메뉴 건너뛰기




Volumn 99, Issue 7, 2008, Pages 2187-2191

Erratum to "Decolorization kinetics of a recombinant Escherichia coli strain harbouring azoreductase gene from Bacillus latrosporous RRK1" [Bioresource Technology 99 (2008) 2187-2191] (DOI:10.1016/j.biortech.2007.05.027);Decolorizing kinetics of a recombinant Escherichia coli SS125 strain harboring azoreductase gene from Bacillus latrosporus RRK1

Author keywords

Azo dyes; Azoreductase gene; Decolorization; Recombinant

Indexed keywords

ANAEROBIC DIGESTION; AZO DYES; CONCENTRATION (PROCESS); REACTION KINETICS;

EID: 38849197080     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2008.08.030     Document Type: Erratum
Times cited : (37)

References (21)
  • 1
    • 0036324837 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F
    • Blumel S., Knackmuss H.J., and Stolz A. Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appli. Environ. Microbiol. 68 (2002) 3948-3955
    • (2002) Appli. Environ. Microbiol. , vol.68 , pp. 3948-3955
    • Blumel, S.1    Knackmuss, H.J.2    Stolz, A.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 0035028105 scopus 로고    scopus 로고
    • Decolorization of an azo dye with recombinant Escherichia coli strain harboring azo-dye-decolorizing determinants from Rhodococcus sp
    • Chang J.S., and Lin C.Y. Decolorization of an azo dye with recombinant Escherichia coli strain harboring azo-dye-decolorizing determinants from Rhodococcus sp. Biotechnol. Lett. 23 (2001) 631-636
    • (2001) Biotechnol. Lett. , vol.23 , pp. 631-636
    • Chang, J.S.1    Lin, C.Y.2
  • 5
    • 1642354143 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis
    • Chen H., Wang R.F., and Cerniglia C.E. Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis. Protein Express. Purif. 34 (2004) 302-310
    • (2004) Protein Express. Purif. , vol.34 , pp. 302-310
    • Chen, H.1    Wang, R.F.2    Cerniglia, C.E.3
  • 6
    • 0027703470 scopus 로고
    • Degradation of azo dyes by environmental microorganisms and helminths
    • Chung K.T., and Stevens Jr. S.E. Degradation of azo dyes by environmental microorganisms and helminths. Environ. Toxicol. Chem. 12 (1993) 2121
    • (1993) Environ. Toxicol. Chem. , vol.12 , pp. 2121
    • Chung, K.T.1    Stevens Jr., S.E.2
  • 7
    • 0026457805 scopus 로고
    • Purification and partial characterization of two azoreductases from Shigella dysenteriae Type 1
    • Ghosh D.K., Mandal A., and Chaudhuri J. Purification and partial characterization of two azoreductases from Shigella dysenteriae Type 1. FEMS Microbiol. Lett. 98 (1992) 229-234
    • (1992) FEMS Microbiol. Lett. , vol.98 , pp. 229-234
    • Ghosh, D.K.1    Mandal, A.2    Chaudhuri, J.3
  • 8
    • 0026040779 scopus 로고
    • Mineralization of the sulfonated azo dye mordant yellow 3 by 6-aminonaphthalene-2-sulfonate-degrading bacterial consortium
    • Haug W., Schmidt A., Nortemann B., Hempel D.C., Stolz A., and Knackmuss H.J. Mineralization of the sulfonated azo dye mordant yellow 3 by 6-aminonaphthalene-2-sulfonate-degrading bacterial consortium. Appl. Environ. Microbiol. 57 (1991) 3144-3149
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3144-3149
    • Haug, W.1    Schmidt, A.2    Nortemann, B.3    Hempel, D.C.4    Stolz, A.5    Knackmuss, H.J.6
  • 9
    • 0035106475 scopus 로고    scopus 로고
    • Kinetics of azo reductase and assessment of toxicity of metabolic products from azo dyes by Pseudomonas luteola
    • Hu T.L. Kinetics of azo reductase and assessment of toxicity of metabolic products from azo dyes by Pseudomonas luteola. Water Sci. Technole Technol. 43 (2001) 261-269
    • (2001) Water Sci. Technole Technol. , vol.43 , pp. 261-269
    • Hu, T.L.1
  • 10
    • 0030822677 scopus 로고    scopus 로고
    • Localization of the enzyme system involved in anerobic reduction of azo dyes by Sphingomonas sp. Strain BN6 and effect of artificial redox mediators on the rate of dye reduction
    • Kuldlich M., Keck A., Klein J., and Stolz A. Localization of the enzyme system involved in anerobic reduction of azo dyes by Sphingomonas sp. Strain BN6 and effect of artificial redox mediators on the rate of dye reduction. Appl. Environ. Microbiol. 63 (1997) 3691-3694
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3691-3694
    • Kuldlich, M.1    Keck, A.2    Klein, J.3    Stolz, A.4
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemnli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemnli, U.K.1
  • 13
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acp D) encodes an azoreductase
    • Nakanishi M., Yatome C., Ishida N., and Kitade Y. Putative ACP phosphodiesterase gene (acp D) encodes an azoreductase. J. Biol. Chem. 276 (2001) 46394-46399
    • (2001) J. Biol. Chem. , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 14
    • 0030687913 scopus 로고    scopus 로고
    • Mutagenicity of azo dyes used in foods, drugs and cosmetics before and after reduction by Clostridium species from the human intestinal tract
    • Rafii F., Hall J.D., and Cerniglia C.E. Mutagenicity of azo dyes used in foods, drugs and cosmetics before and after reduction by Clostridium species from the human intestinal tract. Food Chem. Toxicol. 35 (1997) 897-901
    • (1997) Food Chem. Toxicol. , vol.35 , pp. 897-901
    • Rafii, F.1    Hall, J.D.2    Cerniglia, C.E.3
  • 15
    • 0033066384 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of an azoreductase gene from Clostridium perfringens and comparison with azoreductase genes from other bacteria
    • Rafii F., and Coleman T. Cloning and expression in Escherichia coli of an azoreductase gene from Clostridium perfringens and comparison with azoreductase genes from other bacteria. J. Basic Microbiol. 39 (1999) 29-35
    • (1999) J. Basic Microbiol. , vol.39 , pp. 29-35
    • Rafii, F.1    Coleman, T.2
  • 16
    • 0036533848 scopus 로고    scopus 로고
    • Effects of different quinoid redox mediators on the anaerobic reduction of azo dyes by bacteria
    • Rau J., Knackmuss H.J., and Stolz A. Effects of different quinoid redox mediators on the anaerobic reduction of azo dyes by bacteria. Environ. Sci. Technol. 36 (2002) 1497-1504
    • (2002) Environ. Sci. Technol. , vol.36 , pp. 1497-1504
    • Rau, J.1    Knackmuss, H.J.2    Stolz, A.3
  • 17
    • 7444237119 scopus 로고    scopus 로고
    • Microaerophilic-aerobic sequential batch reactor for treatment of azo dyes containing simulated wastewater
    • Sandhya S., Padmavathy S., Swaminathan K., Subrahmanyam Y.V., and Kaul S.N. Microaerophilic-aerobic sequential batch reactor for treatment of azo dyes containing simulated wastewater. Process Biochem. 40 (2005) 885-890
    • (2005) Process Biochem. , vol.40 , pp. 885-890
    • Sandhya, S.1    Padmavathy, S.2    Swaminathan, K.3    Subrahmanyam, Y.V.4    Kaul, S.N.5
  • 18
    • 0035937804 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for azo reduction for Bacillus sp. OY1-22 isolated for soil
    • Suzuki Y., Yodu T., Ruhul A., and Suigiura W. Molecular cloning and characterization of the gene coding for azo reduction for Bacillus sp. OY1-22 isolated for soil. J. Biol. Chem. 276 12 (2001) 9059-9069
    • (2001) J. Biol. Chem. , vol.276 , Issue.12 , pp. 9059-9069
    • Suzuki, Y.1    Yodu, T.2    Ruhul, A.3    Suigiura, W.4
  • 19
    • 0041912374 scopus 로고    scopus 로고
    • Degradation of a tannery and textile dye, Navitan Fast Blue S5R by Pseudomonas aeruginosa
    • Valli N.C., and Rajkumar G.S. Degradation of a tannery and textile dye, Navitan Fast Blue S5R by Pseudomonas aeruginosa. World J. Microbiol. Biotechnol. 19 (2003) 609-614
    • (2003) World J. Microbiol. Biotechnol. , vol.19 , pp. 609-614
    • Valli, N.C.1    Rajkumar, G.S.2
  • 20
    • 0030199687 scopus 로고    scopus 로고
    • Decolorization and biodegradation of methyl red by Klebsiella pneumoniae RS13
    • Wong P.K., and Yuen P.Y. Decolorization and biodegradation of methyl red by Klebsiella pneumoniae RS13. Wat. Res. 30 (1996) 1736-1744
    • (1996) Wat. Res. , vol.30 , pp. 1736-1744
    • Wong, P.K.1    Yuen, P.Y.2
  • 21
    • 9444285518 scopus 로고    scopus 로고
    • Bacterial decolorization of an azo dye with a natural isolate of Pseudomonas luteola and genetically modified Escherichia coli
    • Yeh M.S., and Chang J.S. Bacterial decolorization of an azo dye with a natural isolate of Pseudomonas luteola and genetically modified Escherichia coli. J. Chem. Technol. Biotechnol. 79 (2004) 1354-1360
    • (2004) J. Chem. Technol. Biotechnol. , vol.79 , pp. 1354-1360
    • Yeh, M.S.1    Chang, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.