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Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76

BACKGROUND: Xylan is the most abundant hemicellulose polysaccharide in nature, which can be converted into high value-added products. However, its recalcitrance to breakdown requires the synergistic action of multiple enzymes. Aspergillus niger, possessing numerous xylan degrading isozyme-encoding g...

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Autores principales: Zhang, Shu, Zhao, Sha, Shang, Weihao, Yan, Zijuan, Wu, Xiuyun, Li, Yingjie, Chen, Guanjun, Liu, Xinli, Wang, Lushan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8112042/
https://www.ncbi.nlm.nih.gov/pubmed/33971954
http://dx.doi.org/10.1186/s13068-021-01967-1
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author Zhang, Shu
Zhao, Sha
Shang, Weihao
Yan, Zijuan
Wu, Xiuyun
Li, Yingjie
Chen, Guanjun
Liu, Xinli
Wang, Lushan
author_facet Zhang, Shu
Zhao, Sha
Shang, Weihao
Yan, Zijuan
Wu, Xiuyun
Li, Yingjie
Chen, Guanjun
Liu, Xinli
Wang, Lushan
author_sort Zhang, Shu
collection PubMed
description BACKGROUND: Xylan is the most abundant hemicellulose polysaccharide in nature, which can be converted into high value-added products. However, its recalcitrance to breakdown requires the synergistic action of multiple enzymes. Aspergillus niger, possessing numerous xylan degrading isozyme-encoding genes, are highly effective xylan degraders in xylan-rich habitats. Therefore, it is necessary to explore gene transcription, the mode of action and cooperation mechanism of different xylanase isozymes to further understand the efficient xylan-degradation by A. niger. RESULTS: Aspergillus niger An76 encoded a comprehensive set of xylan-degrading enzymes, including five endo-xylanases (one GH10 and four GH11). Quantitative transcriptional analysis showed that three xylanase genes (xynA, xynB and xynC) were up-regulated by xylan substrates, and the order and amount of enzyme secretion differed. Specifically, GH11 xylanases XynA and XynB were initially secreted successively, followed by GH10 xylanase XynC. Biochemical analyses displayed that three GH11 xylanases (XynA, XynB and XynD) showed differences in catalytic performance and product profiles, possibly because of intricate hydrogen bonding between substrates and functional residues in the active site architectures impacted their binding capacity. Among these, XynB had the best performance in the degradation of xylan and XynE had no catalytic activity. Furthermore, XynA and XynB showed synergistic effects during xylan degradation. CONCLUSIONS: The sequential secretion and different action modes of GH11 xylanases were essential for the efficient xylan degradation by A. niger An76. The elucidation of the degradation mechanisms of these xylanase isozymes further improved our understanding of GH-encoding genes amplification in filamentous fungi and may guide the design of the optimal enzyme cocktails in industrial applications. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13068-021-01967-1.
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spelling pubmed-81120422021-05-12 Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76 Zhang, Shu Zhao, Sha Shang, Weihao Yan, Zijuan Wu, Xiuyun Li, Yingjie Chen, Guanjun Liu, Xinli Wang, Lushan Biotechnol Biofuels Research BACKGROUND: Xylan is the most abundant hemicellulose polysaccharide in nature, which can be converted into high value-added products. However, its recalcitrance to breakdown requires the synergistic action of multiple enzymes. Aspergillus niger, possessing numerous xylan degrading isozyme-encoding genes, are highly effective xylan degraders in xylan-rich habitats. Therefore, it is necessary to explore gene transcription, the mode of action and cooperation mechanism of different xylanase isozymes to further understand the efficient xylan-degradation by A. niger. RESULTS: Aspergillus niger An76 encoded a comprehensive set of xylan-degrading enzymes, including five endo-xylanases (one GH10 and four GH11). Quantitative transcriptional analysis showed that three xylanase genes (xynA, xynB and xynC) were up-regulated by xylan substrates, and the order and amount of enzyme secretion differed. Specifically, GH11 xylanases XynA and XynB were initially secreted successively, followed by GH10 xylanase XynC. Biochemical analyses displayed that three GH11 xylanases (XynA, XynB and XynD) showed differences in catalytic performance and product profiles, possibly because of intricate hydrogen bonding between substrates and functional residues in the active site architectures impacted their binding capacity. Among these, XynB had the best performance in the degradation of xylan and XynE had no catalytic activity. Furthermore, XynA and XynB showed synergistic effects during xylan degradation. CONCLUSIONS: The sequential secretion and different action modes of GH11 xylanases were essential for the efficient xylan degradation by A. niger An76. The elucidation of the degradation mechanisms of these xylanase isozymes further improved our understanding of GH-encoding genes amplification in filamentous fungi and may guide the design of the optimal enzyme cocktails in industrial applications. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13068-021-01967-1. BioMed Central 2021-05-10 /pmc/articles/PMC8112042/ /pubmed/33971954 http://dx.doi.org/10.1186/s13068-021-01967-1 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Zhang, Shu
Zhao, Sha
Shang, Weihao
Yan, Zijuan
Wu, Xiuyun
Li, Yingjie
Chen, Guanjun
Liu, Xinli
Wang, Lushan
Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
title Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
title_full Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
title_fullStr Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
title_full_unstemmed Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
title_short Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
title_sort synergistic mechanism of gh11 xylanases with different action modes from aspergillus niger an76
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8112042/
https://www.ncbi.nlm.nih.gov/pubmed/33971954
http://dx.doi.org/10.1186/s13068-021-01967-1
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