메뉴 건너뛰기




Volumn 43, Issue 3, 2008, Pages 241-252

Variability of enzyme system of Nocardioform bacteria as a basis of their metabolic activity

Author keywords

Application; Enzymes; Nocardioform bacteria; Xenobiotics

Indexed keywords

AROMATIC HYDROCARBONS; BIODEGRADATION; ENZYME ACTIVITY; METABOLISM;

EID: 41349113215     PISSN: 03601234     EISSN: 15324109     Source Type: Journal    
DOI: 10.1080/03601230701771180     Document Type: Review
Times cited : (8)

References (116)
  • 1
    • 0034840415 scopus 로고    scopus 로고
    • Biodegradation and bioremediation of hydrocarbons in extreme environments
    • Margesin, R.; Schinner, F. Biodegradation and bioremediation of hydrocarbons in extreme environments. Appl. Microbiol. Biotechnol. 2001, 56, 650-663.
    • (2001) Appl. Microbiol. Biotechnol , vol.56 , pp. 650-663
    • Margesin, R.1    Schinner, F.2
  • 2
    • 41349106922 scopus 로고    scopus 로고
    • Bergey's Manual of Determinative Bacteriology. 9th Ed.; Holt, J.G., Krieg, N.R., Sneath, P.H.A., Staley, J.T., Williams, S.T., eds.; Williams & Wilkins: Baltimore, Philadelphia, HongKong, London, Munich, Sydney, Tokyo, (A Waverly Company). 1997, 2, 630-654.
    • Bergey's Manual of Determinative Bacteriology. 9th Ed.; Holt, J.G., Krieg, N.R., Sneath, P.H.A., Staley, J.T., Williams, S.T., eds.; Williams & Wilkins: Baltimore, Philadelphia, HongKong, London, Munich, Sydney, Tokyo, (A Waverly Company). 1997, 2, 630-654.
  • 7
    • 33947371315 scopus 로고    scopus 로고
    • Transcriptomic analysis reveals a bifurcated terephthalate degradation pathway in Rhodococcus sp. strain RHA1
    • Hara, H.; Eltis, L.D.; Davies, J.E.; Mohn, W.W. Transcriptomic analysis reveals a bifurcated terephthalate degradation pathway in Rhodococcus sp. strain RHA1. J. Bacteriol. 2007, 189, 1641-1647.
    • (2007) J. Bacteriol , vol.189 , pp. 1641-1647
    • Hara, H.1    Eltis, L.D.2    Davies, J.E.3    Mohn, W.W.4
  • 8
    • 0028276797 scopus 로고
    • Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6: Identification of a new family of extradiol dioxygenases
    • Asturias, J.A.; Eltis, L.D.; Prucha, M.; Timmis, K.N. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6: identification of a new family of extradiol dioxygenases. J. Biol. Chem. 1994a, 269, 7807-7815.
    • (1994) J. Biol. Chem , vol.269 , pp. 7807-7815
    • Asturias, J.A.1    Eltis, L.D.2    Prucha, M.3    Timmis, K.N.4
  • 9
    • 0027981885 scopus 로고
    • Reclassification of the polychlorinated biphenyl-degraders Acinetobacter sp. strain P6 and Corynebacter sp. strain MB1 as Rhodococcus globerulus
    • Asturias, J.A.; Moore, E.; Yakimov, M.M.; Klatte, S.; Timmis, K.N. Reclassification of the polychlorinated biphenyl-degraders Acinetobacter sp. strain P6 and Corynebacter sp. strain MB1 as Rhodococcus globerulus. Syst. Appl. Microbiol. 1994b, 17, 226-231.
    • (1994) Syst. Appl. Microbiol , vol.17 , pp. 226-231
    • Asturias, J.A.1    Moore, E.2    Yakimov, M.M.3    Klatte, S.4    Timmis, K.N.5
  • 10
    • 0029059059 scopus 로고
    • Characterization of biphenyl catabolic genes of gram-positive polychlorinated biphenyl degrader Rhodococcus sp. RHA1
    • Masai, E.; Yamada, A.; Healy, J.M.; Hatta, T.; Kimbara, K.; Fukuda, M.; Yano, K. Characterization of biphenyl catabolic genes of gram-positive polychlorinated biphenyl degrader Rhodococcus sp. RHA1. Appl. Environm. Microbiol. 1995, 61, 2079-2085.
    • (1995) Appl. Environm. Microbiol , vol.61 , pp. 2079-2085
    • Masai, E.1    Yamada, A.2    Healy, J.M.3    Hatta, T.4    Kimbara, K.5    Fukuda, M.6    Yano, K.7
  • 11
    • 0031039131 scopus 로고    scopus 로고
    • The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA 1
    • Masai, E.; Sugiyama, K.; Iwashita, N.; Shimizu, S.; Hauschild, J.E.; Hatta, T.; Kimbara, K.; Yano, K.; Fukuda, M. The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA 1. Gene 1997, 187, 141-149.
    • (1997) Gene , vol.187 , pp. 141-149
    • Masai, E.1    Sugiyama, K.2    Iwashita, N.3    Shimizu, S.4    Hauschild, J.E.5    Hatta, T.6    Kimbara, K.7    Yano, K.8    Fukuda, M.9
  • 12
    • 0032819205 scopus 로고    scopus 로고
    • Purification and characterization of a novel naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038
    • Larkin, M.J.; Allen, C.C.R.; Kulakov, L.A.; Lipscomb, D.A. Purification and characterization of a novel naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038. J. Bacteriol. 1999, 181, 6200-6204.
    • (1999) J. Bacteriol , vol.181 , pp. 6200-6204
    • Larkin, M.J.1    Allen, C.C.R.2    Kulakov, L.A.3    Lipscomb, D.A.4
  • 13
    • 0033986797 scopus 로고    scopus 로고
    • Cloning and characterization of a novel cis-naphthalene dihyrodiol dehydrogenase gene (narB) from Rhodococcus sp. NCIMB12038
    • Kulakov, L.A.; Allen, C.C.R.; Lipscomb, D.A.; Larkin, M.J. Cloning and characterization of a novel cis-naphthalene dihyrodiol dehydrogenase gene (narB) from Rhodococcus sp. NCIMB12038. FEMS Microbiol. Lett. 2000, 182, 327-331.
    • (2000) FEMS Microbiol. Lett , vol.182 , pp. 327-331
    • Kulakov, L.A.1    Allen, C.C.R.2    Lipscomb, D.A.3    Larkin, M.J.4
  • 14
    • 0027250341 scopus 로고
    • Three different 2,3-dihydroxybiphenyl-1,2- dioxygenases in the Gram-positive polychlorobiphenyl-degrading Rhodococcus globerulus P6
    • Asturias, J.A.; Timmis, K.N. Three different 2,3-dihydroxybiphenyl-1,2- dioxygenases in the Gram-positive polychlorobiphenyl-degrading Rhodococcus globerulus P6. J. sBacteriol. 1993, 175, 4631-4640.
    • (1993) J. sBacteriol , vol.175 , pp. 4631-4640
    • Asturias, J.A.1    Timmis, K.N.2
  • 15
    • 33845641699 scopus 로고    scopus 로고
    • Specificity of catechol ortho-cleavage during para-toluate degradation by Rhodococcus opacus 1cp
    • Suvorova, M.V.; Solyanikova, I.P.; Golovleva, L.A. Specificity of catechol ortho-cleavage during para-toluate degradation by Rhodococcus opacus 1cp. Biochemistry (Russian) 2006, 71, 1316-1323.
    • (2006) Biochemistry (Russian) , vol.71 , pp. 1316-1323
    • Suvorova, M.V.1    Solyanikova, I.P.2    Golovleva, L.A.3
  • 16
    • 41349094501 scopus 로고    scopus 로고
    • Translated from Biokhimiya, 2006, 71, 1616-1624.
    • Translated from Biokhimiya, 2006, 71, 1616-1624.
  • 17
    • 0009632107 scopus 로고
    • Pyrocatechases of the Rhodococcus erythropolis strain - a chlorophenol destructor: Purification and properties
    • Maltseva, O.V.; Solyanikova, I.P.; Golovleva, L.A. Pyrocatechases of the Rhodococcus erythropolis strain - a chlorophenol destructor: purification and properties. Biokhimiya (Russian) 1991, 56, 2188-2197.
    • (1991) Biokhimiya (Russian) , vol.56 , pp. 2188-2197
    • Maltseva, O.V.1    Solyanikova, I.P.2    Golovleva, L.A.3
  • 18
    • 0028559891 scopus 로고
    • Chlorocatechol 1,2-dioxygenase from Rhodococcus erythropolis 1CP. Kinetic and immunochemical comparison with analogous enzymes from gram-negative strains
    • Maltseva, O.V.; Solyanikova, I.P.; Golovleva, L.A. Chlorocatechol 1,2-dioxygenase from Rhodococcus erythropolis 1CP. Kinetic and immunochemical comparison with analogous enzymes from gram-negative strains. Eur. J. Biochem. 1994, 226, 1053-1061.
    • (1994) Eur. J. Biochem , vol.226 , pp. 1053-1061
    • Maltseva, O.V.1    Solyanikova, I.P.2    Golovleva, L.A.3
  • 19
    • 0036777640 scopus 로고    scopus 로고
    • A new modified ortho-cleavage pathway of 2-chlorophenol degradation by Rhodococcus opacus 1CP: Genetic and biochemical evidences
    • Moiseeva, O.V.; Solyanikova, I.P.; Kaschabek, S.; Thiel, M.; Golovleva, L.A.; Schloemann, M. A new modified ortho-cleavage pathway of 2-chlorophenol degradation by Rhodococcus opacus 1CP: genetic and biochemical evidences. J.Bacteriol. 2002, 184, 5282-5292.
    • (2002) J.Bacteriol , vol.184 , pp. 5282-5292
    • Moiseeva, O.V.1    Solyanikova, I.P.2    Kaschabek, S.3    Thiel, M.4    Golovleva, L.A.5    Schloemann, M.6
  • 20
    • 0031024669 scopus 로고    scopus 로고
    • Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP
    • Eulberg, D.; Golovleva, L.A.; Schlömann, M. Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP. J. Bacteriol. 1997, 179, 370-381.
    • (1997) J. Bacteriol , vol.179 , pp. 370-381
    • Eulberg, D.1    Golovleva, L.A.2    Schlömann, M.3
  • 21
    • 0025159432 scopus 로고
    • Three isozymes of catechol 1,2-dioxygenas (pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1
    • Nakai, C.; Horiike, K.; Kuramitzu, S.; Kagamiyama, H.; and Nozaki, M. Three isozymes of catechol 1,2-dioxygenas (pyrocatechase), αα, αβ, and ββ, from Pseudomonas arvilla C-1. J. Biol. Chem. 1990, 265, 660-665.
    • (1990) J. Biol. Chem , vol.265 , pp. 660-665
    • Nakai, C.1    Horiike, K.2    Kuramitzu, S.3    Kagamiyama, H.4    Nozaki, M.5
  • 23
    • 0033590643 scopus 로고    scopus 로고
    • Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria species ANA-18
    • Murakami, S.; Takashima, A.; Takemoto, J.; Takinaka, S.; Shinke, R.; Aoki, K. Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria species ANA-18. Gene 1999, 226, 189-198.
    • (1999) Gene , vol.226 , pp. 189-198
    • Murakami, S.1    Takashima, A.2    Takemoto, J.3    Takinaka, S.4    Shinke, R.5    Aoki, K.6
  • 24
    • 0034468205 scopus 로고    scopus 로고
    • Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens
    • Briganti, F.; Pessione, E.; Giunta, C.; Mazzoli, R.; Scozzafava, A. Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens. J.Protein.Chem. 2000, 19, 709-716.
    • (2000) J.Protein.Chem , vol.19 , pp. 709-716
    • Briganti, F.1    Pessione, E.2    Giunta, C.3    Mazzoli, R.4    Scozzafava, A.5
  • 25
    • 0032087199 scopus 로고    scopus 로고
    • Purification and characterization of two muconate cycloisomerase isozymes from aniline-assimilating Frateuria species ANA-18
    • Murakami, S.; Takemoto, J.; Takashima, A.; Shinke, R.; Aoki, K. Purification and characterization of two muconate cycloisomerase isozymes from aniline-assimilating Frateuria species ANA-18. Biosci. Biotechnol. Biochem. 1998, 68, 1129-1133.
    • (1998) Biosci. Biotechnol. Biochem , vol.68 , pp. 1129-1133
    • Murakami, S.1    Takemoto, J.2    Takashima, A.3    Shinke, R.4    Aoki, K.5
  • 26
    • 0029795374 scopus 로고    scopus 로고
    • Harwood, C.S.; Parales, R.E. The β-ketoadipate pathway and the biology of self-identity. Annu. Rev. Microbiol. 1996, 50, 553-590.
    • Harwood, C.S.; Parales, R.E. The β-ketoadipate pathway and the biology of self-identity. Annu. Rev. Microbiol. 1996, 50, 553-590.
  • 27
    • 0017280757 scopus 로고
    • Properties of an inducible uptake system for β-ketoadipate in Pseudomonas putida
    • Ornston, L.N.; Parke, D. Properties of an inducible uptake system for β-ketoadipate in Pseudomonas putida. J. Bacteriol. 1976, 125, 475-488.
    • (1976) J. Bacteriol , vol.125 , pp. 475-488
    • Ornston, L.N.1    Parke, D.2
  • 28
    • 27744566414 scopus 로고    scopus 로고
    • The fluorene catabolic linear plasmid in Terrabacter sp. strain DBF63 carries the beta-ketoadipate pathway genes, pcaRHGBDCFIJ, also found in proteobacteria
    • Habe, H.; Chung, J.S.; Ishida, A.; Kasuga, K.; Ide, K.; Takemura, T.; Nojiri, H.; Yamane, H.; Omori, T. The fluorene catabolic linear plasmid in Terrabacter sp. strain DBF63 carries the beta-ketoadipate pathway genes, pcaRHGBDCFIJ, also found in proteobacteria. Microbiology 2005, 151, 3713-3722.
    • (2005) Microbiology , vol.151 , pp. 3713-3722
    • Habe, H.1    Chung, J.S.2    Ishida, A.3    Kasuga, K.4    Ide, K.5    Takemura, T.6    Nojiri, H.7    Yamane, H.8    Omori, T.9
  • 30
    • 0028106170 scopus 로고
    • Location of flavincontaining aromatic compound oxygenases from Rhodococcus erythropolis
    • Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y. Location of flavincontaining aromatic compound oxygenases from Rhodococcus erythropolis. J. Ferment. Bioeng. 1994, 78, 111-113.
    • (1994) J. Ferment. Bioeng , vol.78 , pp. 111-113
    • Suemori, A.1    Nakajima, K.2    Kurane, R.3    Nakamura, Y.4
  • 31
    • 0029846509 scopus 로고    scopus 로고
    • Temperature and detergent-dependent oligomeric structure of flavoprotein monohydroxybenzoate hydroxylases from Rhodococcus erythropolis
    • Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y. Temperature and detergent-dependent oligomeric structure of flavoprotein monohydroxybenzoate hydroxylases from Rhodococcus erythropolis. J. Ferment. Bioeng. 1996, 82, 174-176.
    • (1996) J. Ferment. Bioeng , vol.82 , pp. 174-176
    • Suemori, A.1    Nakajima, K.2    Kurane, R.3    Nakamura, Y.4
  • 32
    • 0022425431 scopus 로고
    • Purification and properties of NADH/NADPHdependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum
    • Fujii, T.; Kaneda, T. Purification and properties of NADH/NADPHdependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum. Eur. J. Biochem. 1985, 147, 97-104.
    • (1985) Eur. J. Biochem , vol.147 , pp. 97-104
    • Fujii, T.1    Kaneda, T.2
  • 33
    • 0035413245 scopus 로고    scopus 로고
    • Purification and properties of p-hydroxybenzoate hydroxylase from Rhodococcus strains
    • Jadan, A.P.; van Berkel, W.J.H.; Golovleva, L.A.; Golovlev, E.L. Purification and properties of p-hydroxybenzoate hydroxylase from Rhodococcus strains. Biochemistry (Russian) 2001, 66, 898-903.
    • (2001) Biochemistry (Russian) , vol.66 , pp. 898-903
    • Jadan, A.P.1    van Berkel, W.J.H.2    Golovleva, L.A.3    Golovlev, E.L.4
  • 35
    • 0035819564 scopus 로고    scopus 로고
    • Analysis of the pobA and pobR genes controlling expression of p-hydroxybenzoate hydroxylase in Azotobacter chroococcum
    • Quinn, J.A.; McKay, D.B.; Entsch, B. Analysis of the pobA and pobR genes controlling expression of p-hydroxybenzoate hydroxylase in Azotobacter chroococcum. Gene 2001, 264, 77-85.
    • (2001) Gene , vol.264 , pp. 77-85
    • Quinn, J.A.1    McKay, D.B.2    Entsch, B.3
  • 36
    • 41349119095 scopus 로고    scopus 로고
    • Bühler, M.; Schindler, J. Aliphatic hydrocarbons. In Biotransformations, 6a; Kieslich, K., Ed.; Verlag Chemie Weinheim: Weinheim, Germany, 1984; pp. 329-385.
    • Bühler, M.; Schindler, J. Aliphatic hydrocarbons. In Biotransformations, 6a; Kieslich, K., Ed.; Verlag Chemie Weinheim: Weinheim, Germany, 1984; pp. 329-385.
  • 37
    • 0025379301 scopus 로고
    • Bioconversions of aliphatic compounds by Pseudomonasoleovorans in multiphase bioreactors: Background and economic potential
    • Witholt, B.; de Smet, M.J.; Kingma, J.; van Beilen, J.B.; Kok, M.; Lageveen, R.G.; Eggink, G. Bioconversions of aliphatic compounds by Pseudomonasoleovorans in multiphase bioreactors: background and economic potential. Trends Biotechnol. 1990, 8, 46-52.
    • (1990) Trends Biotechnol , vol.8 , pp. 46-52
    • Witholt, B.1    de Smet, M.J.2    Kingma, J.3    van Beilen, J.B.4    Kok, M.5    Lageveen, R.G.6    Eggink, G.7
  • 38
    • 0036188547 scopus 로고    scopus 로고
    • Functional analysis of alkane hydroxylases from gram-negative and gram-positive bacteria
    • Smiths, T.H.M.; Balada, S.B.; Witholt, B.; van Beilen, J.B. Functional analysis of alkane hydroxylases from gram-negative and gram-positive bacteria. J. Bacteriol. 2002, 184, 6, 1733-1742.
    • (2002) J. Bacteriol , vol.184 , Issue.6 , pp. 1733-1742
    • Smiths, T.H.M.1    Balada, S.B.2    Witholt, B.3    van Beilen, J.B.4
  • 39
    • 0035119328 scopus 로고    scopus 로고
    • Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high molecularweight rubredoxin
    • Das, A.; Coulter, E.D.; Kurts, D.M.; Ljungdahl, L.G. Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high molecularweight rubredoxin. J.Bacteriol. 2001, 183, 1560-1567.
    • (2001) J.Bacteriol , vol.183 , pp. 1560-1567
    • Das, A.1    Coulter, E.D.2    Kurts, D.M.3    Ljungdahl, L.G.4
  • 40
    • 0025306810 scopus 로고
    • Ecological fate, effects and prospects for the elimination of environmental polychlorinaed biphenils (PCBs)
    • Hooper, S.W.; Pettigrew, C.A.; Sayler, C.S. Ecological fate, effects and prospects for the elimination of environmental polychlorinaed biphenils (PCBs). Environm. Toxicol. Chem. 1990, 9, 655-667.
    • (1990) Environm. Toxicol. Chem , vol.9 , pp. 655-667
    • Hooper, S.W.1    Pettigrew, C.A.2    Sayler, C.S.3
  • 41
    • 0018743211 scopus 로고
    • Comparative effects of Arochlor 1254 and phenanthrene on glucose uptake by freshwater microbial populations
    • Sayler, G.S.; Lund, L.C.; Shiaris, M.P.; Sherill, T.W.; Perkins, R.E. Comparative effects of Arochlor 1254 and phenanthrene on glucose uptake by freshwater microbial populations. Appl. Environ. Microbiol. 1979, 37, 878-885.
    • (1979) Appl. Environ. Microbiol , vol.37 , pp. 878-885
    • Sayler, G.S.1    Lund, L.C.2    Shiaris, M.P.3    Sherill, T.W.4    Perkins, R.E.5
  • 43
    • 0015759528 scopus 로고
    • Photodecomposition of chlorinated biphenyls and bibenzofurans
    • Crosby, D.G.; Moilamen, K.W. Photodecomposition of chlorinated biphenyls and bibenzofurans. Bull. Environ. Contam.Toxicol. 1973, 10, 372-377.
    • (1973) Bull. Environ. Contam.Toxicol , vol.10 , pp. 372-377
    • Crosby, D.G.1    Moilamen, K.W.2
  • 44
    • 0348055323 scopus 로고
    • The PCB problem: Separation fact from fiction
    • Feb
    • McGraw, M.G. The PCB problem: separation fact from fiction. Electrical World 1983, Feb., 49-72.
    • (1983) Electrical World , pp. 49-72
    • McGraw, M.G.1
  • 45
    • 0015540224 scopus 로고
    • Degradation of polychlorinated biphenyls by two species of Achromobacter
    • Ahmed, M.; Focht, D.D. Degradation of polychlorinated biphenyls by two species of Achromobacter. Can. J. Microbiol. 1973, 19, 47-52.
    • (1973) Can. J. Microbiol , vol.19 , pp. 47-52
    • Ahmed, M.1    Focht, D.D.2
  • 47
    • 0018306487 scopus 로고
    • Effect of chlorine substitution on the bacterial metabolism of various polychlorinated biphenyls
    • Furukawa, K.; Tomizuka, N.; Kamibayashi, A. Effect of chlorine substitution on the bacterial metabolism of various polychlorinated biphenyls. Appl. Environ. Microbiol. 1979, 38, 301-310.
    • (1979) Appl. Environ. Microbiol , vol.38 , pp. 301-310
    • Furukawa, K.1    Tomizuka, N.2    Kamibayashi, A.3
  • 49
    • 0020002259 scopus 로고
    • Biotransformation of PCB by natural assemblages of freshwater microorganisms
    • Shiaris, M.P.; Sayler, G.S. Biotransformation of PCB by natural assemblages of freshwater microorganisms. Environ. Sci. Technol. 1982, 16, 367-369.
    • (1982) Environ. Sci. Technol , vol.16 , pp. 367-369
    • Shiaris, M.P.1    Sayler, G.S.2
  • 50
    • 85006160523 scopus 로고
    • Isolation and characterization of a Gram-positive polychlorinated biphenyl-degrading bacterium, Rhodococcus erythropolis strain TA421, from a termite ecosystem
    • Chung, S.-Y.; Maede, M.; Song, E.; Horikoshi, K.; Kudo, T. Isolation and characterization of a Gram-positive polychlorinated biphenyl-degrading bacterium, Rhodococcus erythropolis strain TA421, from a termite ecosystem. Biosci. Biotechnol. Biochem. 1994, 58, 2111-2113.
    • (1994) Biosci. Biotechnol. Biochem , vol.58 , pp. 2111-2113
    • Chung, S.-Y.1    Maede, M.2    Song, E.3    Horikoshi, K.4    Kudo, T.5
  • 51
    • 0028797047 scopus 로고
    • Multiple genes encoding 2,3-dihydroxybiphenil 1,2-dioxygenase in the Gram-positive polychlorobiphenyl- degrading bacterium Rhodococcus erythropolis TA 421, isolated from a termit ecosystem
    • Maeda, M.; Chung, S.Y.; Song, E.; Kudo, T. Multiple genes encoding 2,3-dihydroxybiphenil 1,2-dioxygenase in the Gram-positive polychlorobiphenyl- degrading bacterium Rhodococcus erythropolis TA 421, isolated from a termit ecosystem. Appl. Enviromn. Microbiol. 1995, 61, 549-555.
    • (1995) Appl. Enviromn. Microbiol , vol.61 , pp. 549-555
    • Maeda, M.1    Chung, S.Y.2    Song, E.3    Kudo, T.4
  • 52
    • 10944255832 scopus 로고    scopus 로고
    • Biodegradation of seven polychlorinated biphenyls by a newly isolated aerobic bacterium (Rhodococcus sp. Ro4)
    • Yang, X.; Sun, Y.; Qian, S. Biodegradation of seven polychlorinated biphenyls by a newly isolated aerobic bacterium (Rhodococcus sp. Ro4). J. Ind. Biotechnol. 2004, 31, 415-420.
    • (2004) J. Ind. Biotechnol , vol.31 , pp. 415-420
    • Yang, X.1    Sun, Y.2    Qian, S.3
  • 53
    • 0028971916 scopus 로고
    • Sequence and expression of the bpdC1C2BADE genes involved in the initial steps of biphenyl/chlorobiphenyl degradation by Rhodococcus sp. M5
    • Wang, Y.; Garnon, J.; Labbe, D.; Bergeron, H.; Lau, P.C.K. Sequence and expression of the bpdC1C2BADE genes involved in the initial steps of biphenyl/chlorobiphenyl degradation by Rhodococcus sp. M5. Gene 1995, 164, 117-122.
    • (1995) Gene , vol.164 , pp. 117-122
    • Wang, Y.1    Garnon, J.2    Labbe, D.3    Bergeron, H.4    Lau, P.C.K.5
  • 54
    • 0029128756 scopus 로고
    • A novel transformation of polychlorinated biphenyls by Rhodococcus sp. strain RHA1
    • Seto, M.; Kimbara, K.; Shimura, M.; Hatta, T.; Fukuda, M.; Yado, K. A novel transformation of polychlorinated biphenyls by Rhodococcus sp. strain RHA1. Appl. Environm. Microbiol. 1995, 61, 3353-3358.
    • (1995) Appl. Environm. Microbiol , vol.61 , pp. 3353-3358
    • Seto, M.1    Kimbara, K.2    Shimura, M.3    Hatta, T.4    Fukuda, M.5    Yado, K.6
  • 55
    • 0031779621 scopus 로고    scopus 로고
    • Two nearly identical aromatic compound hydrolase genes in a strong polychlorobiphenyl degrader, Rhodococcus sp. strain RHA1
    • Yamada, A.; Kishi, H.; Sugiyama, K.; Nakamura, K.; Masai, E.; Fukuda, M. Two nearly identical aromatic compound hydrolase genes in a strong polychlorobiphenyl degrader, Rhodococcus sp. strain RHA1. Appl. Environm. Microbiol. 1998, 64, 2006-2012.
    • (1998) Appl. Environm. Microbiol , vol.64 , pp. 2006-2012
    • Yamada, A.1    Kishi, H.2    Sugiyama, K.3    Nakamura, K.4    Masai, E.5    Fukuda, M.6
  • 56
    • 3042802019 scopus 로고    scopus 로고
    • New aerobic Gram-positive mircoorganism with exceptional abilities to degrade ortho- and para-chlorinated biphenyls
    • Rybkina, D.O.; Plotnikova, E.G.; Dorofeeva, L.V.; Mironenko, Y.L.; Demakov, V.A. New aerobic Gram-positive mircoorganism with exceptional abilities to degrade ortho- and para-chlorinated biphenyls. Microbiologiya (Russian) 2003, 72, 759-765.
    • (2003) Microbiologiya (Russian) , vol.72 , pp. 759-765
    • Rybkina, D.O.1    Plotnikova, E.G.2    Dorofeeva, L.V.3    Mironenko, Y.L.4    Demakov, V.A.5
  • 57
    • 0033600133 scopus 로고    scopus 로고
    • cis-2,3-Dihydro-2,3-dihydroxybiphenyl dehydrogenase and cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase catalyze dehydrogenation of the same range of substrates
    • Barriault, D.; Vedadi, M.; Powlowski, J.; Sylvestre, M. cis-2,3-Dihydro-2,3-dihydroxybiphenyl dehydrogenase and cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase catalyze dehydrogenation of the same range of substrates. Biochem. Biophys.Res. Commun. 1999, 260, 181-187.
    • (1999) Biochem. Biophys.Res. Commun , vol.260 , pp. 181-187
    • Barriault, D.1    Vedadi, M.2    Powlowski, J.3    Sylvestre, M.4
  • 58
    • 11844284911 scopus 로고    scopus 로고
    • Evolutionary devergent extradiol dioxygenases possess higher specificities for polychlorinated biphenyl metabolites
    • Fortin, P.D.; Lo, A.T.-F.; Haro, M.-A.; Kashabek S.-R.; Reineke, W.; Eltis, L.D. Evolutionary devergent extradiol dioxygenases possess higher specificities for polychlorinated biphenyl metabolites. J. Bacteriol. 2005, 187, 415-421.
    • (2005) J. Bacteriol , vol.187 , pp. 415-421
    • Fortin, P.D.1    Lo, A.T.-F.2    Haro, M.-A.3    Kashabek, S.-R.4    Reineke, W.5    Eltis, L.D.6
  • 59
    • 84907112796 scopus 로고
    • Aerobic and anaerobic biodegradation of PCBs: A review
    • Abramowicz, D.A. Aerobic and anaerobic biodegradation of PCBs: a review. Crit. Rev. Biotechnol. 1990, 10, 241-251.
    • (1990) Crit. Rev. Biotechnol , vol.10 , pp. 241-251
    • Abramowicz, D.A.1
  • 60
    • 0030803913 scopus 로고    scopus 로고
    • Tree of the seven bphC genes of Rhodococcus eruthropolis TA421, isolated from a termite ecosystem, are located on an indigenous plasmid associated with biphenyl degradation
    • Kosoma, S.; Maeda, M.; Fuji, F.; Arai, H.; Kudo, T. Tree of the seven bphC genes of Rhodococcus eruthropolis TA421, isolated from a termite ecosystem, are located on an indigenous plasmid associated with biphenyl degradation. Appl. Environ. Microbiol. 1997, 63, 3282-3285.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 3282-3285
    • Kosoma, S.1    Maeda, M.2    Fuji, F.3    Arai, H.4    Kudo, T.5
  • 62
    • 41349121732 scopus 로고    scopus 로고
    • Plotnikova, E.G, Rybkina, D.O, Demakov, V.A. Strain Rhodococcus ruber, destructor of polichlorinated biphenyls. Patent No. 2262531. 2005
    • Plotnikova, E.G.; Rybkina, D.O.; Demakov, V.A. Strain Rhodococcus ruber - destructor of polichlorinated biphenyls. Patent No. 2262531. 2005.
  • 63
    • 0025056536 scopus 로고
    • DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: Evidence indicating shuffling of genes and of DNA sequences withing genes during their evolutionary vivergence
    • Hartnet, C.; Neidle, E.L.; Ngai, K.-L.; Ornston, L.N. DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: evidence indicating shuffling of genes and of DNA sequences withing genes during their evolutionary vivergence. J. Bacteriol. 1990, 172, 956-966.
    • (1990) J. Bacteriol , vol.172 , pp. 956-966
    • Hartnet, C.1    Neidle, E.L.2    Ngai, K.-L.3    Ornston, L.N.4
  • 64
    • 0033025299 scopus 로고    scopus 로고
    • Molecular characterization of the genes pcaG and pcaH, encoding protocatechate 3,4-dioxygenase, which are essential for vanillin catabolism in Pseudomonas sp. strain HR 199
    • Overhage, J.A.; Kresse, U.; Priefert, H.; Sommer, H.; Krammer, G.; Rabenhorst, J.; Steinbüchel, A. Molecular characterization of the genes pcaG and pcaH, encoding protocatechate 3,4-dioxygenase, which are essential for vanillin catabolism in Pseudomonas sp. strain HR 199. Appl. Environ. Microbiol. 1999, 65, 951-960.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 951-960
    • Overhage, J.A.1    Kresse, U.2    Priefert, H.3    Sommer, H.4    Krammer, G.5    Rabenhorst, J.6    Steinbüchel, A.7
  • 65
    • 0034636805 scopus 로고    scopus 로고
    • Structure of Acinetobacter sp. ADP1 protocatechuate 3,4-dioxygenase at 2.2 Å resolution: Implications for the mechanisms of an intradiol dioxygenase
    • Vetting, M.W.; D'Argenio, D.A.; Ornston, L.N.; Ohlendorf, D.H. Structure of Acinetobacter sp. ADP1 protocatechuate 3,4-dioxygenase at 2.2 Å resolution: implications for the mechanisms of an intradiol dioxygenase. Biochemistry, 2000, 39, 7943-7955.
    • (2000) Biochemistry , vol.39 , pp. 7943-7955
    • Vetting, M.W.1    D'Argenio, D.A.2    Ornston, L.N.3    Ohlendorf, D.H.4
  • 67
    • 0026715272 scopus 로고
    • The biology and genetics of the genus Rhodococcus
    • Finnerty, W.R. The biology and genetics of the genus Rhodococcus. Ann. Rev. Microbiol. 1992, 46, 193-218.
    • (1992) Ann. Rev. Microbiol , vol.46 , pp. 193-218
    • Finnerty, W.R.1
  • 70
    • 0036024817 scopus 로고    scopus 로고
    • Gordonia (nocardia) amarae foaming due to biosurfactant production
    • Pagilla, K.R.; Sood, A.; Kim, H. Gordonia (nocardia) amarae foaming due to biosurfactant production. Water Sci Technol. 2002, 46, 519-524.
    • (2002) Water Sci Technol , vol.46 , pp. 519-524
    • Pagilla, K.R.1    Sood, A.2    Kim, H.3
  • 71
    • 0029980555 scopus 로고    scopus 로고
    • Significance of bacterial surface-active compounds in interaction of bacteria with interfaces
    • Neu, T.R. Significance of bacterial surface-active compounds in interaction of bacteria with interfaces. Microbiol. Rev. 1996, 60, 151-166.
    • (1996) Microbiol. Rev , vol.60 , pp. 151-166
    • Neu, T.R.1
  • 72
    • 0026642213 scopus 로고
    • Biosurfactants: Moving toward industrial application
    • Fiechter, A. Biosurfactants: moving toward industrial application. Trends in Biotechnol. 1992, 10, 208-217.
    • (1992) Trends in Biotechnol , vol.10 , pp. 208-217
    • Fiechter, A.1
  • 73
    • 0028335202 scopus 로고
    • Biosurfactants in environmental biotechnology
    • Finnerty, W.R. Biosurfactants in environmental biotechnology. Curr. Opin. Biotechnol. 1994, 5, 291-295.
    • (1994) Curr. Opin. Biotechnol , vol.5 , pp. 291-295
    • Finnerty, W.R.1
  • 74
    • 41349098280 scopus 로고    scopus 로고
    • Philp, J.C.; Bell, K.S. Applied studies with bacteria of the genus Rhodococcus relevant to treatment of land and water contaminated by industrial process. In Pros. Intern. Symp. Industr. Environm., Taelon Natl. Uni. Technol.: Seoul, Korea, 1995, pp. 105-126.
    • Philp, J.C.; Bell, K.S. Applied studies with bacteria of the genus Rhodococcus relevant to treatment of land and water contaminated by industrial process. In Pros. Intern. Symp. Industr. Environm., Taelon Natl. Uni. Technol.: Seoul, Korea, 1995, pp. 105-126.
  • 75
    • 84950324579 scopus 로고
    • Nutritional requirements and growth characteristics of a biosurfactant producing Rhodocccus bacterium
    • Abu-Ruwaida, A.S.; Banat, I.M.; Haditirto, S.; Khamis, A. Nutritional requirements and growth characteristics of a biosurfactant producing Rhodocccus bacterium. World J. Microbiol. Biotechnol. 1991, 7, 53-61.
    • (1991) World J. Microbiol. Biotechnol , vol.7 , pp. 53-61
    • Abu-Ruwaida, A.S.1    Banat, I.M.2    Haditirto, S.3    Khamis, A.4
  • 76
    • 0032461944 scopus 로고    scopus 로고
    • Biological treatment of crude oil contaminated soil in Russia
    • Lerner, D.N, Walton, N.R.G, Eds, Engineering Geology Special Publication 14; Geological Soc: London
    • Christofi, N.; Ivshina, I.B.; Kuyukina, M.S.; Philp, J.C. Biological treatment of crude oil contaminated soil in Russia. In Cantaminated Land and Groundwater: Future Directions, Lerner, D.N., Walton, N.R.G., Eds.; Engineering Geology Special Publication 14; Geological Soc: London, 1998; pp. 45-51.
    • (1998) Cantaminated Land and Groundwater: Future Directions , pp. 45-51
    • Christofi, N.1    Ivshina, I.B.2    Kuyukina, M.S.3    Philp, J.C.4
  • 77
    • 0029793755 scopus 로고    scopus 로고
    • Screening and selection of surfactant-producing bacteria from waste lubrication oil
    • Mercade, M.E.; Monleon, L.; Deandres, C. Screening and selection of surfactant-producing bacteria from waste lubrication oil. J. Appl. Bacteriol. 1996, 81, 161-166.
    • (1996) J. Appl. Bacteriol , vol.81 , pp. 161-166
    • Mercade, M.E.1    Monleon, L.2    Deandres, C.3
  • 78
    • 0028308116 scopus 로고
    • Cesium accumulation and growth characteristics of Rhodococcus erythropolis CS98 and Rhodococcus sp. strain CS402
    • Tomioka, N.; Uchiyama, H.; Yagi, O. Cesium accumulation and growth characteristics of Rhodococcus erythropolis CS98 and Rhodococcus sp. strain CS402. Appl. Environm. Microbiol. 1994, 60, 2227-2231.
    • (1994) Appl. Environm. Microbiol , vol.60 , pp. 2227-2231
    • Tomioka, N.1    Uchiyama, H.2    Yagi, O.3
  • 80
    • 41349098502 scopus 로고    scopus 로고
    • Transformation of steroides by aktinobacterium
    • Donova, M.V. Transformation of steroides by aktinobacterium. Applied Biochem Microbiol. (Russian) 2006, 43, 1-12.
    • (2006) Applied Biochem Microbiol. (Russian) , vol.43 , pp. 1-12
    • Donova, M.V.1
  • 82
    • 0037335928 scopus 로고    scopus 로고
    • Synthesis of imidazol-2-yl amino acids by using cells from alkane-oxidizing bacteria
    • Mikolasch, A.; Hammer, E.; Schauer, F. Synthesis of imidazol-2-yl amino acids by using cells from alkane-oxidizing bacteria. Appl. Environ. Microbiol. 2003, 69, 1670-1679.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 1670-1679
    • Mikolasch, A.1    Hammer, E.2    Schauer, F.3
  • 83
    • 33847034113 scopus 로고    scopus 로고
    • Bacterial preparation of enantiopure unactivated aziridine-2-carboxamides and their transformation into enantiopure nonnatural amino acids and vicdiamines
    • Moran-Ramallal, R.; Liz, R.; Gotor, V. Bacterial preparation of enantiopure unactivated aziridine-2-carboxamides and their transformation into enantiopure nonnatural amino acids and vicdiamines. Org Lett. 2007, 1, 521-524.
    • (2007) Org Lett , vol.1 , pp. 521-524
    • Moran-Ramallal, R.1    Liz, R.2    Gotor, V.3
  • 84
    • 0037031629 scopus 로고    scopus 로고
    • Practical and convenient enzymatic synthesis of enantiopure alpha-amino acids and amides
    • Wang, M.X.; Lin, S.J. Practical and convenient enzymatic synthesis of enantiopure alpha-amino acids and amides. J. Org. Chem. 2002, 67, 6542-6545.
    • (2002) J. Org. Chem , vol.67 , pp. 6542-6545
    • Wang, M.X.1    Lin, S.J.2
  • 85
    • 17044374655 scopus 로고    scopus 로고
    • Nitrile biotransformations for highly enantioselective synthesis of oxiranecarboxamides with tertiary and quaternary stereocenters; efficient chemoenzymatic approaches to enantiopure alpha-methylated serine and isoserine derivatives
    • Wang, M.X.; Deng, G.; Wang, D.X.; Zheng, Q.Y. Nitrile biotransformations for highly enantioselective synthesis of oxiranecarboxamides with tertiary and quaternary stereocenters; efficient chemoenzymatic approaches to enantiopure alpha-methylated serine and isoserine derivatives. J Org Chem. 2005, 70, 2439-2444.
    • (2005) J Org Chem , vol.70 , pp. 2439-2444
    • Wang, M.X.1    Deng, G.2    Wang, D.X.3    Zheng, Q.Y.4
  • 86
    • 0029996889 scopus 로고    scopus 로고
    • Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides
    • Hirrlinger, B.; Stolz, A.; Knackmuss, H.J. Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides. J. Bacteriol. 1996, 178, 3501-3507.
    • (1996) J. Bacteriol , vol.178 , pp. 3501-3507
    • Hirrlinger, B.1    Stolz, A.2    Knackmuss, H.J.3
  • 87
    • 0037423457 scopus 로고    scopus 로고
    • Highly enantioselective synthesis of alpha, alpha-disubstituted malonamic acids through asymmetric hydrolysis of dinitriles with Rhodococcus sp. CGMCC 0497
    • Wu, Z.L.; Li, Z.Y. Highly enantioselective synthesis of alpha, alpha-disubstituted malonamic acids through asymmetric hydrolysis of dinitriles with Rhodococcus sp. CGMCC 0497. Chem. Commun. (Camb) 2003, 7, 386-387.
    • (2003) Chem. Commun. (Camb) , vol.7 , pp. 386-387
    • Wu, Z.L.1    Li, Z.Y.2
  • 88
    • 0028478144 scopus 로고
    • Enzyme-catalysed enantioselective hydrolysis of racemic naproxen nitrile
    • Effenberger, F.; Bohme, J. Enzyme-catalysed enantioselective hydrolysis of racemic naproxen nitrile. Bioorg Med Chem. 1994, 2, 715-721.
    • (1994) Bioorg Med Chem , vol.2 , pp. 715-721
    • Effenberger, F.1    Bohme, J.2
  • 89
    • 33748632359 scopus 로고    scopus 로고
    • A novel NADP+-dependent L-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: A promising enzyme for the production of double chiral aminoalcohols
    • Kataoka, M.; Nakamura, Y.; Urano, N.; Ishige, T.; Shi, G.; Kita, S.; Sakamoto, K.; Shimizu, S. A novel NADP+-dependent L-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols. Lett. Appl. Microbiol. 2006, 43, 430-435.
    • (2006) Lett. Appl. Microbiol , vol.43 , pp. 430-435
    • Kataoka, M.1    Nakamura, Y.2    Urano, N.3    Ishige, T.4    Shi, G.5    Kita, S.6    Sakamoto, K.7    Shimizu, S.8
  • 90
    • 33645120633 scopus 로고    scopus 로고
    • Enhanced biodegradation of diesel oil by a newly identified Rhodococcus baikonurensis EN3 in the presence ofmycolic acid
    • Lee, M.; Kim, M.K.; Singleton, I.; Goodfellow, M.; Lee, S.T.J. Enhanced biodegradation of diesel oil by a newly identified Rhodococcus baikonurensis EN3 in the presence ofmycolic acid. Appl. Microbiol. 2006, 100, 325-33.
    • (2006) Appl. Microbiol , vol.100 , pp. 325-333
    • Lee, M.1    Kim, M.K.2    Singleton, I.3    Goodfellow, M.4    Lee, S.T.J.5
  • 91
    • 31844434048 scopus 로고    scopus 로고
    • Effect of the synthesized mycolic acid on the biodegradation of diesel oil by Gordonia nitida strain LE31
    • Lee, M.; Kim, M.K.; Kwon, M.J.; Park, B.D.; Kim, M.H.; Goodfellow, M.; Lee, S.T. Effect of the synthesized mycolic acid on the biodegradation of diesel oil by Gordonia nitida strain LE31. J. Biosci. Bioeng. 2005, 100, 429-436.
    • (2005) J. Biosci. Bioeng , vol.100 , pp. 429-436
    • Lee, M.1    Kim, M.K.2    Kwon, M.J.3    Park, B.D.4    Kim, M.H.5    Goodfellow, M.6    Lee, S.T.7
  • 92
    • 27144487443 scopus 로고    scopus 로고
    • Toxic effect of biosurfactant addition on the biodegradation of phenanthrene
    • Shin, K.H.; Ahn, Y.; Kim, K.W. Toxic effect of biosurfactant addition on the biodegradation of phenanthrene. Environ. Toxicol. Chem. 2005, 24, 2768-2774.
    • (2005) Environ. Toxicol. Chem , vol.24 , pp. 2768-2774
    • Shin, K.H.1    Ahn, Y.2    Kim, K.W.3
  • 93
    • 0030870287 scopus 로고    scopus 로고
    • Nocardioides pyridinolyticus sp. nov., a pyridine-degrading bacterium isolated from the oxic zone of an oil shale column
    • Yoon, J.H.; Rhee, S.K.; Lee, J.S.; Park, Y.H.; Lee, S.T. Nocardioides pyridinolyticus sp. nov., a pyridine-degrading bacterium isolated from the oxic zone of an oil shale column. Int. J. Syst. Bacteriol. 1997, 47, 933-938.
    • (1997) Int. J. Syst. Bacteriol , vol.47 , pp. 933-938
    • Yoon, J.H.1    Rhee, S.K.2    Lee, J.S.3    Park, Y.H.4    Lee, S.T.5
  • 94
    • 0036324296 scopus 로고    scopus 로고
    • Plasmid-borne genes code for an angular dioxygenase involved in dibenzofuran degradation by Terrabacter sp. strain YK3
    • Iida, T.; Mukouzaka, Y.; Nakamura, K.; Kudo, T. Plasmid-borne genes code for an angular dioxygenase involved in dibenzofuran degradation by Terrabacter sp. strain YK3. Appl. Environ. Microbiol. 2002, 68, 3716-3723.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 3716-3723
    • Iida, T.1    Mukouzaka, Y.2    Nakamura, K.3    Kudo, T.4
  • 95
    • 0031020094 scopus 로고    scopus 로고
    • Characterization of three distinct extradiol dioxygenases involved in mineralization of dibenzofuran by Terrabacter sp. strain DPO360
    • Schmid, A.; Rothe, B.; Altenbuchner, J.; Ludwig, W.; Engesser, K.H. Characterization of three distinct extradiol dioxygenases involved in mineralization of dibenzofuran by Terrabacter sp. strain DPO360. J. Bacteriol. 1997, 179, 53-62.
    • (1997) J. Bacteriol , vol.179 , pp. 53-62
    • Schmid, A.1    Rothe, B.2    Altenbuchner, J.3    Ludwig, W.4    Engesser, K.H.5
  • 96
    • 0027030557 scopus 로고
    • Cloning of DNA from Rhodococcus strains conferring the ability to decolorize sulfonated azo dyes
    • Heiss, G.S.; Gowan, B.; Dabbs, E.R. Cloning of DNA from Rhodococcus strains conferring the ability to decolorize sulfonated azo dyes. FEMS Microbiol. Lett. 1992, 99, 221-226.
    • (1992) FEMS Microbiol. Lett , vol.99 , pp. 221-226
    • Heiss, G.S.1    Gowan, B.2    Dabbs, E.R.3
  • 97
    • 34547485940 scopus 로고    scopus 로고
    • Isolation and characterization of novel atrazine-degrading microorganisms from an agricultural soil
    • Vibber, L.L.; Pressler, M.J.; Colores, G.M. Isolation and characterization of novel atrazine-degrading microorganisms from an agricultural soil. Appl Microbiol Biotechnol. 2007, 21.
    • (2007) Appl Microbiol Biotechnol , vol.21
    • Vibber, L.L.1    Pressler, M.J.2    Colores, G.M.3
  • 98
    • 33645663558 scopus 로고    scopus 로고
    • Characterisation of new strains of atrazine-degrading Nocardioides sp. isolated from Japanese riverbed sediment using naturally derived river ecosystem
    • Satsuma, K. Characterisation of new strains of atrazine-degrading Nocardioides sp. isolated from Japanese riverbed sediment using naturally derived river ecosystem. Pest. Manag. Sci. 2006, 62, 340-349.
    • (2006) Pest. Manag. Sci , vol.62 , pp. 340-349
    • Satsuma, K.1
  • 99
    • 0027988659 scopus 로고
    • Rapid degradation of the triazinone herbicide metamitron by a Rhodococcus sp. isolated from treated soil
    • Parekh, N.R.; Walker, A.; Roberts, S.J.; Welch, S.J. Rapid degradation of the triazinone herbicide metamitron by a Rhodococcus sp. isolated from treated soil. J. Appl. Bacteriol. 1994, 77, 467-475.
    • (1994) J. Appl. Bacteriol , vol.77 , pp. 467-475
    • Parekh, N.R.1    Walker, A.2    Roberts, S.J.3    Welch, S.J.4
  • 100
    • 0001680080 scopus 로고
    • Ring hydroxylation of N-methylcarbamate insecticides by Rhodococcus TE1
    • Behki, R.M.; Topp, E.E.; Blackwell, B.A. Ring hydroxylation of N-methylcarbamate insecticides by Rhodococcus TE1. J. Agric. Food Chem. 1994, 42, 1375-1378.
    • (1994) J. Agric. Food Chem , vol.42 , pp. 1375-1378
    • Behki, R.M.1    Topp, E.E.2    Blackwell, B.A.3
  • 101
  • 102
    • 33846121587 scopus 로고    scopus 로고
    • Metabolite production in degradation of pyrene alone or in a mixture with another polycyclic aromatic hydrocarbon by Mycobacterium sp
    • Zhong, Y.; Luan, T.; Zhou, H.; Lan, C.; Tam, N.F. Metabolite production in degradation of pyrene alone or in a mixture with another polycyclic aromatic hydrocarbon by Mycobacterium sp. Environ Toxicol Chem. 2006, 25, 2853-2859.
    • (2006) Environ Toxicol Chem , vol.25 , pp. 2853-2859
    • Zhong, Y.1    Luan, T.2    Zhou, H.3    Lan, C.4    Tam, N.F.5
  • 103
    • 0035653255 scopus 로고    scopus 로고
    • Identification of a novel metabolite in the degradation of pyrene by Mycobacterium sp. strain AP1: Actions of the isolate on two- and three-ring polycyclic aromatic hydrocarbons
    • Vila, J.; Lopez, Z.; Sabate, J.; Minguillon, C.; Solanas, A.M.; Grifoll, M. Identification of a novel metabolite in the degradation of pyrene by Mycobacterium sp. strain AP1: actions of the isolate on two- and three-ring polycyclic aromatic hydrocarbons. Appl. Environ. Microbiol. 2001, 67, 5497-505.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 5497-5505
    • Vila, J.1    Lopez, Z.2    Sabate, J.3    Minguillon, C.4    Solanas, A.M.5    Grifoll, M.6
  • 104
    • 27444443398 scopus 로고    scopus 로고
    • Metabolism of fluoranthene by mycobacterial strains isolated by their ability to grow in fluoranthene or pyrene
    • Lopez, Z.; Vila, J.; Grifoll, M. Metabolism of fluoranthene by mycobacterial strains isolated by their ability to grow in fluoranthene or pyrene. J. Ind. Microbiol. Biotechnol. 2005, 32, 455-64.
    • (2005) J. Ind. Microbiol. Biotechnol , vol.32 , pp. 455-464
    • Lopez, Z.1    Vila, J.2    Grifoll, M.3
  • 105
    • 0036141651 scopus 로고    scopus 로고
    • The effect of polycyclic aromatic hydrocarbons on the degradation of benzo[a]pyrene by Mycobacterium sp. strain RJGII-135
    • McLellan, S.L.; Warshawsky, D.; Shann, J.R. The effect of polycyclic aromatic hydrocarbons on the degradation of benzo[a]pyrene by Mycobacterium sp. strain RJGII-135. Environ. Toxicol. Chem. 2002, 21, 253-259.
    • (2002) Environ. Toxicol. Chem , vol.21 , pp. 253-259
    • McLellan, S.L.1    Warshawsky, D.2    Shann, J.R.3
  • 106
    • 0034034019 scopus 로고    scopus 로고
    • A novel phenanthrene dioxygenase from Nocardioides sp. Strain KP7: Expression in Escherichia coli
    • Saito, A.; Iwabuchi, T.; Harayama, S. A novel phenanthrene dioxygenase from Nocardioides sp. Strain KP7: expression in Escherichia coli. J Bacteriol. 2000, 182, 2134-2141.
    • (2000) J Bacteriol , vol.182 , pp. 2134-2141
    • Saito, A.1    Iwabuchi, T.2    Harayama, S.3
  • 107
    • 0037870591 scopus 로고    scopus 로고
    • Effects of aromatics on the degradation of benzo(a) pyrene in slurry reactors
    • Gong, Z.; Li, P.; Wang, X.; Tai, P.; Zhang, H. Effects of aromatics on the degradation of benzo(a) pyrene in slurry reactors. Huan Jing Ke Xue 2002, 23, 69-73.
    • (2002) Huan Jing Ke Xue , vol.23 , pp. 69-73
    • Gong, Z.1    Li, P.2    Wang, X.3    Tai, P.4    Zhang, H.5
  • 108
    • 0034526279 scopus 로고    scopus 로고
    • Two-liquid-phase slurry bioreactors to enhance the degradation of high-molecular-weight polycyclic aromatic hydrocarbons in soil
    • Villemur, R.; Deziel, E.; Benachenhou, A.; Marcoux, J.; Gauthier, E.; Lepine, F.; Beaudet, R.; Comeau, Y. Two-liquid-phase slurry bioreactors to enhance the degradation of high-molecular-weight polycyclic aromatic hydrocarbons in soil. Biotechnol Prog. 2000, 16, 966-972.
    • (2000) Biotechnol Prog , vol.16 , pp. 966-972
    • Villemur, R.1    Deziel, E.2    Benachenhou, A.3    Marcoux, J.4    Gauthier, E.5    Lepine, F.6    Beaudet, R.7    Comeau, Y.8
  • 110
    • 0034772598 scopus 로고    scopus 로고
    • Enhanced biodegradation of methylhydrazine and hydrazine contaminated NASA wastewater in fixed-film bioreactor
    • Nwankwoala, A.U.; Egiebor, N.O.; Nyavor, K. Enhanced biodegradation of methylhydrazine and hydrazine contaminated NASA wastewater in fixed-film bioreactor. Biodegradation 2001, 12, 1-10.
    • (2001) Biodegradation , vol.12 , pp. 1-10
    • Nwankwoala, A.U.1    Egiebor, N.O.2    Nyavor, K.3
  • 111
    • 0036158681 scopus 로고    scopus 로고
    • Formaldehyde removal in synthetic and industrial wastewater by Rhodococcus erythropolis UPV-1
    • Hidalgo, A.; Lopategi, A.; Prieto, M.; Serra, J.L.; Llama, M.J. Formaldehyde removal in synthetic and industrial wastewater by Rhodococcus erythropolis UPV-1. Appl. Microbiol. Biotechnol. 2002, 58, 260-263.
    • (2002) Appl. Microbiol. Biotechnol , vol.58 , pp. 260-263
    • Hidalgo, A.1    Lopategi, A.2    Prieto, M.3    Serra, J.L.4    Llama, M.J.5
  • 112
    • 0020681427 scopus 로고
    • Microbial Treatment of soil to remove pentachlorophenol
    • Edgehill, R.U.; Finn, R.K. Microbial Treatment of soil to remove pentachlorophenol. Appl. Envir. Microbiol. 1983, 45, 1122-1125.
    • (1983) Appl. Envir. Microbiol , vol.45 , pp. 1122-1125
    • Edgehill, R.U.1    Finn, R.K.2
  • 113
    • 0035986631 scopus 로고    scopus 로고
    • Degradation characteristics of a dibenzofuran-degrader Terrabacter sp. strain DBF63 toward chlorinated dioxins in soil
    • Habe, H.; Ide, K.; Yotsumoto, M.; Tsuji, H.; Yoshida, T.; Nojiri, H.; Omori, T. Degradation characteristics of a dibenzofuran-degrader Terrabacter sp. strain DBF63 toward chlorinated dioxins in soil. Chemosphere 2002, 48, 201-207.
    • (2002) Chemosphere , vol.48 , pp. 201-207
    • Habe, H.1    Ide, K.2    Yotsumoto, M.3    Tsuji, H.4    Yoshida, T.5    Nojiri, H.6    Omori, T.7
  • 115
    • 34147173369 scopus 로고    scopus 로고
    • A model study of pesticide biodegradation in soil
    • Bieganska, J. A model study of pesticide biodegradation in soil. Izv. RAS. Biology 2007, 1, 91-101.
    • (2007) Izv. RAS. Biology , vol.1 , pp. 91-101
    • Bieganska, J.1
  • 116
    • 0032897686 scopus 로고    scopus 로고
    • Cavalca, L.; Hartmann, A.; Rouard, N.; Soulas, G. Diversity of tfdC genes: distribution and polymorphism among 2,4-dichlorophenoxyacetic acid degrading soil bacteria. FEMS Microbiol. Ecol. 1999, 29, 45-58.
    • Cavalca, L.; Hartmann, A.; Rouard, N.; Soulas, G. Diversity of tfdC genes: distribution and polymorphism among 2,4-dichlorophenoxyacetic acid degrading soil bacteria. FEMS Microbiol. Ecol. 1999, 29, 45-58.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.