Influence of nitro group on biotransformation of nitrotoluenes in Pseudomonas putida strain OU83

Walia, Sandeep; Ali-Sadat, Shadan; Chaudhry, G. Rasul

doi:10.1016/s0048-3575(03)00068-3

Cited by 15 publications

(9 citation statements)

References 33 publications

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“…However, much less information is available on the bacterial degradation of 2-nitrotoluene except that studied in Pseudomonas sp. strain JS42, which involves formation of 3-methylcatechol with release of nitrite (Haigler et al 1994) and the biotransformation of 2-nitrotoluene to 2-aminotoluene by Pseudomonas putida OU83 (Walia et al 2003). In this paper, we report the isolation and characterization of an indigenous bacterial consortium capable of degrading nitroaromatic compounds and the pathway for the degradation of 2-nitrotoluene by Micrococcus sp.…”

Section: Introductionmentioning

confidence: 87%

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Biodegradation of 2-Nitrotoluene by Micrococcus sp. strain SMN-1

2010

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A bacterial consortium capable of degrading nitroaromatic compounds was isolated from pesticide-contaminated soil samples by selective enrichment on 2-nitrotoluene as a sole source of carbon and energy. The three different bacterial isolates obtained from bacterial consortium were identified as Bacillus sp. (A and C), Bacillus flexus (B) and Micrococcus sp. (D) on the basis of their morphological and biochemical characteristics and by phylogenetic analysis based on 16S rRNA gene sequences. The pathway for the degradation of 2-nitrotoluene by Micrococcus sp. strain SMN-1 was elucidated by the isolation and identification of metabolites, growth and enzymatic studies. The organism degraded 2-nitrotoluene through 3-methylcatechol by a meta-cleavage pathway, with release of nitrite.

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Section: Introductionmentioning

confidence: 87%

“…strain SMN-1 appears to be similar to that described in Pseudomonas sp. strain JS42 (Haigler et al 1994) but differs from that described in P. putida strain OU83, which involves reduction of 2-nitrotoluene to 2-aminotoluene (Walia et al 2003).…”

Section: Identification Of Metabolites Of 2-nitrotoluenementioning

confidence: 99%

Biodegradation of 2-Nitrotoluene by Micrococcus sp. strain SMN-1

2010

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“…Furthermore, the solvent tolerance of P. putida DOT-T1E might be exploited to enlarge the spectrum of solvents applicable for in situ product extraction and for the production of a broader range of organic compounds in two-liquid-phase bioreactor setups (11). m-Nitrotoluene was not oxidized in P. putida strains DOT-T1E and PpS81, yet the synthesis of oxidative enzymes involved in the mineralization of m-nitrotoluene via m-nitrobenzyl alcohol, m-nitrobenzaldehyde, and mnitrobenzoic acid has been reported for P. putida strain OU83 upon induction with m-nitrotoluene (1,50). Interestingly, mtoluidine accumulated as the main product, apparently without significant inhibition of the m-nitrotoluene hydroxylation.…”

Section: Discussionmentioning

confidence: 99%

Suitability of RecombinantEscherichia coliandPseudomonas putidaStrains for Selective Biotransformation ofm-Nitrotoluene by Xylene Monooxygenase

Meyer

Schmid

2005

Appl Environ Microbiol

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Escherichia coli JM101(pSPZ3), containing xylene monooxygenase (XMO) from Pseudomonas putida mt-2, catalyzes specific oxidations and reductions of m-nitrotoluene and derivatives thereof. In addition to reactions catalyzed by XMO, we focused on biotransformations by native enzymes of the E. coli host and their effect on overall biocatalyst performance. While m-nitrotoluene was consecutively oxygenated to m-nitrobenzyl alcohol, m-nitrobenzaldehyde, and m-nitrobenzoic acid by XMO, the oxidation was counteracted by an alcohol dehydrogenase(s) from the E. coli host, which reduced m-nitrobenzaldehyde to m-nitrobenzyl alcohol. Furthermore, the enzymatic background of the host reduced the nitro groups of the reactants resulting in the formation of aromatic amines, which were shown to effectively inhibit XMO in a reversible fashion. Host-intrinsic oxidoreductases and their reaction products had a major effect on the activity of XMO during biocatalysis of m-nitrotoluene. P. putida DOT-T1E and P. putida PpS81 were compared to E. coli JM101 as alternative hosts for XMO. These promising strains contained an additional dehydrogenase that oxidized m-nitrobenzaldehyde to the corresponding acid but catalyzed the formation of XMO-inhibiting aromatic amines at a significantly lower level than E. coli JM101.Microbial enzymes are useful catalysts for the degradation of organic pollutants in bioremediation but also for the synthesis of added-value products in biocatalytic applications. Various large-scale processes based on bacterial enzymes have been established (17,26,30,47), which illustrate the increasing impact of biocatalysis in the chemical industry (45). Heterologous gene expression has developed to a standard technology for increasing and controlling enzyme activities in bioprocesses. It allows catalysis of a variety of reactions in a limited number of bacterial strains used as recombinant hosts. The focus on a few suitable hosts is emphasized, e.g., by the PlugBug concept (DSM, Heerlen, The Netherlands). Of these strains, Escherichia coli strains are easily accessible for genetic and biochemical engineering and provide high metabolic activity for cofactor regeneration. Their use as recombinant hosts is especially favorable in cofactor-dependent oxygenase-based processes (7) for the conversion of various aromatic hydrocarbons to industrially relevant products (5, 38, 54). E. coli JM101(pSPZ3) (39) contains xylene monooxygenase (XMO) from Pseudomonas putida mt-2 and oxidizes the methyl groups of a variety of toluene and xylene derivatives to the corresponding alcohols, aldehydes, and acids (8,12,55).Nitroaromatics are widely used in large amounts as synthetic intermediates, dyes, pesticides, pharmaceuticals, and explosives (21, 46). Their electrophilic character makes them susceptible to reduction by all kinds of microbial systems (41). Numerous bacterial strains, such as those of Pseudomonas species (1, 43) and E. coli (13), provide enzymes that are able to transform nitro groups of aromatic compounds under aerobic condition...

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“…However, some bacteria such as Pseudomonas sp. strain JS42 (Haigler et al, 1994), Pseudomonas putida OU83 (Walia et al, 2003) and Micrococcus sp. (Mulla et al, 2011) could use 2-nitrotoluene as a sole source of carbon.…”

Section: Introductionmentioning

confidence: 99%

Bioremediation of 3,5-dinitrobenzoic acid and aniline by a Corynebacterium sp.

Ahmed¹,

Y²,

Kumosani³

et al. 2013

Afr. J. Microbiol. Res.

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Corynebacterium sp was isolated from the soil by using 3-5 dinitro benzoic acid (DNB) as a sole carbon source. The highest rate of degradation of aniline (AN) or DNB was found in the exponential phase of the growth of the bacterium. After 24 h, about 50% of DNB and 30% of AN were degraded by Corynebacterium sp. At a concentration of 0.5 to 1 g/L of AN or DNB, good growth was obtained and the protocatechuic acid was detected. The optimum concentration of yeast extract was 2 g/l. Catechol 1-2 dioxygenase was induced in the cells grown on a medium containing AN or DNB. A significant activity of this enzyme was detected, which means that ortho cleavage pathway may be present in Corynebacterium sp.

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Influence of nitro group on biotransformation of nitrotoluenes in Pseudomonas putida strain OU83

Cited by 15 publications

References 33 publications

Biodegradation of 2-Nitrotoluene by Micrococcus sp. strain SMN-1

Biodegradation of 2-Nitrotoluene by Micrococcus sp. strain SMN-1

Suitability of RecombinantEscherichia coliandPseudomonas putidaStrains for Selective Biotransformation ofm-Nitrotoluene by Xylene Monooxygenase

Bioremediation of 3,5-dinitrobenzoic acid and aniline by a Corynebacterium sp.

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