Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Miao, Youzhi, Li, Juan, Xiao, Zhizhuang, Shen, Qirong, Zhang, Ruifu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
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
_version_ 1782377770673766400
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
work_keys_str_mv AT miaoyouzhi characterizationandidentificationofthexylanolyticenzymesfromaspergillusfumigatusz5
AT lijuan characterizationandidentificationofthexylanolyticenzymesfromaspergillusfumigatusz5
AT xiaozhizhuang characterizationandidentificationofthexylanolyticenzymesfromaspergillusfumigatusz5
AT shenqirong characterizationandidentificationofthexylanolyticenzymesfromaspergillusfumigatusz5
AT zhangruifu characterizationandidentificationofthexylanolyticenzymesfromaspergillusfumigatusz5