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Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.
- Source :
-
Scientific reports [Sci Rep] 2018 Apr 11; Vol. 8 (1), pp. 5856. Date of Electronic Publication: 2018 Apr 11. - Publication Year :
- 2018
-
Abstract
- 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 <superscript>-1</superscript> and space-time yields of up to 660 g <subscript>DAP</subscript> l <superscript>-1</superscript> d <superscript>-1</superscript> 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.
- Subjects :
- Batch Cell Culture Techniques methods
Biocatalysis
Bioreactors microbiology
Carboxy-Lyases genetics
Carboxy-Lyases isolation & purification
Corynebacterium glutamicum metabolism
Escherichia coli genetics
Escherichia coli Proteins genetics
Escherichia coli Proteins isolation & purification
Lysine metabolism
Metabolic Engineering methods
Recombinant Proteins genetics
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Cadaverine biosynthesis
Carboxy-Lyases metabolism
Escherichia coli enzymology
Escherichia coli Proteins metabolism
Inclusion Bodies enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 8
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 29643457
- Full Text :
- https://doi.org/10.1038/s41598-018-24070-2