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Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles
BACKGROUND: As a ubiquitous filamentous fungal, Aspergillus spp. play a critical role in lignocellulose degradation, which was also defined as considerable cell factories for organic acids and industrially relevant enzymes producer. Nevertheless, the production of various extracellular enzymes can b...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6318881/ https://www.ncbi.nlm.nih.gov/pubmed/30622646 http://dx.doi.org/10.1186/s13068-018-1350-2 |
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author | Miao, Jiaxi Wang, Mengmeng Ma, Lei Li, Tuo Huang, Qiwei Liu, Dongyang Shen, Qirong |
author_facet | Miao, Jiaxi Wang, Mengmeng Ma, Lei Li, Tuo Huang, Qiwei Liu, Dongyang Shen, Qirong |
author_sort | Miao, Jiaxi |
collection | PubMed |
description | BACKGROUND: As a ubiquitous filamentous fungal, Aspergillus spp. play a critical role in lignocellulose degradation, which was also defined as considerable cell factories for organic acids and industrially relevant enzymes producer. Nevertheless, the production of various extracellular enzymes can be influenced by different factors including nitrogen source, carbon source, cultivation temperature, and initial pH value. Thus, this study aims to reveal how amino acids affect the decomposition of lignocellulose by Aspergillus fumigatus Z5 through transcriptional and proteomics methods. RESULTS: The activities of several lignocellulosic enzymes secreted by A. fumigatus Z5 adding with cysteine, methionine, and ammonium sulfate were determined with the chromatometry method. The peak of endo-glucanase (7.33 ± 0.03 U mL(−1)), exo-glucanase (10.50 ± 0.07 U mL(−1)), β-glucosidase (21.50 ± 0.22 U mL(−1)), and xylanase (76.43 ± 0.71 U mL(−1)) were all obtained in the Cys treatment. The secretomes of A. fumigatus Z5 under different treatments were also identified by LC–MS/MS, and 227, 256 and 159 different proteins were identified in the treatments of Cys, Met, and CK (Control, treatment with ammonium sulfate as the sole nitrogen source), respectively. Correlation analysis results of transcriptome and proteome data with fermentation profiles showed that most of the cellulose-degrading enzymes including cellulases, hemicellulases and glycoside hydrolases were highly upregulated when cysteine was added to the growth medium. In particular, the enzymes that convert cellulose into cellobiose appear to be upregulated. This study could increase knowledge of lignocellulose bioconversion pathways and fungal genetics. CONCLUSIONS: Transcriptome and proteome analyses’ results indicated that cysteine could significantly promote the secretion of lignocellulosic enzymes of an efficient lignocellulosic decomposing strain, A. fumigatus Z5. The possible reason for these results is that Z5 preferred to use amino acids such as cysteine to adapt to the external environment through upregulating carbon-related metabolism pathways. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-018-1350-2) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6318881 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-63188812019-01-08 Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles Miao, Jiaxi Wang, Mengmeng Ma, Lei Li, Tuo Huang, Qiwei Liu, Dongyang Shen, Qirong Biotechnol Biofuels Research BACKGROUND: As a ubiquitous filamentous fungal, Aspergillus spp. play a critical role in lignocellulose degradation, which was also defined as considerable cell factories for organic acids and industrially relevant enzymes producer. Nevertheless, the production of various extracellular enzymes can be influenced by different factors including nitrogen source, carbon source, cultivation temperature, and initial pH value. Thus, this study aims to reveal how amino acids affect the decomposition of lignocellulose by Aspergillus fumigatus Z5 through transcriptional and proteomics methods. RESULTS: The activities of several lignocellulosic enzymes secreted by A. fumigatus Z5 adding with cysteine, methionine, and ammonium sulfate were determined with the chromatometry method. The peak of endo-glucanase (7.33 ± 0.03 U mL(−1)), exo-glucanase (10.50 ± 0.07 U mL(−1)), β-glucosidase (21.50 ± 0.22 U mL(−1)), and xylanase (76.43 ± 0.71 U mL(−1)) were all obtained in the Cys treatment. The secretomes of A. fumigatus Z5 under different treatments were also identified by LC–MS/MS, and 227, 256 and 159 different proteins were identified in the treatments of Cys, Met, and CK (Control, treatment with ammonium sulfate as the sole nitrogen source), respectively. Correlation analysis results of transcriptome and proteome data with fermentation profiles showed that most of the cellulose-degrading enzymes including cellulases, hemicellulases and glycoside hydrolases were highly upregulated when cysteine was added to the growth medium. In particular, the enzymes that convert cellulose into cellobiose appear to be upregulated. This study could increase knowledge of lignocellulose bioconversion pathways and fungal genetics. CONCLUSIONS: Transcriptome and proteome analyses’ results indicated that cysteine could significantly promote the secretion of lignocellulosic enzymes of an efficient lignocellulosic decomposing strain, A. fumigatus Z5. The possible reason for these results is that Z5 preferred to use amino acids such as cysteine to adapt to the external environment through upregulating carbon-related metabolism pathways. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-018-1350-2) contains supplementary material, which is available to authorized users. BioMed Central 2019-01-04 /pmc/articles/PMC6318881/ /pubmed/30622646 http://dx.doi.org/10.1186/s13068-018-1350-2 Text en © The Author(s) 2019 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 Miao, Jiaxi Wang, Mengmeng Ma, Lei Li, Tuo Huang, Qiwei Liu, Dongyang Shen, Qirong Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles |
title | Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles |
title_full | Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles |
title_fullStr | Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles |
title_full_unstemmed | Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles |
title_short | Effects of amino acids on the lignocellulose degradation by Aspergillus fumigatus Z5: insights into performance, transcriptional, and proteomic profiles |
title_sort | effects of amino acids on the lignocellulose degradation by aspergillus fumigatus z5: insights into performance, transcriptional, and proteomic profiles |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6318881/ https://www.ncbi.nlm.nih.gov/pubmed/30622646 http://dx.doi.org/10.1186/s13068-018-1350-2 |
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