Production of longer-chain alcohols from lignocellulosic biomass: butanol, isopropanol and 2,3-butanediol

López-Contreras, Ana M.; Kuit, Wouter; Siemerink, Marco A. J.; Kengen, Servé W. M.; Springer, Jan; Claassen, P.A.M.

doi:10.1533/9781845699611.5.415

Cited by 20 publications

(16 citation statements)

References 152 publications

(151 reference statements)

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“…In the past, both ABE and IBE fermentations were performed worldwide at industrial scale until they were replaced by petrochemical processes (Jones and Woods 1986; Rogers et al 2006). Many resources are currently being devoted to develop economically-viable fermentation processes based primarly on lignocellulosic biomass hydrolysates as substrates (Dürre 20072008; López-Contreras et al 2010; Green 2011). …”

Section: Introductionmentioning

confidence: 99%

Simultaneous production of isopropanol, butanol, ethanol and 2,3-butanediol by Clostridium acetobutylicum ATCC 824 engineered strains

et al. 2012

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Isopropanol represents a widely-used commercial alcohol which is currently produced from petroleum. In nature, isopropanol is excreted by some strains of Clostridium beijerinckii, simultaneously with butanol and ethanol during the isopropanol butanol ethanol (IBE) fermentation. In order to increase isopropanol production, the gene encoding the secondary-alcohol dehydrogenase enzyme from C. beijerinckii NRRL B593 (adh) which catalyzes the reduction of acetone to isopropanol, was cloned into the acetone, butanol and ethanol (ABE)-producing strain C. acetobutylicum ATCC 824. The transformants showed high capacity for conversion of acetone into isopropanol (> 95%). To increase isopropanol production levels in ATCC 824, polycistronic transcription units containing, in addition to the adh gene, homologous genes of the acetoacetate decarboxylase (adc), and/or the acetoacetyl-CoA:acetate/butyrate:CoA transferase subunits A and B (ctfA and ctfB) were constructed and introduced into the wild-type strain. Combined overexpression of the ctfA and ctfB genes resulted in enhanced solvent production. In non-pH-controlled batch cultures, the total solvents excreted by the transformant overexpressing the adh, ctfA, ctfB and adc genes were 24.4 g/L IBE (including 8.8 g/L isopropanol), while the control strain harbouring an empty plasmid produced only 20.2 g/L ABE (including 7.6 g/L acetone). The overexpression of the adc gene had limited effect on IBE production. Interestingly, all transformants with the adh gene converted acetoin (a minor fermentation product) into 2,3-butanediol, highlighting the wide metabolic versatility of solvent-producing Clostridia.

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Section: Introductionmentioning

confidence: 99%

Simultaneous production of isopropanol, butanol, ethanol and 2,3-butanediol by Clostridium acetobutylicum ATCC 824 engineered strains

et al. 2012

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“…lostridia are well known for their capacity to produce various acids and alcohols as end products of the anaerobic breakdown of different polysaccharides (1). These fermentation products are of interest as building blocks in the chemical industry or as biofuels.…”

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confidence: 99%

“…2,3-Butanediol and especially the pure enantiomeric forms are very valuable for the synthesis of chiral high-value pharmaceuticals. Alternatively, 2,3-butanediol may be enzymatically converted into 2-butanol, a potential biofuel with the same energetic value as 1-butanol but with less toxicity to the fermenting organism (1).…”

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confidence: 99%

Molecular Characterization of an NADPH-Dependent Acetoin Reductase/2,3-Butanediol Dehydrogenase from Clostridium beijerinckii NCIMB 8052

Raedts

Siemerink

Levisson

et al. 2014

Appl Environ Microbiol

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Acetoin reductase is an important enzyme for the fermentative production of 2,3-butanediol, a chemical compound with a very broad industrial use. Here, we report on the discovery and characterization of an acetoin reductase from Clostridium beijerinckii NCIMB 8052. An in silico screen of the C. beijerinckii genome revealed eight potential acetoin reductases. One of them (CBEI_1464) showed substantial acetoin reductase activity after expression in Escherichia coli. The purified enzyme (C. beijerinckii acetoin reductase [Cb-ACR]) was found to exist predominantly as a homodimer. In addition to acetoin (or 2,3-butanediol), other secondary alcohols and corresponding ketones were converted as well, provided that another electronegative group was attached to the adjacent C-3 carbon. Optimal activity was at pH 6.5 (reduction) and 9.5 (oxidation) and around 68°C. Cb-ACR accepts both NADH and NADPH as electron donors; however, unlike closely related enzymes, NADPH is preferred (K m , 32 M). Cb-ACR was compared to characterized close homologs, all belonging to the "threonine dehydrogenase and related Zndependent dehydrogenases" (COG1063). Metal analysis confirmed the presence of 2 Zn 2؉ atoms. To gain insight into the substrate and cofactor specificity, a structural model was constructed. The catalytic zinc atom is likely coordinated by Cys 37 , His 70 , and Glu 71 , while the structural zinc site is probably composed of Cys 100 , Cys 103 , Cys 106 , and Cys 114 . Residues determining NADP specificity were predicted as well. The physiological role of Cb-ACR in C. beijerinckii is discussed.

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“…Door bioraffinage en fermentatie omgezette zeesla biomassa kan dienen als biobrandstof en verder als vervanging van petrochemisch geproduceerde energiedragers in de markt voor bulkchemicaliën (López-Contreras et al 2010, Green 2011.…”

Section: Zeesla Als Bron Voor Biobrandstofunclassified

Haalbaarheid van het aanlanden van zeesla uit de Waddenzee : Randvoorwaarden en richtlijnen voor het oprichten van een commerciële aanvoerstroom

Jak¹,

Lubsch²,

Beier³

2020

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Production of longer-chain alcohols from lignocellulosic biomass: butanol, isopropanol and 2,3-butanediol

Cited by 20 publications

References 152 publications

Simultaneous production of isopropanol, butanol, ethanol and 2,3-butanediol by Clostridium acetobutylicum ATCC 824 engineered strains

Simultaneous production of isopropanol, butanol, ethanol and 2,3-butanediol by Clostridium acetobutylicum ATCC 824 engineered strains

Molecular Characterization of an NADPH-Dependent Acetoin Reductase/2,3-Butanediol Dehydrogenase from Clostridium beijerinckii NCIMB 8052

Haalbaarheid van het aanlanden van zeesla uit de Waddenzee : Randvoorwaarden en richtlijnen voor het oprichten van een commerciële aanvoerstroom

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