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High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase
BACKGROUND: Agmatine is a member of biogenic amines and is an important medicine which is widely used to regulate body balance and neuroprotective effects. At present, the industrial production of agmatine mainly depends on the chemical method, but it is often accompanied by problems including cumbe...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8805389/ https://www.ncbi.nlm.nih.gov/pubmed/35101042 http://dx.doi.org/10.1186/s12934-022-01742-3 |
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author | Yang, Fengyu Xu, Jiayu Zhu, Yichun Wang, Yi Xu, Meijuan Rao, Zhiming |
author_facet | Yang, Fengyu Xu, Jiayu Zhu, Yichun Wang, Yi Xu, Meijuan Rao, Zhiming |
author_sort | Yang, Fengyu |
collection | PubMed |
description | BACKGROUND: Agmatine is a member of biogenic amines and is an important medicine which is widely used to regulate body balance and neuroprotective effects. At present, the industrial production of agmatine mainly depends on the chemical method, but it is often accompanied by problems including cumbersome processes, harsh reaction conditions, toxic substances production and heavy environmental pollution. Therefore, to tackle the above issues, arginine decarboxylase was overexpressed heterologously and rationally designed in Corynebacterium crenatum to produce agmatine from glucose by one-step fermentation. RESULTS: In this study, we report the development in the Generally Regarded as Safe (GRAS) l-arginine-overproducing C. crenatum for high-titer agmatine biosynthesis through overexpressing arginine decarboxylase based on metabolic engineering. Then, arginine decarboxylase was mutated to release feedback inhibition and improve catalytic activity. Subsequently, the specific enzyme activity and half-inhibitory concentration of I534D mutant were increased 35.7% and 48.1%, respectively. The agmatine production of the whole-cell bioconversion with AGM3 was increased by 19.3% than the AGM2. Finally, 45.26 g/L agmatine with the yield of 0.31 g/g glucose was achieved by one-step fermentation of the engineered C. crenatum with overexpression of speA(I534D). CONCLUSIONS: The engineered C. crenatum strain AGM3 in this work was proved as an efficient microbial cell factory for the industrial fermentative production of agmatine. Based on the insights from this work, further producing other valuable biochemicals derived from l-arginine by Corynebacterium crenatum is feasible. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12934-022-01742-3. |
format | Online Article Text |
id | pubmed-8805389 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-88053892022-02-03 High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase Yang, Fengyu Xu, Jiayu Zhu, Yichun Wang, Yi Xu, Meijuan Rao, Zhiming Microb Cell Fact Research BACKGROUND: Agmatine is a member of biogenic amines and is an important medicine which is widely used to regulate body balance and neuroprotective effects. At present, the industrial production of agmatine mainly depends on the chemical method, but it is often accompanied by problems including cumbersome processes, harsh reaction conditions, toxic substances production and heavy environmental pollution. Therefore, to tackle the above issues, arginine decarboxylase was overexpressed heterologously and rationally designed in Corynebacterium crenatum to produce agmatine from glucose by one-step fermentation. RESULTS: In this study, we report the development in the Generally Regarded as Safe (GRAS) l-arginine-overproducing C. crenatum for high-titer agmatine biosynthesis through overexpressing arginine decarboxylase based on metabolic engineering. Then, arginine decarboxylase was mutated to release feedback inhibition and improve catalytic activity. Subsequently, the specific enzyme activity and half-inhibitory concentration of I534D mutant were increased 35.7% and 48.1%, respectively. The agmatine production of the whole-cell bioconversion with AGM3 was increased by 19.3% than the AGM2. Finally, 45.26 g/L agmatine with the yield of 0.31 g/g glucose was achieved by one-step fermentation of the engineered C. crenatum with overexpression of speA(I534D). CONCLUSIONS: The engineered C. crenatum strain AGM3 in this work was proved as an efficient microbial cell factory for the industrial fermentative production of agmatine. Based on the insights from this work, further producing other valuable biochemicals derived from l-arginine by Corynebacterium crenatum is feasible. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12934-022-01742-3. BioMed Central 2022-01-31 /pmc/articles/PMC8805389/ /pubmed/35101042 http://dx.doi.org/10.1186/s12934-022-01742-3 Text en © The Author(s) 2022 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 Yang, Fengyu Xu, Jiayu Zhu, Yichun Wang, Yi Xu, Meijuan Rao, Zhiming High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
title | High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
title_full | High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
title_fullStr | High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
title_full_unstemmed | High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
title_short | High-level production of the agmatine in engineered Corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
title_sort | high-level production of the agmatine in engineered corynebacterium crenatum with the inhibition-releasing arginine decarboxylase |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8805389/ https://www.ncbi.nlm.nih.gov/pubmed/35101042 http://dx.doi.org/10.1186/s12934-022-01742-3 |
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