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Volumn 65, Issue 7, 2006, Pages 1146-1152

Bioremediation of halogenated compounds: Comparison of dehalogenating bacteria and improvement of catalyst stability

Author keywords

Haloalkane dehalogenase; Rhodococcus erythropolis NCIMB13064; Sphingomonas paucimobilis UT26; Xanthobacter autotrophicus GJ10

Indexed keywords

HALOALKANE DEHALOGENASE; RHODOCOCCUS ERYTHROPOLIS NCIMB13064; SPHINGOMONAS PAUCIMOBILIS UT26; XANTHOBACTER AUTOTROPHICUS GJ10;

EID: 33748578423     PISSN: 00456535     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemosphere.2006.04.007     Document Type: Article
Times cited : (12)

References (18)
  • 2
    • 0030047984 scopus 로고    scopus 로고
    • A mechanistic approach to deriving quantitative structure-activity relationship models for microbial degradation of organic compounds
    • Damborsky J. A mechanistic approach to deriving quantitative structure-activity relationship models for microbial degradation of organic compounds. SAR QSAR Environ. Res. 5 (1996) 27-36
    • (1996) SAR QSAR Environ. Res. , vol.5 , pp. 27-36
    • Damborsky, J.1
  • 3
    • 0344822639 scopus 로고    scopus 로고
    • Analysis of the reaction mechanism and substrate specificity of haloalkane dehalogenases by sequential and structural comparisons
    • Damborsky J., and Koca J. Analysis of the reaction mechanism and substrate specificity of haloalkane dehalogenases by sequential and structural comparisons. Protein Eng. 12 (1999) 989-998
    • (1999) Protein Eng. , vol.12 , pp. 989-998
    • Damborsky, J.1    Koca, J.2
  • 5
    • 0034609209 scopus 로고    scopus 로고
    • Enzymatic dehalogenation of gas substrates with haloalkane dehalogenase
    • Dravis B.C., Lejeune K.E., Hetro A.D., and Russel A.J. Enzymatic dehalogenation of gas substrates with haloalkane dehalogenase. Biotechnol. Bioeng. 69 (2000) 235-241
    • (2000) Biotechnol. Bioeng. , vol.69 , pp. 235-241
    • Dravis, B.C.1    Lejeune, K.E.2    Hetro, A.D.3    Russel, A.J.4
  • 6
    • 1542405952 scopus 로고    scopus 로고
    • Haloalkane hydrolysis by Rhodococcus erythropolis cells: A comparison of conventional aqueous phase dehalogenation and non-conventional gas phase dehalogenation
    • Erable B., Goubet I., Lamare S., Legoy M.D., and Maugard T. Haloalkane hydrolysis by Rhodococcus erythropolis cells: A comparison of conventional aqueous phase dehalogenation and non-conventional gas phase dehalogenation. Biotechnol. Bioeng. 86 (2004) 47-54
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 47-54
    • Erable, B.1    Goubet, I.2    Lamare, S.3    Legoy, M.D.4    Maugard, T.5
  • 7
    • 0025931434 scopus 로고
    • Biotransformation of halogenated compounds
    • Hardman D.J. Biotransformation of halogenated compounds. Crit. Rev. Biotechnol. 11 (1991) 1-40
    • (1991) Crit. Rev. Biotechnol. , vol.11 , pp. 1-40
    • Hardman, D.J.1
  • 8
    • 0021966251 scopus 로고
    • Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10
    • Janssen D.B., Scheper A., Dijkhuizen L., and Witholt B. Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10. Appl. Environ. Microbiol. 49 (1985) 673-677
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 673-677
    • Janssen, D.B.1    Scheper, A.2    Dijkhuizen, L.3    Witholt, B.4
  • 10
    • 1842479420 scopus 로고    scopus 로고
    • Evolving haloalkane dehalogenases
    • Janssen D.B. Evolving haloalkane dehalogenases. Curr. Opin. Chem. Biol. 8 (2004) 150-159
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 150-159
    • Janssen, D.B.1
  • 11
    • 0021798672 scopus 로고
    • Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
    • Keuning S., Janssen D.B., and Witholt B. Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J. Bacteriol. 163 (1985) 635-639
    • (1985) J. Bacteriol. , vol.163 , pp. 635-639
    • Keuning, S.1    Janssen, D.B.2    Witholt, B.3
  • 12
    • 0036595008 scopus 로고    scopus 로고
    • Volatile organic compounds in some urban locations in United States
    • Mohamed M.F., Kang D., and Aneja V.P. Volatile organic compounds in some urban locations in United States. Chemosphere 47 (2002) 863-882
    • (2002) Chemosphere , vol.47 , pp. 863-882
    • Mohamed, M.F.1    Kang, D.2    Aneja, V.P.3
  • 13
    • 0027436421 scopus 로고
    • Cloning and sequencing of a dehalogenase gene encoding an enzyme with hydrolase activity involved in the degradation of gamma-hexachlorocyclohexane in Pseudomonas paucimobilis
    • Nagata Y., Nariya T., Ohtomo R., Fukuda M., and Takagi M. Cloning and sequencing of a dehalogenase gene encoding an enzyme with hydrolase activity involved in the degradation of gamma-hexachlorocyclohexane in Pseudomonas paucimobilis. J. Bacteriol. 175 (1993) 6403-6410
    • (1993) J. Bacteriol. , vol.175 , pp. 6403-6410
    • Nagata, Y.1    Nariya, T.2    Ohtomo, R.3    Fukuda, M.4    Takagi, M.5
  • 14
    • 0030853537 scopus 로고    scopus 로고
    • Purification and characterization of haloalkane dehalogenase of a new substrate class from a hexachlorohexane degrading bacterium, sphingomonas paucimobilis UT26
    • Nagata Y., Miyauchi K., Damborsky J., Manova K., Ansorgova A., and Takagi M. Purification and characterization of haloalkane dehalogenase of a new substrate class from a hexachlorohexane degrading bacterium, sphingomonas paucimobilis UT26. Appl. Environ. Microbiol. 63 (1997) 3707-3710
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3707-3710
    • Nagata, Y.1    Miyauchi, K.2    Damborsky, J.3    Manova, K.4    Ansorgova, A.5    Takagi, M.6
  • 15
    • 0037117757 scopus 로고    scopus 로고
    • Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition
    • Oakley A.J., Prokop Z., Bohac M., Kmunicek K.J., Jedlicka T., Monincova M., Kuta-Smatanova I., Nagata Y., and Damborsky J. Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition. Biochemistry 41 (2002) 4847-4855
    • (2002) Biochemistry , vol.41 , pp. 4847-4855
    • Oakley, A.J.1    Prokop, Z.2    Bohac, M.3    Kmunicek, K.J.4    Jedlicka, T.5    Monincova, M.6    Kuta-Smatanova, I.7    Nagata, Y.8    Damborsky, J.9
  • 16
    • 15844362298 scopus 로고    scopus 로고
    • Specificity and kinetics of haloalkane dehalogenase
    • Schanstra J.P., Kingma J., and Janssen D.B. Specificity and kinetics of haloalkane dehalogenase. J. Biol. Chem. 271 (1996) 14747-14753
    • (1996) J. Biol. Chem. , vol.271 , pp. 14747-14753
    • Schanstra, J.P.1    Kingma, J.2    Janssen, D.B.3
  • 18
    • 33748544531 scopus 로고    scopus 로고
    • Stafford, T.M., 1993. The microbial degradation of chloroalkanes. PhD Thesis, University of Belfast, Ireland.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.