Improved 1, 2, 4-butanetriol production from an engineered Escherichia coli by co-expression of different chaperone proteins

@article{Lu2016Improved12,
  title={Improved 1, 2, 4-butanetriol production from an engineered Escherichia coli by co-expression of different chaperone proteins},
  author={Xinyao Lu and Shuying He and H. Zong and Jian Song and Wen Chen and B. Zhuge},
  journal={World Journal of Microbiology and Biotechnology},
  year={2016},
  volume={32},
  pages={1-9}
}
Abstract1, 2, 4-Butanetriol (BT) is a high-value non-natural chemical and has important applications in polymers, medical production and military industry. In the constructed BT biosynthesis pathway from xylose in Escherichia coli, the xylose dehydrogenase (Xdh) and the benzoylformate decarboxylase (MdlC) are heterologous enzymes and the activity of MdlC is the key limiting factor for BT production. In this study, six chaperone protein systems were introduced into the engineered E. coli… Expand
Production of 1,2,4-butanetriol from xylose by Saccharomyces cerevisiae through Fe metabolic engineering.
TLDR
Improvement of the recombinant strain was performed by the screening of optimal 2-ketoacid decarboxylase suitable for 1,2,4-butanetriol production and the enhancement of Fe uptake ability to improve the XylD enzymatic activity. Expand
Optimization of 1,2,4‐butanetriol production from xylose in Saccharomyces cerevisiae by metabolic engineering of NADH/NADPH balance
TLDR
To improve the BT yield in S. cerevisiae by genetic engineering, the amount of the key intermediate 2‐keto‐3‐deoxy‐xylonate as described previously was successfully reduced in 41% by multiple integrations of Lactococcus lactis 2-ketoacid decarboxylase gene kdcA into the yeast genome. Expand
Modification of an engineered Escherichia coli by a combined strategy of deleting branch pathway, fine-tuning xylose isomerase expression, and substituting decarboxylase to improve 1,2,4-butanetriol production.
TLDR
This work provided some effective strategies for improving BT production by balancing the carbon flux redistribution and reducing power regeneration. Expand
Engineering Escherichia coli to grow constitutively on D-xylose using the carbon-efficient Weimberg pathway
TLDR
Escherichia coli is engineered to utilize d-xylose constitutively using the Weimberg pathway, to allow direct production of 2-oxoglutarate without CO2 loss, and offers great potential for use as a new host strain to engineer carbon-efficient production of fuels and chemicals via the WeIMberg pathway. Expand
Co-production of 1,2,4-butantriol and ethanol from lignocellulose hydrolysates.
TLDR
This study provided a novel strategy for BT production from sugarcane bagasse, and demonstrated the potential for making full use of sugarcanes bagasse hydrolysates to co-production value-added products. Expand
Everyone loves an underdog: metabolic engineering of the xylose oxidative pathway in recombinant microorganisms
TLDR
Improving the d-xylose uptake, growth yields, and product titer through several metabolic engineering techniques bring some of these recombinant strains close to industrial viability, but more developments are still needed to optimize the XOP pathway in the host strains, particularly in the minimization of by-product formation. Expand
Engineering of xylose metabolism in Escherichia coli for the production of valuable compounds
TLDR
This review aims to provide relevant and current information about significant advances in the metabolic engineering of d-xylose metabolism in E. coli by focusing on unconventional and synthetic d-Xylose metabolic pathways as several review articles have already discussed the engineering of native d- xylose metabolites. Expand
Genetic engineering modification and fermentation optimization for extracellular production of recombinant proteins using Escherichia coli
TLDR
To improve the secretion efficiency of target proteins, various strategies, including signal peptide optimization, periplasmic leakage, and chaperones co-expression have been developed and these strategies were summarized for the future guidance of extracellular production of recombinant proteins using E. coli. Expand
A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.
TLDR
The structure, function, and role of major E. coli molecular chaperones in recombinant technology such as trigger factor, GroEL, DnaK and ClpB are discussed. Expand
Synthetic and Systems Biology Approach towards Designing Metabolic Bypass and Identifying Novel Enzymes for Cholesterol Lowering Drug Precursor (BTO) Biosynthesis from Crude Glycerol
1, 2, 4-Butanetriol (BTO) is a potential precursor of Cholesterol Lowering Drugs. BTO production is predominantly dependent on chemical conversions at present. Biological route for BTO biosynthesisExpand
...
1
2
...

References

SHOWING 1-10 OF 28 REFERENCES
Direct bioconversion of d-xylose to 1,2,4-butanetriol in an engineered Escherichia coli
TLDR
This is the first report on the direct production of BT from d -xylose by a single microbial host and may serve as a starting point for further metabolic engineering works to increase the titer of BT toward industrial scale viability. Expand
Design and Construction of a Non-Natural Malate to 1,2,4-Butanetriol Pathway Creates Possibility to Produce 1,2,4-Butanetriol from Glucose
TLDR
Following assembly of two functional modules, BT was detected in the fermentation broth upon addition of malate, proving BT can be biosynthesized from malate and suggesting that such novel BT biosynthetic pathway has created the possibility for the production of BT from the cheaper substrate glucose. Expand
Metabolic Engineering of Escherichia coli for the Production of Xylonate
TLDR
The results suggest that the engineered E. coli strain has a promising perspective for large-scale production of xylonate, a valuable chemical for versatile applications. Expand
Improvement of productivity of active horseradish peroxidase in Escherichia coli by coexpression of Dsb proteins.
TLDR
Coexpression of Dsb proteins improves both the cell growth and the productivity of HRP, and coexpression of molecular chaperones did not improve active HRP production. Expand
Microbial synthesis of the energetic material precursor 1,2,4-butanetriol.
TLDR
As a catalytic route to 1,2,4-butanetriol, microbial synthesis avoids the high H2 pressures and elevated temperatures required by catalytic hydrogenation of malic acid. Expand
Functional expression of lipase A from Candida antarctica in Escherichia coli—A prerequisite for high-throughput screening and directed evolution
Abstract We report for the first time the functional and heterologous expression of lipase A from Candida antarctica (CalA) in the cytoplasm of Escherichia coli Origami™ B cells. Expression underExpand
Identification in the mould Hypocrea jecorina of a gene encoding an NADP+: d-xylose dehydrogenase
TLDR
A gene coding for an NADP+-dependent d-xylose dehydrogenase was identified in the mould Hypocrea jecorina (Trichoderma reesei) and a histidine-tagged enzyme was purified and characterized. Expand
Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida.
TLDR
Comparison of the X-ray structures of both enzymes identified two residues in each that were likely to be involved in determining substrate specificity that proved to be a real chimera between PDC and BFD and provided the most interesting result with an almost complete reversal of the stereochemistry of its 2-hydroxypropiophenone product. Expand
Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli
TLDR
Whereas overexpression of TF alone was sufficient to prevent aggregation of endostatin, overexpressive of TF together with GroEL-GroES was more effective for ORP150 and lysozyme, suggesting that TF and GroEL -GroES play synergistic roles in vivo. Expand
Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology.
TLDR
The disaggregation capacity of this bi-chaperone system has now been demonstrated in vitro and in vivo for a wide variety of aggregated proteins and offers a new perspective to increase the solubility of proteins of interest. Expand
...
1
2
3
...