Glyoxylic Acid Production Using Microbial Transformant Catalysts

Gavagan, John E.; Fager, Susan K.; Seip, John E.; Payne, Mark S.; Anton, David L.; DiCosimo, Robert

doi:10.1021/jo00118a009

Cited by 44 publications

(25 citation statements)

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“…L-Lactate was incubated with Pediococcus Llactate oxidase in the presence of bovine liver catalase to destroy the hydrogen peroxide side product. 1,46 In meaningful intervals, an aliquot was taken from the reaction mixture and incubated with 2 for signal amplification. After signal amplification, the efficiency of the reaction mixtures to inactivate pore 1 was tested and plotted as a function of incubation time (Fig.…”

Section: Resultsmentioning

confidence: 99%

Chirality sensing with pores: Reactive signal amplifiers for otherwise undetectable small molecules

Henning

Matile

2008

Chirality

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Recently, we have introduced a concept to determine enantiomeric excess (ee) with synthetic multifunctional pores (Tanaka and Matile, Chirality 2008;20:307-312). The reported approach is, however, limited to macromolecules and not applicable to small molecules. The problem is that the ability of synthetic pores to respond to chemical stimulation decreases with the size and the charge of the analyte. Here we demonstrate that this problem can be overcome with reactive signal amplifiers that covalently capture elusive analytes for sensitive recognition by the pore. For proof of principle, we use L-lactate and D-lactate as representative pair of enantiomers, L-lactate oxidase as stereospecific signal generator, and cascade blue hydrazide as reactive signal amplifier to capture the produced pyruvate. After stereospecific signal generation and reactive signal amplification, L-lactate was detectable quantitatively and without further optimization in the presence of at least 99% ee of D-lactate. Attempts to sense the traces of impurity in commercial samples of D-lactate gave values in the expected range (99.6% ee expected, 99.3 +/- 0.1% ee found).

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Section: Resultsmentioning

confidence: 99%

Chirality sensing with pores: Reactive signal amplifiers for otherwise undetectable small molecules

Henning

Matile

2008

Chirality

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“…Glyoxylic acid is produced chemically through the oxidation of glyoxal involving nitric acid or via a three-step reaction that involves the ozonolysis of dimethyl maleate and hydrogenation of the resulting methylglyoxylate hemiacetal (Seip et al, 1993;Gavagan et al, 1995). Chemical production, therefore, has the major drawback of a high concentration of oxalic acid as a by-product.…”

Section: Introductionmentioning

confidence: 99%

Aldehyde oxidase carrying an unusual subunit structure from Pseudomonas sp. MX‐058

Thiwthong¹,

Kataoka²,

Iwasaki³

et al. 2008

Microbial Biotechnology

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SummaryPseudomonas sp. MX‐058 produces aldehyde oxidase catalysing glyoxal to glyoxylic acid. Two aldehyde oxidases (F10 and F13) were purified to homogeneity from Pseudomonas sp. MX‐058. F10 and F13 had subunit structures, a heterotetramer and heteropentamer respectively. The N‐terminal amino acid sequences of all subunits were highly homologous to amino acid sequences of the putative oxidoreductases of Pseudomonas strains. All of these homologous oxidoreductases have a heterotrimer structure consisting of 85‐88 (α), 37‐39 (β) and 18‐23 (γ) kDa subunits. However, the α‐subunits of F10 and F13 might have decomposed into two [80 (α1) and 9 kDa (α2)] and three [58 (α1′), 22 (α1″) and 9 (α2) kDa] subunits, respectively, while the β‐ and γ‐subunits remained intact. Both F10 and F13 show high activity toward several aliphatic and aromatic aldehydes. The aldehyde oxidases of Pseudomonas sp. MX‐058 has unique protein structures, α1α2βγ for F10 and α1′α1″α2βγ for F13, a heterotetramer and heteropentamer respectively. The enzymes exhibit significantly low activity toward glyoxylic acid compared with glyoxal, which is an advantageous property for glyoxylic acid production from glyoxal.

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“…Examples for the enzymatic production of glyoxylic acid are the conversion of glycolic acid by glycolic acid oxidase from spinach, selectively yielding as much as 98% glyoxylic acid in a whole-cell system. Further, a two-step chemoenzymatic route using base catalysis and glycolic acid oxidase for the synthesis of glyoxylic acid from glyoxal, as well as the synthesis of glycolic acid by using glycerol oxidase from Aspergillus japonicus, has been described (15,21,39). …”

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confidence: 99%

Ethylene Glycol Metabolism by Pseudomonas putida

Mückschel

Simon

Klebensberger

et al. 2012

Appl Environ Microbiol

106

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dIn this study, we investigated the metabolism of ethylene glycol in the Pseudomonas putida strains KT2440 and JM37 by employing growth and bioconversion experiments, directed mutagenesis, and proteome analysis. We found that strain JM37 grew rapidly with ethylene glycol as a sole source of carbon and energy, while strain KT2440 did not grow within 2 days of incubation under the same conditions. However, bioconversion experiments revealed metabolism of ethylene glycol by both strains, with the temporal accumulation of glycolic acid and glyoxylic acid for strain KT2440. This accumulation was further increased by targeted mutagenesis. The key enzymes and specific differences between the two strains were identified by comparative proteomics. In P. putida JM37, tartronate semialdehyde synthase (Gcl), malate synthase (GlcB), and isocitrate lyase (AceA) were found to be induced in the presence of ethylene glycol or glyoxylic acid. Under the same conditions, strain KT2440 showed induction of AceA only. Despite this difference, the two strains were found to use similar periplasmic dehydrogenases for the initial oxidation step of ethylene glycol, namely, the two redundant pyrroloquinoline quinone (PQQ)-dependent enzymes PedE and PedH. From these results we constructed a new pathway for the metabolism of ethylene glycol in P. putida. Furthermore, we conclude that Pseudomonas putida might serve as a useful platform from which to establish a whole-cell biocatalyst for the production of glyoxylic acid from ethylene glycol.

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Glyoxylic Acid Production Using Microbial Transformant Catalysts

Cited by 44 publications

References 0 publications

Chirality sensing with pores: Reactive signal amplifiers for otherwise undetectable small molecules

Chirality sensing with pores: Reactive signal amplifiers for otherwise undetectable small molecules

Aldehyde oxidase carrying an unusual subunit structure from Pseudomonas sp. MX‐058

Ethylene Glycol Metabolism by Pseudomonas putida

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