Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76
Abstract 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-en...
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| Format: | Article |
| Language: | English |
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BMC
2021-05-01
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| Series: | Biotechnology for Biofuels |
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| Online Access: | https://doi.org/10.1186/s13068-021-01967-1 |
| _version_ | 1818208746119102464 |
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| author | Shu Zhang Sha Zhao Weihao Shang Zijuan Yan Xiuyun Wu Yingjie Li Guanjun Chen Xinli Liu Lushan Wang |
| author_facet | Shu Zhang Sha Zhao Weihao Shang Zijuan Yan Xiuyun Wu Yingjie Li Guanjun Chen Xinli Liu Lushan Wang |
| author_sort | Shu Zhang |
| collection | DOAJ |
| description | Abstract 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. |
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| institution | Directory Open Access Journal |
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| language | English |
| last_indexed | 2024-12-12T04:49:43Z |
| publishDate | 2021-05-01 |
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| series | Biotechnology for Biofuels |
| spelling | doaj.art-466100b5a9fb4806893c5ac0eb00e2552022-12-22T00:37:31ZengBMCBiotechnology for Biofuels1754-68342021-05-0114111310.1186/s13068-021-01967-1Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76Shu Zhang0Sha Zhao1Weihao Shang2Zijuan Yan3Xiuyun Wu4Yingjie Li5Guanjun Chen6Xinli Liu7Lushan Wang8State Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversityState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversityState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversitySchool of Life Sciences, Shandong UniversityState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversityState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversityState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversityState Key Laboratory of Biobased Material and Green Papermaking, Qilu University of Technology, Shandong Academy of SciencesState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong UniversityAbstract 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.https://doi.org/10.1186/s13068-021-01967-1Aspergillus nigerGH11 xylanasesTranscription analysisDegradation patternSynergistic hydrolysis |
| spellingShingle | Shu Zhang Sha Zhao Weihao Shang Zijuan Yan Xiuyun Wu Yingjie Li Guanjun Chen Xinli Liu Lushan Wang Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76 Biotechnology for Biofuels Aspergillus niger GH11 xylanases Transcription analysis Degradation pattern Synergistic hydrolysis |
| 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 | Aspergillus niger GH11 xylanases Transcription analysis Degradation pattern Synergistic hydrolysis |
| url | https://doi.org/10.1186/s13068-021-01967-1 |
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