Jennifer, Fu, Jiajia, Wang, Qiang, Silva, Carla, Cavaco-Paulo, Artur
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2018
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6104406/
https://www.ncbi.nlm.nih.gov/pubmed/30136217
http://dx.doi.org/10.1186/s13568-018-0665-5
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author Su, Jing
Noro, Jennifer
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
author_facet Su, Jing
Noro, Jennifer
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
author_sort Su, Jing
collection PubMed
description Laccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We found that PEGylated and immobilized laccase forms have differentiated catalytic behavior revealing distinct conversion rates and differentiated poly(catechol) chains, as confirmed by UV–Visible spectroscopy, by the total content of OH groups and by MALDI-TOF spectroscopy. The synergy underlying on the immobilized/PEGylated enzyme forms reveal to be responsible for the highest conversion rates and for the longer polymers produced. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13568-018-0665-5) contains supplementary material, which is available to authorized users.
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spelling pubmed-61044062018-09-04 Exploring PEGylated and immobilized laccases for catechol polymerization Su, Jing Noro, Jennifer Fu, Jiajia Wang, Qiang Silva, Carla Cavaco-Paulo, Artur AMB Express Original Article Laccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We found that PEGylated and immobilized laccase forms have differentiated catalytic behavior revealing distinct conversion rates and differentiated poly(catechol) chains, as confirmed by UV–Visible spectroscopy, by the total content of OH groups and by MALDI-TOF spectroscopy. The synergy underlying on the immobilized/PEGylated enzyme forms reveal to be responsible for the highest conversion rates and for the longer polymers produced. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13568-018-0665-5) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2018-08-22 /pmc/articles/PMC6104406/ /pubmed/30136217 http://dx.doi.org/10.1186/s13568-018-0665-5 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Su, Jing
Noro, Jennifer
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
Exploring PEGylated and immobilized laccases for catechol polymerization
title Exploring PEGylated and immobilized laccases for catechol polymerization
title_full Exploring PEGylated and immobilized laccases for catechol polymerization
title_fullStr Exploring PEGylated and immobilized laccases for catechol polymerization
title_full_unstemmed Exploring PEGylated and immobilized laccases for catechol polymerization
title_short Exploring PEGylated and immobilized laccases for catechol polymerization
title_sort exploring pegylated and immobilized laccases for catechol polymerization
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6104406/
https://www.ncbi.nlm.nih.gov/pubmed/30136217
http://dx.doi.org/10.1186/s13568-018-0665-5
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