Efficient 3-hydroxypropionic acid production from glycerol by metabolically engineered Klebsiella pneumoniae

Jiang, Jiaqi; Huang, Bing; Wu, Hui; Li, Zhimin; Ye, Qin

doi:10.1186/s40643-018-0218-4

Cited by 15 publications

(8 citation statements)

References 28 publications

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“…Although acetate production was not completely abolished, they did manage to reduce it from 163 mM (at 400 rpm) to only 80 mM (at 600 rpm; Ko et al, 2017). Recently, a production of 61.9 g/L 3-HP with a yield of 0.58 mol 3−HP /mol glycerol in 38 h in a 5 L bioreactor operated in fed-batch mode by using an engineered K. pneumoniae strain was reported (Jiang et al, 2018). The aeration rate was reduced to half of the initial rate once the cell biomass OD reached close to the maximum value.…”

Section: Process Engineering For Optimizing 3-hp Productionmentioning

confidence: 99%

Production of 3-Hydroxypropanoic Acid From Glycerol by Metabolically Engineered Bacteria

Jers

Kalantari

Garg

et al. 2019

Front. Bioeng. Biotechnol.

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3-hydroxypropanoic acid (3-HP) is a valuable platform chemical with a high demand in the global market. 3-HP can be produced from various renewable resources. It is used as a precursor in industrial production of a number of chemicals, such as acrylic acid and its many derivatives. In its polymerized form, 3-HP can be used in bioplastic production. Several microbes naturally possess the biosynthetic pathways for production of 3-HP, and a number of these pathways have been introduced in some widely used cell factories, such as Escherichia coli and Saccharomyces cerevisiae . Latest advances in the field of metabolic engineering and synthetic biology have led to more efficient methods for bio-production of 3-HP. These include new approaches for introducing heterologous pathways, precise control of gene expression, rational enzyme engineering, redirecting the carbon flux based on in silico predictions using genome scale metabolic models, as well as optimizing fermentation conditions. Despite the fact that the production of 3-HP has been extensively explored in established industrially relevant cell factories, the current production processes have not yet reached the levels required for industrial exploitation. In this review, we explore the state of the art in 3-HP bio-production, comparing the yields and titers achieved in different microbial cell factories and we discuss possible methodologies that could make the final step toward industrially relevant cell factories.

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Section: Process Engineering For Optimizing 3-hp Productionmentioning

confidence: 99%

Production of 3-Hydroxypropanoic Acid From Glycerol by Metabolically Engineered Bacteria

Jers

Kalantari

Garg

et al. 2019

Front. Bioeng. Biotechnol.

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“…Nevertheless, due to the global food shortage and increase of food price, non-food based substrates, such as crude glycerol, methane, methanol and syngas, were developed as alternative substrates in bio-based industry [7–11]. Acetic acid, a cost-effective non-food based feedstock, can be generated from a variety of cheap sources via chemical or biological ways.…”

Section: Introductionmentioning

confidence: 99%

Metabolic engineering of Escherichia coli carrying the hybrid acetone-biosynthesis pathway for efficient acetone biosynthesis from acetate

et al. 2019

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BackgroundThe shortage of food based feedstocks has been one of the stumbling blocks in industrial biomanufacturing. The acetone bioproduction from the traditional acetone–butanol–ethanol fermentation is limited by the non-specificity of products and competitive utilization of food-based substrates. Using genetically modified Escherichia coli to produce acetone as sole product from the cost-effective non-food based substrates showed great potential to overcome these problems.ResultsA novel acetone biosynthetic pathway were constructed based on genes from Clostridium acetobutylicum (thlA encoding for thiolase, adc encoding for acetoacetate decarboxylase, ctfAB encoding for coenzyme A transferase) and Escherichia coli MG1655 (atoB encoding acetyl-CoA acetyltransferase, atoDA encoding for acetyl-CoA: acetoacetyl-CoA transferase subunit α and β). Among these constructs, one recombinant MG1655 derivative containing the hybrid pathway consisting of thlA, atoDA, and adc, produced the highest level of acetone from acetate. Reducing the gluconeogenesis pathway had little effect on acetone production, while blocking the TCA cycle by knocking out the icdA gene enhanced the yield of acetone significantly. As a result, acetone concentration increased up to 113.18 mM in 24 h by the resting cell culture coupling with gas-stripping methods.ConclusionsAn engineered E. coli strain with optimized hybrid acetone biosynthetic pathway can utilize acetate as substrate efficiently to synthesize acetone without other non-gas byproducts. It provides a potential method for industrial biomanufacturing of acetone by engineered E. coli strains from non-food based substrate.Electronic supplementary materialThe online version of this article (10.1186/s12934-019-1054-8) contains supplementary material, which is available to authorized users.

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“…In previous studies, the most studied biological approach for 3-HP production is fermentation employing engineered Klebsiella pneumoniae or E. coli (50)(51)(52)(53). For example, 3-HP has been produced in the highest titer of 83.8 g/liter and an STY of 28 g liter Ϫ1 day Ϫ1 in K. pneumoniae (51).…”

Section: Discussionmentioning

confidence: 99%

Efficient Synthesis of Methyl 3-Acetoxypropionate by a Newly Identified Baeyer-Villiger Monooxygenase

Liu

et al. 2019

Appl Environ Microbiol

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Baeyer-Villiger monooxygenases (BVMOs) are an emerging class of promising biocatalysts for the oxidation of ketones to prepare corresponding esters or lactones. Although many BVMOs have been reported, the development of highly efficient enzymes for use in industrial applications is desirable. In this work, we identified a BVMO from Rhodococcus pyridinivorans (BVMO Rp ) with a high affinity toward aliphatic methyl ketones (K m Ͻ 3.0 M). The enzyme was highly soluble and relatively stable, with a half-life of 23 h at 30°C and pH 7.5. The most effective substrate discovered so far is 2-hexanone (k cat ϭ 2.1 s Ϫ1 ; K m ϭ 1.5 M). Furthermore, BVMO Rp exhibited excellent regioselectivity toward most aliphatic ketones, preferentially forming typical (i.e., normal) products. Using the newly identified BVMO Rp as the catalyst, a high concentration (26.0 g/liter; 200 mM) of methyl levulinate was completely converted to methyl 3-acetoxypropionate after 4 h, with a space-time yield of 5.4 g liter Ϫ1 h Ϫ1 . Thus, BVMO Rp is a promising biocatalyst for the synthesis of 3-hydroxypropionate from readily available biobased levulinate to replace the conventional fermentation. IMPORTANCE BVMOs are emerging as a green alternative to traditional oxidants in the BV oxidation of ketones. Although many BVMOs are discovered and used in organic synthesis, few are really applied in industry, especially in the case of aliphatic ketones. Herein, a highly soluble and relatively stable monooxygenase from Rhodococcus pyridinivorans (BVMO Rp ) was identified with high activity and excellent regioselectivity toward most aliphatic ketones. BVMO Rp possesses unusually high substrate loading during the catalysis of the oxidation of biobased methyl levulinate to 3-hydroxypropionic acid derivatives. This study indicates that the synthesis of 3-hydroxypropionate from readily available biobased levulinate by BVMO Rp -catalyzed oxidation holds great promise to replace traditional fermentation.

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Efficient 3-hydroxypropionic acid production from glycerol by metabolically engineered Klebsiella pneumoniae

Cited by 15 publications

References 28 publications

Production of 3-Hydroxypropanoic Acid From Glycerol by Metabolically Engineered Bacteria

Production of 3-Hydroxypropanoic Acid From Glycerol by Metabolically Engineered Bacteria

Metabolic engineering of Escherichia coli carrying the hybrid acetone-biosynthesis pathway for efficient acetone biosynthesis from acetate

Efficient Synthesis of Methyl 3-Acetoxypropionate by a Newly Identified Baeyer-Villiger Monooxygenase

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