Improved cadaverine production from mutant <i>Klebsiella oxytoca</i> lysine decarboxylase

Li, Naiqiang; Chou, Howard H.; Xu, Yan

doi:10.1002/elsc.201500037

Cited by 9 publications

(2 citation statements)

References 20 publications

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“…The oxidation and decarboxylation of lysine lead to 5-aminovaleric acid and 5-diaminopentane, respectively. The former reaction proceeds with lysine oxidase, while the latter with lysine decarboxylase [ 100 – 102 ]. The potential application of 5-aminovaleric acid and 5-diaminopentane is their use for production of nylon and polyamide.…”

Section: Bio-based Production Of Fuels and Chemicals From Amino Acidsmentioning

confidence: 99%

Biorefining of protein waste for production of sustainable fuels and chemicals

Chen

et al. 2018

Biotechnol Biofuels

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To mitigate the climate change caused by CO2 emission, the global incentive to the low-carbon alternatives as replacement of fossil fuel-derived products continuously expands the need for renewable feedstock. There will be accompanied by the generation of enormous protein waste as a result. The economical viability of the biorefinery platform can be realized once the surplus protein waste is recycled in a circular economy scenario. In this context, the present review focuses on the current development of biotechnology with the emphasis on biotransformation and metabolic engineering to refine protein-derived amino acids for production of fuels and chemicals. Its scope starts with the explosion of potential feedstock sources rich in protein waste. The availability of techniques is applied for purification and hydrolysis of various feedstock proteins to amino acids. Useful lessons are leaned from the microbial catabolism of amino acids and lay a foundation for the development of the protein-based biotechnology. At last, the future perspective of the biorefinery scheme based on protein waste is discussed associated with remarks on possible solutions to overcome the technical bottlenecks.

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Section: Bio-based Production Of Fuels and Chemicals From Amino Acidsmentioning

confidence: 99%

Biorefining of protein waste for production of sustainable fuels and chemicals

Chen

et al. 2018

Biotechnol Biofuels

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“…Although the synthetic process yields 1,5-pentanediamine at a relatively low cost, the method uses non-renewable fossil fuels and produces serious pollutants in the environment [ 10 ]. Microbial fermentation uses renewable resources but is not broadly applicable in producing 1,5-pentanediamine because of the low efficiency of LDC [ 11 ]. LDC activity sharply reduces when the pH of the medium increases from the consumption of a proton [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and molecular characterization of a metagenome-derived L-lysine decarboxylase gene from subtropical soil microorganisms

Gao

Zhao

et al. 2017

PLoS ONE

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L-lysine decarboxylase (LDC, EC 4.1.1.18) is a key enzyme in the decarboxylation of L-lysine to 1,5-pentanediamine and efficiently contributes significance to biosynthetic capability. Metagenomic technology is a shortcut approach used to obtain new genes from uncultured microorganisms. In this study, a subtropical soil metagenomic library was constructed, and a putative LDC gene named ldc1E was isolated by function-based screening strategy through the indication of pH change by L-lysine decarboxylation. Amino acid sequence comparison and homology modeling indicated the close relation between Ldc1E and other putative LDCs. Multiple sequence alignment analysis revealed that Ldc1E contained a highly conserved motif Ser-X-His-Lys (Pxl), and molecular docking results showed that this motif was located in the active site and could combine with the cofactor pyridoxal 5′-phosphate. The ldc1E gene was subcloned into the pET-30a(+) vector and highly expressed in Escherichia coli BL21 (DE3) pLysS. The recombinant protein was purified to homogeneity. The maximum activity of Ldc1E occurred at pH 6.5 and 40°C using L-lysine monohydrochloride as the substrate. Recombinant Ldc1E had apparent Km, kcat, and kcat/Km values of 1.08±0.16 mM, 5.09±0.63 s−1, and 4.73×103 s−1 M−1, respectively. The specific activity of Ldc1E was 1.53±0.06 U mg−1 protein. Identifying a metagenome-derived LDC gene provided a rational reference for further gene modifications in industrial applications.

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Pentamethylenediamine

2023

Pathway Design for Industrial Fermentation

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Improved cadaverine production from mutant Klebsiella oxytoca lysine decarboxylase

Cited by 9 publications

References 20 publications

Biorefining of protein waste for production of sustainable fuels and chemicals

Biorefining of protein waste for production of sustainable fuels and chemicals

Identification and molecular characterization of a metagenome-derived L-lysine decarboxylase gene from subtropical soil microorganisms

Pentamethylenediamine

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