• Title/Summary/Keyword: hydrolytic dechlorination

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Hydrolytic Dechlorination of 4-Chlorobenzoate Specified by fcbABC of Pseudomonas sp. DJ -12

  • Chae, Jong-Chan;Ahn, Kyung-Joon;Kim, Chi-Kyung
    • Journal of Microbiology and Biotechnology
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    • v.8 no.6
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    • pp.692-695
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    • 1998
  • Pseudomonas sp. DJ-12 was able to degrade 4-chlorobenzoate by hydrolytic dechlorination to produce 4-hydroxybenzoate and chloride ion. The fcbABC genes responsible for the hydrolytic dechlorination were cloned from the chromosomal DNA of the organism. The genes were found to be organized in the order fcbB-fcbA-fcbC, but there was an intergenic space between the fcbA and fcbC genes.

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Catabolic Degradation of 4-Chlorobiphenyl by Pseudomonas sp. DJ-12 via Consecutive Reaction of meta-Cleavage and Hydrolytic Dechlorination

  • Chae, Jong-Chan;Kim, Eunheui;Park, Sang-Ho;Kim, Chi-Kyung
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.5 no.6
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    • pp.449-455
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    • 2000
  • Pseudomonas sp. strain DJ-12 is a bacterial isolate capable of degrading 4-chlorobiphenyl (4CBP) as a carbon and energy source. The catabolic degradation of 4CBP by the strain DJ-12 was studied along with the genetic organization of the genes responsible for the crucial steps of the catabolic degradation. The catabolic pathway was characterized as being conducted by consecutive reactions of the meta-cleavage of 4CBP, hydrolytic dechlorination of 4-chlorobenzoate (4CBA), hydroxylation of 4-hydroxybenzoate, and meta-cleavage of protocatechuate. The pcbC gene responsible for the meta-cleavage of 4CBP only showed a 30 to 40% homology in its deduced amino acid sequence compared to those of the corresponding genes from other strains. The amino acid sequence of 4CBA-CoA dechlorinase showed an 86% homology with that of Pseudomonas sp. CBS3, yet only a 50% homology with that of Arthrobacter spp. However, the fcb genes for the hydrolytic dechlorination of 4CBA in Pseudomonas sp. DJ-12 showed an uniquely different organization from those of CBS3 and other reported strains. Accordingly, these results indicate that strain DJ-12 can degrade 4CBA completely via meta-cleavage and hydrolytic dechlorination using enzymes that are uniquely different in their amino acid sequences from those of other bacterial strains with the same degradation activities.

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Characteristics of Several Bacterial Isolates Capable of Degrading Chloroaliphatic Compounds via Hydrolytic Dechlorination

  • Song, Ji-Sook;Lee, Dong-Hun;Lee, Kyoung;Kim, Chi-Kyung
    • Journal of Microbiology
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    • v.41 no.4
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    • pp.277-283
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    • 2003
  • Haloaliphatic hydrocarbons have been widely used as solvents and ingredients of pesticides and herbicides. However, when these compounds contaminate the environment, they can be very hazardous to animals and humans because of their potential toxicity and carcinogenicity. Therefore, lots of studies have been made for microbial degradation of those pollutant chemicals. In this study, 11 bacterial strains capable of degrading 1,2-dichloroethane (1,2-DCA), 2-chloropropionic acid (2-CPA), 2,3-dichloropropionic acid (2,3-DCPA), and 2-monochloroacetic acid (2-MCA) by hydrolytic dechlorination under aerobic conditions were isolated from wastewaters and rice paddy soil samples. Their morphological and biochemical characteristics and their degradation capabilities of haloaliphatic hydrocarbons were examined. On the basis of the 16S rDNA sequences, 8 different kinds of microbial species, including Pseudomonas plecoglossicida, Xanthobacter flavus, Ralstonia eutropha, were identified. All of the isolated strains can degrade MCA. In particular, strains UE-2 and UE-15 degraded 1,2-DCA, and strain CA-11 degraded 2,3-DCPA, which are hardly degraded by other strains.

Dechlorination of 4-Chlorobenzoate by Pseudomonas sp. DJ-12

  • Chae, Jong-Chan;Kim, Chi-Kyung
    • Journal of Microbiology
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    • v.35 no.4
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    • pp.290-294
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    • 1997
  • 4-Chlorobiphenyl-degrading Pseudomonas sp. DJ-12 was able to degrade 4-chlorobenzoate(4CBA), 4-iodobenzoate, and 4-bromobenzoate completely under aerobic conditions. During. the degradation of 4CBA by Pseudomonas sp. DJ-12, chloride ions were released by dechlorination and 4-hydroxybenzoate was produced as an intermediate metabolite. The NotI-KNA fragments of pKC157 containing dechlorination genes hybridized with the gene encoding 4CBA:CoA dehalogenase of Pseudomonas sp. CBS3 which is responsible for the hydrolytic dechlorination of 4CBA. These results imply that Pseudomonas sp. DJ-12 degrades 4CBA to 40hydroxybenzoate via dechlorination as the initial step of its degradativ pathway. The genes responsible for dechlorination of 4CBA were found to be blcated on the chromosomal DNA of Pseudomonas sp. DJ-12.

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Structural Analysis of the fcbABC Gene Cluster Responsible for Hydrolytic Dechlorination of 4-Chlorobenzoate from pJS1 Plasmid of Comamonas sp. P08

  • Lee, Jeong-Soon;Lee, Kyoung;Ka, Jong-Ok;Jong-Chan;Kim, Chi-Kyung
    • Journal of Microbiology
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    • v.41 no.2
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    • pp.89-94
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    • 2003
  • Bacterial strain No. P08 isolated from wastewater at the Cheongju industrial complex was found to be capable of degrading 4-chlorobenzoate under aerobic condition. P08 was identified as Comamonas sp. from its cellular fatty acid composition and 16S rDNA sequence. The fcb genes, responsible for the hydrolytic dechlorination of 4-chlorobenzoate, were cloned from the plasmid pJJl of Comamonas sp. P08. The fcb gene cluster of comamonas sp. PO8 was organized in the order fcbB-fcbA-fcbTl-fcbT2-fcbT3-fcbC. This organization of the fcb genes was very similar to that of the fcb genes carried on the chromosomal DNA of pseudomonas sp. DJ-12. However, it differed from the fcbA-fcbB -fcbC ordering of Arthrobacter sp. SU. The nucleotide sequences of the fcbABC genes of strain P08 showed 98% and 53% identities to those of Pseudomonas sp. DJ-12 and Arthrobacter sp. SU, respectively. This suggests that the fcb genes might have been derived from Pseudomonas sp. DJ-12 to form plasmid pJSl in Comamonas sp. P08, or that the fcb genes in strain DJ-12 were transposed from Comamonas sp. P08 plasmid.

Biodegradation of Recalcitrant Chlorinated Aromatic Compounds via Microbial Dechlorination (미생물의 탈염소화 작용에 의한 난분해성 염화방향족 오염물질의 분해)

  • 채종찬;김치경
    • Korean Journal of Environmental Biology
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    • v.17 no.2
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    • pp.129-138
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    • 1999
  • Chlorinated aromatic compounds are one of the largest groups of environmental pollutants as a result of world-wide distribution by using them as herbicides, insecticides, fungicides, solvents, hydraulic and heat transfer fluids, plasticizers, and intermediates for chemical synthesis. Because of their toxicity, persistence, and bioaccumulation, the compounds contaminated ubiquitously in the biosphere has attracted public concerns in terms of serious influences to wild lives and a human being, such as carcinogenicity, mutagenicity, and disturbance in endocrine systems. The biological recalcitrance of the compounds is caused by the number, type, and position of the chlorine substituents as well as by their aromatic structures. In general, the carbon-halogen bonds increase the recalcitrance by increasing electronegativity of the substituent, so that the dechlorination of the compounds is focused as an important mechanism for biodegradation of chlorinated aromatics, along with the cleavage of aromatic rings. The removal of the chlorine substituents has been known as a key step for degradation of chlorinated aromatic compounds under aerobic condition. This can occur as an initial step via oxygenolytic, reductive, and hydrolytic mechanisms. The studies on the biochemistry and genetics about microbial dechlorination give us the potential informations for microbial degradation of xenobiotics contaminated in natural microcosms. Such investigations might provide biotechnological approaches to solve the environmental contamination, such as designing effective bioremediation systems using genetically engineered microorganisms.

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Genetic Organization of the dhlA Gene Encoding 1,2-Dichloroethane Dechlorinase from Xanthobacter flavus UE15

  • Song, Ji-Sook;Lee, Dong-Hun;Lee, Kyoung;Kim, Chi-Kyung
    • Journal of Microbiology
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    • v.42 no.3
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    • pp.188-193
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    • 2004
  • Xanthobacter flavus strain UE15 was isolated in wastewater obtained from the Ulsan industrial complex, Korea. This strain functions as a 1,2-dichloroethane (1,2-DCA) degrader, via a mechanism of hydrolytic dechlorination, under aerobic conditions. The UE15 strain was also capable of dechlorinating other chloroaliphatics such as 2-chloroacetic acid and 2-chloropropionic acid. The dhlA gene encoding 1,2-DCA dechlorinase was cloned from the genomic DNA of the UE15 strain, and its nucleotide sequence was determined to consist of 933 base pairs. The deduced amino acid sequence of the DhlA dechlorinase exhibited 100% homology with the corresponding enzyme from X. autotrophicus GJ10, but only 27 to 29% homology with the corresponding enzymes from Rhodococcus rhodochrous, Pseudomonas pavonaceae, and Mycobacterium sp. strain GP1, which all dechlorinate haloalkane compounds. The UE15 strain has an ORF1 (1,356 bp) downstream from the dhlA gene. The OFR1 shows 99% amino acid sequence homology with the transposase reported from X. autotrophicus GJ10. The transposase gene was not found in the vicinity of the dhlA in the GJ10 strain, but rather beside the dhlB gene coding for haloacid dechlorinase. The dhlA and dhlB genes were confirmed to be located at separate chromosomal loci in the Xanthobacter flavus UE15 strain as well as in X. autotrophicus GJ10. The dhlA and transposase the UE15 strain were found to be parenthesized by a pair of insertion sequences, 181247, which were also found on both sides of the transposase gene in the GJ10 strain. This unique structure of the dhlA gene organization in X. flavus strain UE15 suggested that the dechlorinase gene, dhlA, is transferred with the help of the transposase gene.