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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...

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Detalles Bibliográficos
Autores principales: Kloss, Ramona, Limberg, Michael H., Mackfeld, Ursula, Hahn, Doris, Grünberger, Alexander, Jäger, Vera D., Krauss, Ulrich, Oldiges, Marco, Pohl, Martina
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
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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.
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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
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