Excretion of butyraldehyde, isobutyraldehyde and valeraldehyde by Streptomyces cinnamonensis

Pospísil, S

doi:10.1016/0378-1097(94)90398-0

Cited by 3 publications

(3 citation statements)

References 7 publications

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“…We therefore propose that the aldehydes which are the substrates for P. furiosus ADH arise from the nonoxidative decarboxylation of 2-keto acids, produced from glycolysis and amino acid transamination and catalyzed by POR and the related enzymes IOR, KGOR, and VOR. Such aldehydes are very reactive compounds and ultimately toxic, especially at the growth temperature of P. furiosus (16,25,37,49). Hence, ADH is proposed to function in P. furiosus as an aldehyde-scavenging enzyme (Fig.…”

Section: Discussionmentioning

confidence: 99%

An Unusual Oxygen-Sensitive, Iron- and Zinc-Containing Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Pyrococcus furiosus

Adams

1999

J Bacteriol

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Pyrococcus furiosus is a hyperthermophilic archaeon that grows optimally at 100°C by the fermentation of peptides and carbohydrates to produce acetate, CO2, and H2, together with minor amounts of ethanol. The organism also generates H2S in the presence of elemental sulfur (S0). Cell extracts contained NADP-dependent alcohol dehydrogenase activity (0.2 to 0.5 U/mg) with ethanol as the substrate, the specific activity of which was comparable in cells grown with and without S0. The enzyme was purified by multistep column chromatography. It has a subunit molecular weight of 48,000 ± 1,000, appears to be a homohexamer, and contains iron (∼1.0 g-atom/subunit) and zinc (∼1.0 g-atom/subunit) as determined by chemical analysis and plasma emission spectroscopy. Neither other metals nor acid-labile sulfur was detected. Analysis using electron paramagnetic resonance spectroscopy indicated that the iron was present as low-spin Fe(II). The enzyme is oxygen sensitive and has a half-life in air of about 1 h at 23°C. It is stable under anaerobic conditions even at high temperature, with half-lives at 85 and 95°C of 160 and 7 h, respectively. The optimum pH for ethanol oxidation was between 9.4 and 10.2 (at 80°C), and the apparent Km s (at 80°C) for ethanol, acetaldehyde, NADP, and NAD were 29.4, 0.17, 0.071, and 20 mM, respectively. P. furiosus alcohol dehydrogenase utilizes a range of alcohols and aldehydes, including ethanol, 2-phenylethanol, tryptophol, 1,3-propanediol, acetaldehyde, phenylacetaldehyde, and methyl glyoxal. Kinetic analyses indicated a marked preference for catalyzing aldehyde reduction with NADPH as the electron donor. Accordingly, the proposed physiological role of this unusual alcohol dehydrogenase is in the production of alcohols. This reaction simultaneously disposes of excess reducing equivalents and removes toxic aldehydes, both of which are products of fermentation.

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Section: Discussionmentioning

confidence: 99%

An Unusual Oxygen-Sensitive, Iron- and Zinc-Containing Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Pyrococcus furiosus

Adams

1999

J Bacteriol

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“…Also in metabolic routes, formation of butanal and isobutyraldehyde precedes the formation of the corresponding alcohols, as shown in Figures and , respectively. Small amounts are excreted by several microorganisms . A mutant of C. acetobutylicum was found to produce up to 1.7 g/L butanal during ABE fermentation, and it was mentioned that due to its low boiling point (75 °C) recovery should be easier than for 1-butanol (bp 117 °C) …”

Section: Aldehydesmentioning

confidence: 99%

Transformation of Biomass into Commodity Chemicals Using Enzymes or Cells

2013

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“…14 Streptomyces cinnamonensis has been shown to excrete butyraldehyde, isobutyraldehyde and valeraldehyde. 15 Butyraldehyde obtained by the above processes can be used for the butanol production.…”

Section: Introductionmentioning

confidence: 99%

A green process for the production of butanol from butyraldehyde using alcohol dehydrogenase: process details

et al. 2014

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Depletion of energy sources has drawn attention towards production of bio-butanol by fermentation.However, the process is constrained by product inhibition which results in low product yield. Hence, a new strategy wherein butanol was produced from butyraldehyde using alcohol dehydrogenase and NADH as a cofactor was developed. Butyraldehyde can be synthesized chemically or through fermentation. The problem of cofactor regeneration during the reaction for butanol production was solved using substrate coupled and enzyme coupled reactions. The conventional reaction produced 35% of butanol without regeneration of cofactor using 300 mM NADH. The process of substrate coupled reaction was optimized to get maximum conversion. NADH (30 mM) and 100 mg per ml of alcohol dehydrogenase (320 U mg À1 ) could convert 17.39 mM of butyraldehyde to butanol using ethanol (ratio of butyraldehye to ethanol 1 : 4) giving a maximum conversion of 75%. The enzyme coupled reaction under the same conditions showed only 24% conversion of butyraldehyde to butanol using the glutamate dehydrogenase-L-glutamate enzyme system for the regeneration of cofactor. Hence, substrate coupled reaction is suggested as a better method over the enzyme coupled reaction for the cost effective production of butanol.

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Excretion of butyraldehyde, isobutyraldehyde and valeraldehyde by Streptomyces cinnamonensis

Cited by 3 publications

References 7 publications

An Unusual Oxygen-Sensitive, Iron- and Zinc-Containing Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Pyrococcus furiosus

An Unusual Oxygen-Sensitive, Iron- and Zinc-Containing Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Pyrococcus furiosus

Transformation of Biomass into Commodity Chemicals Using Enzymes or Cells

A green process for the production of butanol from butyraldehyde using alcohol dehydrogenase: process details

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