Engineered biosynthesis of medium-chain esters in Escherichia coli

Tai, Yi Shu; Xiong, Mei; Zhang, Kechun

doi:10.1016/j.ymben.2014.10.004

Cited by 75 publications

(95 citation statements)

References 57 publications

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“…Alcohol acyltransferase (AAT) plays a major role in the biosynthesis of acetate esters in plant and yeast. An alcohol acetyltransferase (ATF1) from S. cerevisiae was previously discovered and shown to exhibit a broadly substrate specificity for short‐chain alcohols, fatty alcohols and 2‐PE (Guo et al., ; Rodriguez, Tashiro, & Atsumi, ; Saerens, Delvaux, Verstrepen, & Thevelein, ; Tai, Xiong, & Zhang, ; Yoshimoto, Fukushige, Yonezawa, & Sone, ). After succeeding in demonstrated the biosynthesis of 2‐PE in E. coli , we further generated a 2‐PEAc biosynthetic pathway in this 2‐PE‐producing strain by overexpressing ATF1 for the subsequent esterification 2‐PE to 2‐PEAc.…”

Section: Resultsmentioning

confidence: 99%

“…This result suggests that phenylacetaldehyde is not a good substrate for ADH6. Zhang, 2015;Yoshimoto, Fukushige, Yonezawa, & Sone, 2002). After succeeding in demonstrated the biosynthesis of 2-PE in E. coli, we further generated a 2-PEAc biosynthetic pathway in this 2-PE-producing strain by overexpressing ATF1 for the subsequent esterification 2-PE to 2-PEAc.…”

Section: Construction Of 2-pe Biosynthetic Pathway In Escherichia Colimentioning

confidence: 99%

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Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

et al. 2017

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In order to meet the need of consumer preferences for natural flavor compounds, microbial synthesis method has become a very attractive alternative to the chemical production. The 2‐phenylethanol (2‐PE) and its ester 2‐phenylethylacetate (2‐PEAc) are two extremely important flavor compounds with a rose‐like odor. In recent years, Escherichia coli and yeast have been metabolically engineered to produce 2‐PE. However, a metabolic engineering approach for 2‐PEAc production is rare. Here, we designed and expressed a 2‐PEAc biosynthetic pathway in E. coli. This pathway comprised four steps: aminotransferase (ARO8) for transamination of L‐phenylalanine to phenylpyruvate, 2‐keto acid decarboxylase KDC for the decarboxylation of the phenylpyruvate to phenylacetaldehyde, aldehyde reductase YjgB for the reduction of phenylacetaldehyde to 2‐PE, alcohol acetyltransferase ATF1 for the esterification of 2‐PE to 2‐PEAc. Using the engineered E. coli strain for shake flasks cultivation with 1 g/L L‐phenylalanine, we achieved co‐production of 268 mg/L 2‐PEAc and 277 mg/L 2‐PE. Our results suggest that approximately 65% of L‐phenylalanine was utilized toward 2‐PEAc and 2‐PE biosynthesis and thus demonstrate potential industrial applicability of this microbial platform.

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Section: Resultsmentioning

confidence: 99%

Section: Construction Of 2-pe Biosynthetic Pathway In Escherichia Colimentioning

confidence: 99%

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

et al. 2017

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“…In a separate study, this strategy was applied in a 1.3 L bioreactor coupled with in situ product removal. This system allowed for 36 g/L IBA, representing 42% of the theoretical yield (Table 1) [36].…”

Section: Estersmentioning

confidence: 99%

Microbial production of scent and flavor compounds

Carroll

Desai

Atsumi

2016

Current Opinion in Biotechnology

118

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“…These enzymes catalyze the formation of acetate esters from the two substrates: an alcohol and acetyl-CoA. Alcohol acetyltransferase (ATF1 or ATF2) from S. cerevisiae was earlier discovered and shown to exhibit a broad substrate specificity for short-chain alcohols (Saerens et al 2010;Tai et al 2015;Yoshimoto et al 2002). Recently, recombinant E. coli was engineered to produce volatile esters based on alcohol acetyltransferase (Layton and Trinh 2014;Rodriguez et al 2014;Tai et al 2015).…”

Section: Introductionmentioning

confidence: 99%

“…Alcohol acetyltransferase (ATF1 or ATF2) from S. cerevisiae was earlier discovered and shown to exhibit a broad substrate specificity for short-chain alcohols (Saerens et al 2010;Tai et al 2015;Yoshimoto et al 2002). Recently, recombinant E. coli was engineered to produce volatile esters based on alcohol acetyltransferase (Layton and Trinh 2014;Rodriguez et al 2014;Tai et al 2015). Rodriguez et al further reported the biosynthesis of tetradecyl acetate (Also known as tetradecanol acetate ester) from myristic acid precursor (Rodriguez et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Metabolic engineering of Escherichia coli for production of biodiesel from fatty alcohols and acetyl-CoA

Guo

Pan

2015

Appl Microbiol Biotechnol

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Microbial production of biodiesel from renewable feedstock has attracted intensive attention. Biodiesel is known to be produced from short-chain alcohols and fatty acyl-CoAs through the expression of wax ester synthase/fatty acyl-CoA: diacylglycerol acyltransferase that catalyzes the esterification of short-chain alcohols and fatty acyl-CoAs. Here, we engineered Escherichia coli to produce various fatty alcohol acetate esters, which depend on the expression of Saccharomyces cerevisiae alcohol acetyltransferase ATF1 that catalyzes the esterification of fatty alcohols and acetyl-CoA. The fatty acid biosynthetic pathways generate fatty acyl-ACPs, fatty acyl-CoAs, or fatty acids, which can be converted to fatty alcohols by fatty acyl-CoA reductase, fatty acyl-ACP reductase, or carboxylic acid reductase, respectively. This study showed the biosynthesis of biodiesel from three fatty acid biosynthetic pathway intermediates.

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Engineered biosynthesis of medium-chain esters in Escherichia coli

Cited by 75 publications

References 57 publications

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

Metabolic engineering of Escherichia coli for production of 2‐Phenylethylacetate from L‐phenylalanine

Microbial production of scent and flavor compounds

Metabolic engineering of Escherichia coli for production of biodiesel from fatty alcohols and acetyl-CoA

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