Bio-based production of monomers and polymers by metabolically engineered microorganisms

Chung, Hayoung; Yang, Jung Eun; Ha, Ji Yeon; Chae, Tong Un; Shin, Jae Ho; Gustavsson, Martin; Lee, Sang Yup

doi:10.1016/j.copbio.2015.07.003

Cited by 129 publications

(72 citation statements)

References 63 publications

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“…Both 1,4-BDO and 1,6-HDO are important commodity chemicals, with high annual demand, that are produced on a large scale of several million tons per year and are widely used for the production of plastics, polyurethanes and pharmaceuticals [2, 4]. In addition, 1,6-HDO can be converted by amination to 1,6-hexamethylenediamine, another important chemical in the polymer industry [8]. The recently demonstrated biosynthetic pathway from glucose through succinate to 1,4-BDO proceeds via 4-HB, which is then converted to 1,4-BDO using three different enzymes [41].…”

Section: Resultsmentioning

confidence: 99%

“…Bio-based production of organic acids has become a fast-moving field due to the recent advances in genome sequencing, metabolic engineering and synthetic biology [6, 7]. Bifunctional carboxylic acids (di-acids, hydroxy-acids, oxo-acids, and amino-acids) are of special interest in the polymer industry because they are components of different bio-based polymers (polyesters and polyamides) [2, 8]. In industrially important microorganisms, bifunctional carboxylic acids (succinate, malate, fumarate, 2-oxoglutarate, etc.)…”

Section: Introductionmentioning

confidence: 99%

“…are intermediates of the central carbon metabolism representing potential starting points for the biosynthesis of various chemicals. The growing bio-based production of organic acids from renewable sources makes them attractive substrates for a range of alternative products [5, 8]. Therefore, biocatalytic reduction of carboxylic acids is gaining importance [9].…”

Section: Introductionmentioning

confidence: 99%

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Exploring Bacterial Carboxylate Reductases for the Reduction of Bifunctional Carboxylic Acids

Khusnutdinova

Flick

Popović

et al. 2017

Biotechnology Journal

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Carboxylic acid reductases (CARs) selectively reduce carboxylic acids to aldehydes using ATP and NADPH as cofactors under mild conditions. Although CARs have attracted significant interest, only a few enzymes have been characterized to date, whereas the vast majority of CARs have yet to be examined. Herein we report that 12 bacterial CARs reduced a broad range of bifunctional carboxylic acids containing oxo-, hydroxy-, amino-, or second carboxyl groups with several enzymes showing activity toward 4-hydroxybutanoic (4-HB) and adipic acids. These CARs exhibited significant reductase activity against substrates whose second functional group is separated from the carboxylate by at least three carbons with both carboxylate groups being reduced in dicarboxylic acids. Purified CARs supplemented with cofactor regenerating systems (for ATP and NADPH), an inorganic pyrophosphatase, and an aldo-keto reductase catalyzed a high conversion (50–76%) of 4-HB to 1,4-butanediol (1,4-BDO) and adipic acid to 1,6-hexanediol (1,6-HDO). Likewise, Escherichia coli strains expressing eight different CARs efficiently reduced 4-HB to 1,4-BDO with 50–95% conversion, whereas adipic acid was reduced to a mixture of 6-hydroxyhexanoic acid (6-HHA) and 1,6-HDO. Thus, our results illustrate the broad biochemical diversity of bacterial CARs and their compatibility with other enzymes for applications in biocatalysis.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Exploring Bacterial Carboxylate Reductases for the Reduction of Bifunctional Carboxylic Acids

Khusnutdinova

Flick

Popović

et al. 2017

Biotechnology Journal

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“…Avoiding product re-uptake and/or product degradation is often used in strain optimization for biotechnological processes (Becker et al 2015;Becker and Wittmann 2012;Chung et al 2015;Rodriguez et al 2014) and was important to improve putrescine production by recombinant E. coli (Qian et al 2009). Indeed, it has been reported that the GABA concentration decreased when GABA was produced by direct glutamate decarboxylation (Okai et al 2014;Takahashi et al 2012).…”

Section: Discussionmentioning

confidence: 99%

A new metabolic route for the production of gamma-aminobutyric acid by Corynebacterium glutamicum from glucose

Jorge

Leggewie²,

Wendisch

2016

Amino Acids

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Gamma-aminobutyric acid (GABA), a non-protein amino acid widespread in nature, is a component of pharmaceuticals, foods, and the biodegradable plastic polyamide 4. Corynebacterium glutamicum shows great potential for the production of GABA from glucose. GABA added to the growth medium hardly affected growth of C. glutamicum, since a half-inhibitory concentration of 1.1 M GABA was determined. As alternative to GABA production by glutamate decarboxylation, a new route for the production of GABA via putrescine was established in C. glutamicum. A putrescine-producing recombinant C. glutamicum strain was converted into a GABA producing strain by heterologous expression of putrescine transaminase (PatA) and gamma-aminobutyraldehyde dehydrogenase (PatD) genes from Escherichia coli. The resultant strain produced 5.3 ± 0.1 g L of GABA. GABA production was improved further by adjusting the concentration of nitrogen in the culture medium, by avoiding the formation of the by-product N-acetylputrescine and by deletion of the genes for GABA catabolism and GABA re-uptake. GABA accumulation by this strain was increased by 51 % to 8.0 ± 0.3 g L, and the volumetric productivity was increased to 0.31 g L h; the highest volumetric productivity reported so far for fermentative production of GABA from glucose in shake flasks was achieved.

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“…LCDCA monomers have a much higher value than regular free fatty acids. These building block monomers are used to make various polyamides, polyester and, polyurethanes [3] in the bio-plastic and coating industries. Their use enables the synthesis of various novel polymers with enhanced Multiple-copy integration of YlALK5 using zeta based integrative vector pINA1291(this strain was selected after screening of 10-20 transformants for their growth and production capacities)…”

Section: Introductionmentioning

confidence: 99%

Combinatorial Engineering of Yarrowia lipolytica as a Promising Cell Biorefinery Platform for the de novo Production of Multi-Purpose Long Chain Dicarboxylic Acids

2017

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This proof-of-concept study establishes Yarrowia lipolytica (Y. lipolytica) as a whole cell factory for the de novo production of long chain dicarboxylic acid (LCDCA-16 and 18) using glycerol as the sole source of carbon. Modification of the fatty acid metabolism pathway enabled creating a pool of fatty acids in a β-oxidation deficient strain. We then selectively upregulated the native fatty acid ω-oxidation pathway for the enhanced terminal oxidation of the endogenous fatty acid precursors. Nitrogen-limiting conditions and leucine supplementation were employed to induce fatty acid biosynthesis in an engineered Leu -modified strain. Our genetic engineering strategy allowed a minimum production of 330 mg/L LCDCAs in shake flask. Scale up to a 1-L bioreactor increased the titer to 3.49 g/L. Our engineered yeast also produced citric acid as a major by-product at a titer of 39.2 g/L. These results provide basis for developing Y. lipolytica as a safe biorefinery platform for the sustainable production of high-value LCDCAs from non-oily feedstock.

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Bio-based production of monomers and polymers by metabolically engineered microorganisms

Cited by 129 publications

References 63 publications

Exploring Bacterial Carboxylate Reductases for the Reduction of Bifunctional Carboxylic Acids

Exploring Bacterial Carboxylate Reductases for the Reduction of Bifunctional Carboxylic Acids

A new metabolic route for the production of gamma-aminobutyric acid by Corynebacterium glutamicum from glucose

Combinatorial Engineering of Yarrowia lipolytica as a Promising Cell Biorefinery Platform for the de novo Production of Multi-Purpose Long Chain Dicarboxylic Acids

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