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The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background
BACKGROUND: The filamentous fungus Aspergillus niger is widely exploited as an important expression host for industrial production. The glucoamylase high-producing strain A. niger CICC2462 has been used as a host strain for the establishment of a secretion expression system. It expresses recombinant...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4850703/ https://www.ncbi.nlm.nih.gov/pubmed/27125644 http://dx.doi.org/10.1186/s12934-016-0463-1 |
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author | Zhang, Hui Wang, Shuang Zhang, Xiang xiang Ji, Wei Song, Fuping Zhao, Yue Li, Jie |
author_facet | Zhang, Hui Wang, Shuang Zhang, Xiang xiang Ji, Wei Song, Fuping Zhao, Yue Li, Jie |
author_sort | Zhang, Hui |
collection | PubMed |
description | BACKGROUND: The filamentous fungus Aspergillus niger is widely exploited as an important expression host for industrial production. The glucoamylase high-producing strain A. niger CICC2462 has been used as a host strain for the establishment of a secretion expression system. It expresses recombinant xylanase, mannase and asparaginase at a high level, but some high secretory background proteins in these recombinant strains still remain, such as alpha-amylase and alpha-glucosidase; lead to a low-purity of fermentation products. The aim was to construct an A. niger host strain with a low background of protein secretion. RESULTS: The transcription factor amyR was deleted in A. niger CICC2462, and the results from enzyme activity assays and SDS-PAGE analysis showed that the glucoamylase and amylase activities of the ∆amyR strains were significantly lower than those of the wild-type strain. High-throughput RNA-sequencing and shotgun LC–MS/MS proteomic technology analysis demonstrated that the expression of amylolytic enzymes was decreased at both the transcriptional and translational levels in the ∆amyR strain. Interestingly, the ∆amyR strain growth rate better than the wild-type strain. CONCLUSIONS: Our findings clearly indicated that the ∆amyR strain of A. niger CICC2462 can be used as a host strain with a low background of protein secretion. |
format | Online Article Text |
id | pubmed-4850703 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-48507032016-04-30 The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background Zhang, Hui Wang, Shuang Zhang, Xiang xiang Ji, Wei Song, Fuping Zhao, Yue Li, Jie Microb Cell Fact Research BACKGROUND: The filamentous fungus Aspergillus niger is widely exploited as an important expression host for industrial production. The glucoamylase high-producing strain A. niger CICC2462 has been used as a host strain for the establishment of a secretion expression system. It expresses recombinant xylanase, mannase and asparaginase at a high level, but some high secretory background proteins in these recombinant strains still remain, such as alpha-amylase and alpha-glucosidase; lead to a low-purity of fermentation products. The aim was to construct an A. niger host strain with a low background of protein secretion. RESULTS: The transcription factor amyR was deleted in A. niger CICC2462, and the results from enzyme activity assays and SDS-PAGE analysis showed that the glucoamylase and amylase activities of the ∆amyR strains were significantly lower than those of the wild-type strain. High-throughput RNA-sequencing and shotgun LC–MS/MS proteomic technology analysis demonstrated that the expression of amylolytic enzymes was decreased at both the transcriptional and translational levels in the ∆amyR strain. Interestingly, the ∆amyR strain growth rate better than the wild-type strain. CONCLUSIONS: Our findings clearly indicated that the ∆amyR strain of A. niger CICC2462 can be used as a host strain with a low background of protein secretion. BioMed Central 2016-04-28 /pmc/articles/PMC4850703/ /pubmed/27125644 http://dx.doi.org/10.1186/s12934-016-0463-1 Text en © Zhang et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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 Zhang, Hui Wang, Shuang Zhang, Xiang xiang Ji, Wei Song, Fuping Zhao, Yue Li, Jie The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background |
title | The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background |
title_full | The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background |
title_fullStr | The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background |
title_full_unstemmed | The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background |
title_short | The amyR-deletion strain of Aspergillus niger CICC2462 is a suitable host strain to express secreted protein with a low background |
title_sort | amyr-deletion strain of aspergillus niger cicc2462 is a suitable host strain to express secreted protein with a low background |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4850703/ https://www.ncbi.nlm.nih.gov/pubmed/27125644 http://dx.doi.org/10.1186/s12934-016-0463-1 |
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