High-level l-lysine bioconversion into cadaverine with enhanced productivity using engineered Escherichia coli whole-cell biocatalyst

Leong, Yoong Kit; Chen, Chien-Heng; Huang, Shih-Fang; Lin, Hung‐Yi; Li, Shengfeng; Ng, I‐Son; Chang, Jo‐Shu

doi:10.1016/j.bej.2020.107547

Cited by 20 publications

(7 citation statements)

References 20 publications

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“…The lysine consumption rate was quite comparable to the approach that harnessed the lysogenic system to produce DAP in our previous report. 21 By using the portable and robust PDT7m system, we could further speculate that lysine decarboxylase is not toxic to different strains; thus, a similar lysine conversion was observed among different strains.…”

Section: ■ Results and Discussionmentioning

confidence: 83%

Tailoring Genetic Elements of the Plasmid-Driven T7 System for Stable and Robust One-Step Cloning and Protein Expression in Broad Escherichia coli

Tan

Hsiang

2021

ACS Synth. Biol.

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The plasmid-driven T7 system (PDT7) is a flexible approach to trigger protein overexpression; however, most of the reported PDT7 rely on many auxiliary elements or inducible systems to attenuate the toxicity from the orthogonality of the T7 system, which limits its application as the one-step cloning and protein expression system. In this study, we developed a stable and robust PDT7 via tailoring the genetic elements. By error-prone mutagenesis, a mutated T7RNAP with TTTT insertion conferred a trace but enough amount of T7RNAP for stable and efficient PDT7, denoted as PDT7m. The replication origin was kept at the same level, while the ribosome binding site (RBS) of the T7 promoter was the most contributing factor, thus enhancing the protein expression twofold using PDT7m. For application as a host-independent screening platform, both constitutive and IPTG-inducible PDT7m were constructed. It was found that each strain harnessed different IPTG inducibilities for tailor-made strain selection. Constitutive PDT7m was successfully used to express the homologous protein (i.e., lysine decarboxylase) or heterologous protein (i.e., carbonic anhydrase, CA) as a one-step cloning and protein expression tool to select the best strain for cadaverine (DAP) or CA production, respectively. Additionally, PDT7m is compatible with the pET system for coproduction of DAP and CA simultaneously. Finally, PDT7m was used for in vivo high-end chemical production of aminolevulinic acid (ALA), in which addition of the T7 terminator successfully enhanced 340% ALA titer, thus paving the way to rapidly and effectively screening the superior strain as a cell factory.

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Section: ■ Results and Discussionmentioning

confidence: 83%

Tailoring Genetic Elements of the Plasmid-Driven T7 System for Stable and Robust One-Step Cloning and Protein Expression in Broad Escherichia coli

Tan

Hsiang

2021

ACS Synth. Biol.

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“…After investigating the initial pH, buffer concentration, biocatalyst concentration, l -lysine concentrations, and PLP concentration for E. coli BL21(DE3) (pET-28a(+)-cadA), the whole-cell conversion showed an outstanding efficiency and can produce 144.74 g L −1 cadaverine with the productivity of 72.37 g L −1 h −1 . 76 Kim et al 104 also statistically optimized the cadaverine production system and found that the H. alvei strain had the highest conversion rate under the optimum conditions (125.1 mM l -lysine, 71.5 g L −1 acetone at 35.2 °C for 8.4 h). Kim et al 106 have developed an advanced expression system for E. coli XL1-Blue (pKE112-HaLdcC) which can produce 123.2 g L −1 cadaverine after 12 h of reaction without the addition of the inducer IPTG and co-factor PLP.…”

Section: Process Intensification For Cadaverine Productionmentioning

confidence: 99%

Green chemical and biological synthesis of cadaverine: recent development and challenges

Huang

Zhan-ling

et al. 2021

RSC Adv.

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“…Because C. glutamicum lacks the key enzymes to synthesize cadaverine, whole-cell biocatalysis is mainly dominated by E. coli as detailed in Table 2, in which lysine decarboxylase is expressed for efficient lysine bioconversion into cadaverine. 62,68,69,73 The activity of lysine decarboxylase is closely related to the pH of reaction systems. In the range of pH 5−8, it shows higher enzymatic activity, but the reaction system pH increases significantly with the increasing of cadaverine concentration, resulting in lysine decarboxylase deactivation.…”

Section: Bacteriamentioning

confidence: 99%

“…glutamicum lacks the key enzymes to synthesize cadaverine, whole-cell biocatalysis is mainly dominated by E. coli as detailed in Table , in which lysine decarboxylase is expressed for efficient lysine bioconversion into cadaverine. ,,, The activity of lysine decarboxylase is closely related to the pH of reaction systems. In the range of pH 5–8, it shows higher enzymatic activity, but the reaction system pH increases significantly with the increasing of cadaverine concentration, resulting in lysine decarboxylase deactivation. , To maintain pH stabilization in fermentation broth, a green, novel, and efficient in situ pH control method is proposed by using CO 2 self-released from decarboxylation instead of strong acids via a sealing reactor for cadaverine production (Figure ).…”

Section: Biocatalytic Production Of Cadaverinementioning

confidence: 99%

Cellular Engineering and Biocatalysis Strategies toward Sustainable Cadaverine Production: State of the Art and Perspectives

Liu

et al. 2021

ACS Sustainable Chem. Eng.

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Cadaverine, a diamine monomer, broadly exists in living organisms participating in metabolism processes. As a promising substitute of 1,6-diaminohexane, cadaverine can polymerize with dicarboxylic acids and yield biobased polyamides, polyamide (PA) 5×, showing ecofriendly and excellent mechanical properties in the fields of electronics, automobile, material, storage, and others. Due to the increasing attentions on environment problems, biopolyamide is expected to be an ideal and green material to substitute conventional chemistry polyamide. This review summarizes the properties, potential applications, and production strategies about cadaverine and mainly focuses on the recent developments by cellular engineering Escherichia coli and Corynebacterium glutamicum as main workhorses. In addition, the key enzyme lysine decarboxylase decorated by means of immobilization and mutation to efficiently catalyze lysine and its catalysis mechanisms are also discussed. In order to achieve industrial applications, the indispensable steps of separation and purification are described as well and perspectives for cadaverine manufacturing from renewable resources are further provided.

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High-level l-lysine bioconversion into cadaverine with enhanced productivity using engineered Escherichia coli whole-cell biocatalyst

Cited by 20 publications

References 20 publications

Tailoring Genetic Elements of the Plasmid-Driven T7 System for Stable and Robust One-Step Cloning and Protein Expression in Broad Escherichia coli

Tailoring Genetic Elements of the Plasmid-Driven T7 System for Stable and Robust One-Step Cloning and Protein Expression in Broad Escherichia coli

Green chemical and biological synthesis of cadaverine: recent development and challenges

Cellular Engineering and Biocatalysis Strategies toward Sustainable Cadaverine Production: State of the Art and Perspectives

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