Degradation of 4-chlorobiphenyl and 4-chlorobenzoic acid by the strain Rhodococcus ruber P25

Плотникова, Е. Г.; Solyanikova, Inna P.; Егорова, Д. О.; Шумкова, Е. С.; Golovleva, L. A.

doi:10.1134/s0026261712020117

Cited by 23 publications

(6 citation statements)

References 32 publications

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“…The presence of both orthoand metacleavage pathways in Sphe3 was also validated through proteomic analysis [29]. Although the occurrence of meta-cleavage of PCA has also been demonstrated in Arthrobacter keyseri 12B [30] as well as in other Actinobacteria [31], there is no study on the kinetic characterization of PCA 4,5-dioxygenase in this phylum. The functional and/or kinetic studies of enzymes belonging to the largely uncharacterized Type II extradiol dioxygenase clade of the PCAD-Memo superfamily will allow comparisons among these enzymes, thus shedding more light on this Type in the dioxygenase superfamily.…”

Section: Introductionmentioning

confidence: 97%

Characterization of Protocatechuate 4,5-Dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and In Situ Reaction Monitoring in the NMR Tube

Tsagogiannis

Vandera

Primikyri

et al. 2021

IJMS

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The current study aims at the functional and kinetic characterization of protocatechuate (PCA) 4,5-dioxygenase (PcaA) from Pseudarthrobacter phenanthrenivorans Sphe3. This is the first single subunit Type II dioxygenase characterized in Actinobacteria. RT-PCR analysis demonstrated that pcaA and the adjacent putative genes implicated in the PCA meta-cleavage pathway comprise a single transcriptional unit. The recombinant PcaA is highly specific for PCA and exhibits Michaelis–Menten kinetics with Km and Vmax values of 21 ± 1.6 μM and 44.8 ± 4.0 U × mg−1, respectively, in pH 9.5 and at 20 °C. PcaA also converted gallate from a broad range of substrates tested. The enzymatic reaction products were identified and characterized, for the first time, through in situ biotransformation monitoring inside an NMR tube. The PCA reaction product demonstrated a keto-enol tautomerization, whereas the gallate reaction product was present only in the keto form. Moreover, the transcriptional levels of pcaA and pcaR (gene encoding a LysR-type regulator of the pathway) were also determined, showing an induction when cells were grown on PCA and phenanthrene. Studying key enzymes in biodegradation pathways is significant for bioremediation and for efficient biocatalysts development.

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Section: Introductionmentioning

confidence: 97%

Characterization of Protocatechuate 4,5-Dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and In Situ Reaction Monitoring in the NMR Tube

Tsagogiannis

Vandera

Primikyri

et al. 2021

IJMS

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“…PCBs undergoes dehalogenation to lower chlorinated biphenyl and further to chlorobenzoic acid metabolite. These chlorobiphenyl is further converted into hydroxybenzoic acid and dihydroxybenzoic acid ( Zhai et al, 2010 ; Plotnikova et al, 2012 ). Bedard et al (1987) , have reported chlorinated benzoic acid and chlorinated acetophenone intermediate metabolites from oxidation of PCB congeners.…”

Section: Resultsmentioning

confidence: 99%

PCB-77 biodegradation potential of biosurfactant producing bacterial isolates recovered from contaminated soil

Sandhu

Paul²,

Proćków³

et al. 2022

Front. Microbiol.

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Polychlorinated biphenyls (PCBs) are persistent organic pollutants widely distributed in the environment and possess deleterious health effects. The main objective of the study was to obtain bacterial isolates from PCB-contaminated soil for enhanced biodegradation of PCB-77. Selective enrichment resulted in the isolation of 33 strains of PCB-contaminated soil nearby Bhilai steel plant, Chhattisgarh, India. Based on the prominent growth using biphenyl as the sole carbon source and the confirmation of its degradation by GC-MS/MS analysis, four isolates were selected for further study. The isolates identified by 16S rRNA gene sequencing were Pseudomonas aeruginosa MAPB-2, Pseudomonas plecoglossicida MAPB-6, Brucella anthropi MAPB-9, and Priestia megaterium MAPB-27. The isolate MAPB-9 showed a degradation of 66.15% biphenyl, while MAPB-2, MAPB-6, and MAPB-27 showed a degradation of 62.06, 57.02, and 56.55%, respectively in 48 h. Additionally, the degradation ability of these strains was enhanced with addition of co-metabolite glucose (0.2%) in the culture medium. Addition of glucose showed 100% degradation of biphenyl by MAPB-9, in 48 h, while MAPB-6, MAPB-2, and MAPB-27 showed 97.1, 67.5, and 53.3% degradation, respectively as analyzed by GC-MS/MS. Furthermore, in the presence of inducer, PCB-77 was found to be 59.89, 30.49, 27.19, and 4.43% degraded by MAPB-6, MAPB-9, MAPB-2, and MAPB-27, respectively in 7 d. The production of biosurfactants that aid in biodegradation process were observed in all the isolates. This was confirmed by ATR-FTIR analysis that showed the presence of major functional groups (CH2, CH3, CH, = CH2, C–O–C, C-O) of the biosurfactant. The biosurfactants were further identified by HPTLC and GC-MS/MS analysis. Present study is the first to report PCB-77 degradation potential of Pseudomonas aeruginosa, B. anthropi, Pseudomonas plecoglossicida, and Priestia megaterium. Similarly, this is the first report on Pseudomonas plecoglossicida and Priestia megaterium for PCB biodegradation. Our results suggest that the above isolates can be used for the biodegradation of biphenyl and PCB-77 in PCB-contaminated soil.

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“…4‐CB1 (Crooks and Copley, ), Arthrobacter sp. (Zhuang et al ., ; Zhou et al ., ), Rhodococcus ruber P25 (Plotnikova et al ., ), Betaproteobacteria (Chae et al ., ). 4‐Chlorobenzoate can be used as a substrate for ATP‐dependent 4‐halobenzoate coenzyme A ligase in the cell to generate a reactive metabolite, 4‐chlorobenzoyl coenzyme A (Pieper, ).…”

Section: The Middle Metabolic Pathways For Dehalogenation Of Halogenamentioning

confidence: 99%

Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions

Pimviriyakul

Wongnate

Tinikul

et al. 2019

Microbial Biotechnology

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Summary Halogenated aromatics are used widely in various industrial, agricultural and household applications. However, due to their stability, most of these compounds persist for a long time, leading to accumulation in the environment. Biological degradation of halogenated aromatics provides sustainable, low‐cost and environmentally friendly technologies for removing these toxicants from the environment. This minireview discusses the molecular mechanisms of the enzymatic reactions for degrading halogenated aromatics which naturally occur in various microorganisms. In general, the biodegradation process (especially for aerobic degradation) can be divided into three main steps: upper, middle and lower metabolic pathways which successively convert the toxic halogenated aromatics to common metabolites in cells. The most difficult step in the degradation of halogenated aromatics is the dehalogenation step in the middle pathway. Although a variety of enzymes are involved in the degradation of halogenated aromatics, these various pathways all share the common feature of eventually generating metabolites for utilizing in the energy‐producing metabolic pathways in cells. An in‐depth understanding of how microbes employ various enzymes in biodegradation can lead to the development of new biotechnologies via enzyme/cell/metabolic engineering or synthetic biology for sustainable biodegradation processes.

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Degradation of 4-chlorobiphenyl and 4-chlorobenzoic acid by the strain Rhodococcus ruber P25

Cited by 23 publications

References 32 publications

Characterization of Protocatechuate 4,5-Dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and In Situ Reaction Monitoring in the NMR Tube

Characterization of Protocatechuate 4,5-Dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and In Situ Reaction Monitoring in the NMR Tube

PCB-77 biodegradation potential of biosurfactant producing bacterial isolates recovered from contaminated soil

Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions

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