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Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5
BACKGROUND: Plant biomass, the most abundant natural material on earth, represents a vast source of food and energy in nature. As the main component of plant biomass, xylan is a complex polysaccharide comprising a linear β(1,4)-linked backbone of xylosyl residues substituted by acetyl, arabinosyl, g...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4477485/ https://www.ncbi.nlm.nih.gov/pubmed/26100973 http://dx.doi.org/10.1186/s12866-015-0463-z |
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author | Miao, Youzhi Li, Juan Xiao, Zhizhuang Shen, Qirong Zhang, Ruifu |
author_facet | Miao, Youzhi Li, Juan Xiao, Zhizhuang Shen, Qirong Zhang, Ruifu |
author_sort | Miao, Youzhi |
collection | PubMed |
description | BACKGROUND: Plant biomass, the most abundant natural material on earth, represents a vast source of food and energy in nature. As the main component of plant biomass, xylan is a complex polysaccharide comprising a linear β(1,4)-linked backbone of xylosyl residues substituted by acetyl, arabinosyl, glucuronysyl and 4-O-methylglucuronycyl residues. RESULTS: Aspergillus fumigatus Z5 is an efficient plant biomass depolymerization fungus. In this study, its crude xylanolytic enzymes were characterized and identified by two-dimensional gel electrophoresis (2-DE). The optimal temperature for the crude xylanases was close to 60 °C, the highest xylanase activity was achieved at pH ranged from 3 to 6, and the crude xylanases also showed a very broad region of pH (3–11) stability. The maximal xylanase activity of 21.45 U · ml(−1) was observed in the fourth day of cultivation at 50 °C and 150 rpm with 2 % xylan as the sole carbon source. Zymogram analysis indicated that there were more than seven secreted proteins with xylanase activity. In the crude enzyme, two major endoxylanases, five cellulases and several associated enzymes were identified to be involved in the hydrolysis of polysaccharides. Of the total 13 xylanase genes in the Z5 genome, 11 were observed using q-PCR to be induced by xylan, one of which, An endo-1,4-β-xylanase with a low secretion level, was also expressed and characterized. The final hydrolysis products of xylan by crude enzyme mainly consisted of xylobiose. CONCLUSIONS: This study provides a comprehensive understanding of the depolymerization of xylan by Z5 and will help to design enzymatic strategies for plant biomass utilization. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12866-015-0463-z) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4477485 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-44774852015-06-24 Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 Miao, Youzhi Li, Juan Xiao, Zhizhuang Shen, Qirong Zhang, Ruifu BMC Microbiol Research Article BACKGROUND: Plant biomass, the most abundant natural material on earth, represents a vast source of food and energy in nature. As the main component of plant biomass, xylan is a complex polysaccharide comprising a linear β(1,4)-linked backbone of xylosyl residues substituted by acetyl, arabinosyl, glucuronysyl and 4-O-methylglucuronycyl residues. RESULTS: Aspergillus fumigatus Z5 is an efficient plant biomass depolymerization fungus. In this study, its crude xylanolytic enzymes were characterized and identified by two-dimensional gel electrophoresis (2-DE). The optimal temperature for the crude xylanases was close to 60 °C, the highest xylanase activity was achieved at pH ranged from 3 to 6, and the crude xylanases also showed a very broad region of pH (3–11) stability. The maximal xylanase activity of 21.45 U · ml(−1) was observed in the fourth day of cultivation at 50 °C and 150 rpm with 2 % xylan as the sole carbon source. Zymogram analysis indicated that there were more than seven secreted proteins with xylanase activity. In the crude enzyme, two major endoxylanases, five cellulases and several associated enzymes were identified to be involved in the hydrolysis of polysaccharides. Of the total 13 xylanase genes in the Z5 genome, 11 were observed using q-PCR to be induced by xylan, one of which, An endo-1,4-β-xylanase with a low secretion level, was also expressed and characterized. The final hydrolysis products of xylan by crude enzyme mainly consisted of xylobiose. CONCLUSIONS: This study provides a comprehensive understanding of the depolymerization of xylan by Z5 and will help to design enzymatic strategies for plant biomass utilization. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12866-015-0463-z) contains supplementary material, which is available to authorized users. BioMed Central 2015-06-23 /pmc/articles/PMC4477485/ /pubmed/26100973 http://dx.doi.org/10.1186/s12866-015-0463-z Text en © Miao et al. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Miao, Youzhi Li, Juan Xiao, Zhizhuang Shen, Qirong Zhang, Ruifu Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 |
title | Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 |
title_full | Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 |
title_fullStr | Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 |
title_full_unstemmed | Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 |
title_short | Characterization and identification of the xylanolytic enzymes from Aspergillus fumigatus Z5 |
title_sort | characterization and identification of the xylanolytic enzymes from aspergillus fumigatus z5 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4477485/ https://www.ncbi.nlm.nih.gov/pubmed/26100973 http://dx.doi.org/10.1186/s12866-015-0463-z |
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