Cargando…
Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production
Sustainable and eco-efficient alternatives for the production of platform chemicals, fuels and chemical building blocks require the development of stable, reusable and recyclable biocatalysts. Here we present a novel concept for the biocatalytic production of 1,5-diaminopentane (DAP, trivial name: c...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5895699/ https://www.ncbi.nlm.nih.gov/pubmed/29643457 http://dx.doi.org/10.1038/s41598-018-24070-2 |
_version_ | 1783313701043961856 |
---|---|
author | Kloss, Ramona Limberg, Michael H. Mackfeld, Ursula Hahn, Doris Grünberger, Alexander Jäger, Vera D. Krauss, Ulrich Oldiges, Marco Pohl, Martina |
author_facet | Kloss, Ramona Limberg, Michael H. Mackfeld, Ursula Hahn, Doris Grünberger, Alexander Jäger, Vera D. Krauss, Ulrich Oldiges, Marco Pohl, Martina |
author_sort | Kloss, Ramona |
collection | PubMed |
description | Sustainable and eco-efficient alternatives for the production of platform chemicals, fuels and chemical building blocks require the development of stable, reusable and recyclable biocatalysts. Here we present a novel concept for the biocatalytic production of 1,5-diaminopentane (DAP, trivial name: cadaverine) using catalytically active inclusion bodies (CatIBs) of the constitutive L-lysine decarboxylase from E. coli (EcLDCc-CatIBs) to process L-lysine-containing culture supernatants from Corynebacterium glutamicum. EcLDCc-CatIBs can easily be produced in E. coli followed by a simple purification protocol yielding up to 43% dry CatIBs per dry cell weight. The stability and recyclability of EcLDCc-CatIBs was demonstrated in (repetitive) batch experiments starting from L-lysine concentrations of 0.1 M and 1 M. EcLDC-CatIBs exhibited great stability under reaction conditions with an estimated half-life of about 54 h. High conversions to DAP of 87–100% were obtained in 30–60 ml batch reactions using approx. 180–300 mg EcLDCc-CatIBs, respectively. This resulted in DAP titres of up to 88.4 g l(−1) and space-time yields of up to 660 g(DAP) l(−1) d(−1) per gram dry EcLDCc-CatIBs. The new process for DAP production can therefore compete with the currently best fermentative process as described in the literature. |
format | Online Article Text |
id | pubmed-5895699 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58956992018-04-20 Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production Kloss, Ramona Limberg, Michael H. Mackfeld, Ursula Hahn, Doris Grünberger, Alexander Jäger, Vera D. Krauss, Ulrich Oldiges, Marco Pohl, Martina Sci Rep Article Sustainable and eco-efficient alternatives for the production of platform chemicals, fuels and chemical building blocks require the development of stable, reusable and recyclable biocatalysts. Here we present a novel concept for the biocatalytic production of 1,5-diaminopentane (DAP, trivial name: cadaverine) using catalytically active inclusion bodies (CatIBs) of the constitutive L-lysine decarboxylase from E. coli (EcLDCc-CatIBs) to process L-lysine-containing culture supernatants from Corynebacterium glutamicum. EcLDCc-CatIBs can easily be produced in E. coli followed by a simple purification protocol yielding up to 43% dry CatIBs per dry cell weight. The stability and recyclability of EcLDCc-CatIBs was demonstrated in (repetitive) batch experiments starting from L-lysine concentrations of 0.1 M and 1 M. EcLDC-CatIBs exhibited great stability under reaction conditions with an estimated half-life of about 54 h. High conversions to DAP of 87–100% were obtained in 30–60 ml batch reactions using approx. 180–300 mg EcLDCc-CatIBs, respectively. This resulted in DAP titres of up to 88.4 g l(−1) and space-time yields of up to 660 g(DAP) l(−1) d(−1) per gram dry EcLDCc-CatIBs. The new process for DAP production can therefore compete with the currently best fermentative process as described in the literature. Nature Publishing Group UK 2018-04-11 /pmc/articles/PMC5895699/ /pubmed/29643457 http://dx.doi.org/10.1038/s41598-018-24070-2 Text en © The Author(s) 2018 Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Kloss, Ramona Limberg, Michael H. Mackfeld, Ursula Hahn, Doris Grünberger, Alexander Jäger, Vera D. Krauss, Ulrich Oldiges, Marco Pohl, Martina Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production |
title | Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production |
title_full | Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production |
title_fullStr | Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production |
title_full_unstemmed | Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production |
title_short | Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production |
title_sort | catalytically active inclusion bodies of l-lysine decarboxylase from e. coli for 1,5-diaminopentane production |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5895699/ https://www.ncbi.nlm.nih.gov/pubmed/29643457 http://dx.doi.org/10.1038/s41598-018-24070-2 |
work_keys_str_mv | AT klossramona catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT limbergmichaelh catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT mackfeldursula catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT hahndoris catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT grunbergeralexander catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT jagerverad catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT kraussulrich catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT oldigesmarco catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction AT pohlmartina catalyticallyactiveinclusionbodiesofllysinedecarboxylasefromecolifor15diaminopentaneproduction |