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A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin

Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack...

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Autores principales: Casciello, Carmine, Tonin, Fabio, Berini, Francesca, Fasoli, Elisa, Marinelli, Flavia, Pollegioni, Loredano, Rosini, Elena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5361131/
https://www.ncbi.nlm.nih.gov/pubmed/28352563
http://dx.doi.org/10.1016/j.btre.2016.12.005
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author Casciello, Carmine
Tonin, Fabio
Berini, Francesca
Fasoli, Elisa
Marinelli, Flavia
Pollegioni, Loredano
Rosini, Elena
author_facet Casciello, Carmine
Tonin, Fabio
Berini, Francesca
Fasoli, Elisa
Marinelli, Flavia
Pollegioni, Loredano
Rosini, Elena
author_sort Casciello, Carmine
collection PubMed
description Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their activity on chemically different substrates including a soluble and semi-degraded lignin derivative (known as alkali lignin or Kraft lignin), and we discovered a novel and valuable peroxidase activity produced by the recently classified actinomycete Nonomuraea gerenzanensis. Compared to known fungal manganese and versatile peroxidases, the stability of N. gerenzanensis peroxidase activity at alkaline pHs and its thermostability are significantly higher. From a kinetic point of view, N. gerenzanensis peroxidase activity shows a K(m) for H(2)O(2) similar to that of Phanerochaete chrysosporium and Bjerkandera enzymes and a lower affinity for Mn(2+), whereas it differs from the six Pleurotus ostreatus manganese peroxidase isoenzymes described in the literature. Additionally, N. gerenzanensis peroxidase shows a remarkable dye-decolorizing activity that expands its substrate range and paves the way for an industrial use of this enzyme. These results confirm that by exploring new bacterial diversity, we may be able to discover and exploit alternative biological tools putatively involved in lignin modification and degradation.
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spelling pubmed-53611312017-03-28 A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin Casciello, Carmine Tonin, Fabio Berini, Francesca Fasoli, Elisa Marinelli, Flavia Pollegioni, Loredano Rosini, Elena Biotechnol Rep (Amst) Article Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their activity on chemically different substrates including a soluble and semi-degraded lignin derivative (known as alkali lignin or Kraft lignin), and we discovered a novel and valuable peroxidase activity produced by the recently classified actinomycete Nonomuraea gerenzanensis. Compared to known fungal manganese and versatile peroxidases, the stability of N. gerenzanensis peroxidase activity at alkaline pHs and its thermostability are significantly higher. From a kinetic point of view, N. gerenzanensis peroxidase activity shows a K(m) for H(2)O(2) similar to that of Phanerochaete chrysosporium and Bjerkandera enzymes and a lower affinity for Mn(2+), whereas it differs from the six Pleurotus ostreatus manganese peroxidase isoenzymes described in the literature. Additionally, N. gerenzanensis peroxidase shows a remarkable dye-decolorizing activity that expands its substrate range and paves the way for an industrial use of this enzyme. These results confirm that by exploring new bacterial diversity, we may be able to discover and exploit alternative biological tools putatively involved in lignin modification and degradation. Elsevier 2017-01-03 /pmc/articles/PMC5361131/ /pubmed/28352563 http://dx.doi.org/10.1016/j.btre.2016.12.005 Text en © 2017 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Casciello, Carmine
Tonin, Fabio
Berini, Francesca
Fasoli, Elisa
Marinelli, Flavia
Pollegioni, Loredano
Rosini, Elena
A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
title A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
title_full A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
title_fullStr A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
title_full_unstemmed A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
title_short A valuable peroxidase activity from the novel species Nonomuraea gerenzanensis growing on alkali lignin
title_sort valuable peroxidase activity from the novel species nonomuraea gerenzanensis growing on alkali lignin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5361131/
https://www.ncbi.nlm.nih.gov/pubmed/28352563
http://dx.doi.org/10.1016/j.btre.2016.12.005
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