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Identification of an endo-1,4-beta-xylanase of Ustilago maydis

BACKGROUND: The utilization of raw biomass components such as cellulose or hemicellulose for the production of valuable chemicals has attracted considerable research interest in recent years. One promising approach is the application of microorganisms that naturally convert biomass constituents into...

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Autores principales: Geiser, Elena, Wierckx, Nick, Zimmermann, Martin, Blank, Lars M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737115/
https://www.ncbi.nlm.nih.gov/pubmed/23889751
http://dx.doi.org/10.1186/1472-6750-13-59
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author Geiser, Elena
Wierckx, Nick
Zimmermann, Martin
Blank, Lars M
author_facet Geiser, Elena
Wierckx, Nick
Zimmermann, Martin
Blank, Lars M
author_sort Geiser, Elena
collection PubMed
description BACKGROUND: The utilization of raw biomass components such as cellulose or hemicellulose for the production of valuable chemicals has attracted considerable research interest in recent years. One promising approach is the application of microorganisms that naturally convert biomass constituents into value added chemicals. One of these organisms – Ustilago maydis – can grow on xylan, the second most abundant polysaccharide in nature, while at the same time it produces chemicals of biotechnological interest. RESULTS: In this study, we present the identification of an endo-1,4-beta xylanase responsible for xylan degradation. Xylanase activity of U. maydis cells was indirectly detected by the quantification of released reducing sugars and could be confirmed by visualizing oligosaccharides as degradation products of xylan by thin layer chromatography. A putative endo-1,4-beta-xylanase, encoded by um06350.1, was identified in the supernatant of xylan-grown cells. To confirm the activity, we displayed the putative xylanase on the surface of the xylanase negative Saccharomyces cerevisiae EBY100. The presented enzyme converted xylan to xylotriose, similar to the source organism U. maydis. CONCLUSIONS: The xylan degradation ability together with its unicellular and yeast-like growth makes U. maydis MB215 a promising candidate for the production of valuable chemicals such as itaconic acid or glycolipids from lignocellulosic biomass. Therefore, the characterization of the endo-1,4-beta-xylanase, encoded by um06350.1, is a further step towards the biotechnological application of U. maydis and its enzymes.
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spelling pubmed-37371152013-08-08 Identification of an endo-1,4-beta-xylanase of Ustilago maydis Geiser, Elena Wierckx, Nick Zimmermann, Martin Blank, Lars M BMC Biotechnol Research Article BACKGROUND: The utilization of raw biomass components such as cellulose or hemicellulose for the production of valuable chemicals has attracted considerable research interest in recent years. One promising approach is the application of microorganisms that naturally convert biomass constituents into value added chemicals. One of these organisms – Ustilago maydis – can grow on xylan, the second most abundant polysaccharide in nature, while at the same time it produces chemicals of biotechnological interest. RESULTS: In this study, we present the identification of an endo-1,4-beta xylanase responsible for xylan degradation. Xylanase activity of U. maydis cells was indirectly detected by the quantification of released reducing sugars and could be confirmed by visualizing oligosaccharides as degradation products of xylan by thin layer chromatography. A putative endo-1,4-beta-xylanase, encoded by um06350.1, was identified in the supernatant of xylan-grown cells. To confirm the activity, we displayed the putative xylanase on the surface of the xylanase negative Saccharomyces cerevisiae EBY100. The presented enzyme converted xylan to xylotriose, similar to the source organism U. maydis. CONCLUSIONS: The xylan degradation ability together with its unicellular and yeast-like growth makes U. maydis MB215 a promising candidate for the production of valuable chemicals such as itaconic acid or glycolipids from lignocellulosic biomass. Therefore, the characterization of the endo-1,4-beta-xylanase, encoded by um06350.1, is a further step towards the biotechnological application of U. maydis and its enzymes. BioMed Central 2013-07-26 /pmc/articles/PMC3737115/ /pubmed/23889751 http://dx.doi.org/10.1186/1472-6750-13-59 Text en Copyright © 2013 Geiser et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Geiser, Elena
Wierckx, Nick
Zimmermann, Martin
Blank, Lars M
Identification of an endo-1,4-beta-xylanase of Ustilago maydis
title Identification of an endo-1,4-beta-xylanase of Ustilago maydis
title_full Identification of an endo-1,4-beta-xylanase of Ustilago maydis
title_fullStr Identification of an endo-1,4-beta-xylanase of Ustilago maydis
title_full_unstemmed Identification of an endo-1,4-beta-xylanase of Ustilago maydis
title_short Identification of an endo-1,4-beta-xylanase of Ustilago maydis
title_sort identification of an endo-1,4-beta-xylanase of ustilago maydis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737115/
https://www.ncbi.nlm.nih.gov/pubmed/23889751
http://dx.doi.org/10.1186/1472-6750-13-59
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