메뉴 건너뛰기




Volumn 12, Issue 1, 2009, Pages 13-21

Detoxification of azo dyes by a novel pH-versatile, salt-resistant laccase from Streptomyces ipomoea

Author keywords

Azo dye detoxification; Laccases; Streptomyces ipomoea

Indexed keywords

IPOMOEA; STREPTOMYCES; STREPTOMYCES IPOMOEAE;

EID: 66349111649     PISSN: 11396709     EISSN: 16181905     Source Type: Journal    
DOI: 10.2436/20.1501.01.77     Document Type: Article
Times cited : (140)

References (50)
  • 2
    • 0037391271 scopus 로고    scopus 로고
    • Kraft pulp biobleaching and mediated oxidation of a nonphenolic substrate by laccase from Streptomyces cyaneus CECT 3335
    • Arias ME, Arenas M, Rodríguez J, Soliveri J, Ball AS, Hernández M (2003) Kraft pulp biobleaching and mediated oxidation of a nonphenolic substrate by laccase from Streptomyces cyaneus CECT 3335. Appl Environ Microbiol 69:1953-1958
    • (2003) Appl Environ Microbiol , vol.69 , pp. 1953-1958
    • Arias, M.E.1    Arenas, M.2    Rodríguez, J.3    Soliveri, J.4    Ball, A.S.5    Hernández, M.6
  • 3
    • 33645027271 scopus 로고    scopus 로고
    • Fungal laccases-Occurrence and properties
    • Baldrian P (2006) Fungal laccases-Occurrence and properties. FEMS Microbiol Rev 30:215-242
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 215-242
    • Baldrian, P.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 17444419429 scopus 로고    scopus 로고
    • Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes
    • Camarero S, Ibarra D, Martínez MJ, Martínez AT (2005) Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes. Appl Environ Microbiol 71:1775-1784
    • (2005) Appl Environ Microbiol , vol.71 , pp. 1775-1784
    • Camarero, S.1    Ibarra, D.2    Martínez, M.J.3    Martínez, A.T.4
  • 7
    • 0037333713 scopus 로고    scopus 로고
    • Laccases and their occurrence in prokaryotes
    • Claus H (2003) Laccases and their occurrence in prokaryotes. Arch Microbiol 179:145-150
    • (2003) Arch Microbiol , vol.179 , pp. 145-150
    • Claus, H.1
  • 8
    • 54349126619 scopus 로고    scopus 로고
    • Production of two novel laccase isoforms by a thermotolerant strain of Pycnoporus sanguineus isolated from an oil-polluted tropical habitat
    • Dantán-González E, Vite-Vallejo O, Martínez-Anaya C, et al. (2008) Production of two novel laccase isoforms by a thermotolerant strain of Pycnoporus sanguineus isolated from an oil-polluted tropical habitat. Int Microbiol 11:163-169
    • (2008) Int Microbiol , vol.11 , pp. 163-169
    • Dantán-González, E.1    Vite-Vallejo, O.2    Martínez-Anaya, C.3
  • 9
    • 0037317124 scopus 로고    scopus 로고
    • Prokaryotic utilization of the twin-arginine translocation pathway: A genomic survey
    • Dilks K, Rose RW, Hartmann E, Pohlschroder M (2003) Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey. J Bacteriol 185:1478-1483
    • (2003) J Bacteriol , vol.185 , pp. 1478-1483
    • Dilks, K.1    Rose, R.W.2    Hartmann, E.3    Pohlschroder, M.4
  • 10
    • 0742305629 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae
    • Dittmer NT, Suderman RJ, Jiang H, Zhu YC, Gorman MJ, Kramer KJ, Kanost MR (2004) Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae. Insect Biochem Mol Biol 34:29-41
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 29-41
    • Dittmer, N.T.1    Suderman, R.J.2    Jiang, H.3    Zhu, Y.C.4    Gorman, M.J.5    Kramer, K.J.6    Kanost, M.R.7
  • 11
    • 44649140429 scopus 로고    scopus 로고
    • Homologous cloning, expression, and characterisation of a laccase from Streptomyces coelicolor and enzymatic decolourisation of an indigo dye
    • Dubé E, Shareck F, Hurtubise Y, Daneault C, Beauregard M (2008) Homologous cloning, expression, and characterisation of a laccase from Streptomyces coelicolor and enzymatic decolourisation of an indigo dye. Appl Microbiol Biotechnol 79:597-603
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 597-603
    • Dubé, E.1    Shareck, F.2    Hurtubise, Y.3    Daneault, C.4    Beauregard, M.5
  • 12
    • 0000369624 scopus 로고
    • A method for the determination of amino acid sequence in peptides
    • Edman P (1949) A method for the determination of amino acid sequence in peptides. Arch Biochem 22:475
    • (1949) Arch Biochem , vol.22 , pp. 475
    • Edman, P.1
  • 13
    • 0037632906 scopus 로고    scopus 로고
    • Enzymological characterization of EpoA, a laccase-like phenol oxidase produced by Streptomyces griseus
    • Endo K, Hayashi Y, Hibi T, Hosono K, Beppu T, Ueda K (2003) Enzymological characterization of EpoA, a laccase-like phenol oxidase produced by Streptomyces griseus. J Biochem (Tokyo) 133:671-677
    • (2003) J Biochem (Tokyo) , vol.133 , pp. 671-677
    • Endo, K.1    Hayashi, Y.2    Hibi, T.3    Hosono, K.4    Beppu, T.5    Ueda, K.6
  • 14
    • 0035987267 scopus 로고    scopus 로고
    • A novel extracytoplasmic phenol oxidase of Streptomyces: Its possible involvement in the onset of morphogenesis
    • Endo K, Hosono K, Beppu T, Ueda K (2002) A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis. Microbiology 148:1767-1776
    • (2002) Microbiology , vol.148 , pp. 1767-1776
    • Endo, K.1    Hosono, K.2    Beppu, T.3    Ueda, K.4
  • 15
    • 0037468239 scopus 로고    scopus 로고
    • The toxicity of textile reactive azo dyes after hydrolysis and decolourisation
    • Gottlieb A, Shaw C, Smith A, Wheatley A, Forsythe S (2003) The toxicity of textile reactive azo dyes after hydrolysis and decolourisation. J Biotechnol 101:49-56
    • (2003) J Biotechnol , vol.101 , pp. 49-56
    • Gottlieb, A.1    Shaw, C.2    Smith, A.3    Wheatley, A.4    Forsythe, S.5
  • 16
  • 18
    • 0034629250 scopus 로고    scopus 로고
    • Laccase activity tests and laccase inhibitors
    • Johannes C, Majcherczyk A (2000) Laccase activity tests and laccase inhibitors. J Biotechnol 78:193-199
    • (2000) J Biotechnol , vol.78 , pp. 193-199
    • Johannes, C.1    Majcherczyk, A.2
  • 19
    • 0041322840 scopus 로고    scopus 로고
    • Electrochemical characterization of purified Rhus vernicifera laccase: Voltammetric evidence for a sequential four-electron transfer
    • Johnson DL, Thompson JL Brinkmann SM, Schuller KA, Martin LL (2003) Electrochemical characterization of purified Rhus vernicifera laccase: voltammetric evidence for a sequential four-electron transfer. Biochemistry 42:10229-10237
    • (2003) Biochemistry , vol.42 , pp. 10229-10237
    • Johnson, D.L.1    Thompson, J.L.2    Brinkmann, S.M.3    Schuller, K.A.4    Martin, L.L.5
  • 20
    • 84892083722 scopus 로고    scopus 로고
    • Bioremediation for the decolorization of textile dyes-A review
    • In: Lichtfouse E, Schwarzbauer J, Robert D (eds), Springer, Berlin
    • Kandelbauer A, Gübitz GM (2005) Bioremediation for the decolorization of textile dyes-A review. In: Lichtfouse E, Schwarzbauer J, Robert D (eds) Environmental chemistry: Green chemistry and pollutants in ecosystems. Springer, Berlin, pp 269-288
    • (2005) Environmental Chemistry: Green Chemistry and Pollutants in Ecosystems , pp. 269-288
    • Kandelbauer, A.1    Gübitz, G.M.2
  • 22
    • 0142040829 scopus 로고    scopus 로고
    • Anovel extracellular multicopper oxidase from Phanerochaete chrysosporium with ferroxidase activity
    • Larrondo LF, Salas L, Melo F, Vicuña R, Cullen D (2003) Anovel extracellular multicopper oxidase from Phanerochaete chrysosporium with ferroxidase activity. Appl Environ Microbiol 69:6257-6263
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6257-6263
    • Larrondo, L.F.1    Salas, L.2    Melo, F.3    Vicuña, R.4    Cullen, D.5
  • 23
    • 0034788827 scopus 로고    scopus 로고
    • Fungal laccase: Properties and activity on lignin
    • Leonowicz A, Cho NS, Luterek J, et al. (2001) Fungal laccase: properties and activity on lignin. J Basic Microbiol 41:185-227
    • J Basic Microbiol , vol.41 , pp. 185-227
    • Leonowicz, A.1    Cho, N.S.2    Luterek, J.3
  • 24
    • 21344447936 scopus 로고    scopus 로고
    • Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds
    • Lorenzo M, Moldes D, Couto SR, Sanroman MA (2005) Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds. Chemosphere 60:1124-1128
    • (2005) Chemosphere , vol.60 , pp. 1124-1128
    • Lorenzo, M.1    Moldes, D.2    Couto, S.R.3    Sanroman, M.A.4
  • 25
    • 0344996573 scopus 로고
    • Active-siteelectronic structure contributions to electron-transfer pathways in rubredoxin and plastocyanin: Direct versus superexchange
    • Lowery MD, Guckert JA, Gebhard MS, Solomon EI (1993) Active-site electronic structure contributions to electron-transfer pathways in rubredoxin and plastocyanin: direct versus superexchange. J Am Chem Soc 115:3012-3013
    • (1993) J Am Chem Soc , vol.115 , pp. 3012-3013
    • Lowery, M.D.1    Guckert, J.A.2    Gebhard, M.S.3    Solomon, E.I.4
  • 26
    • 4344699077 scopus 로고    scopus 로고
    • Characterization of SLAC: A small laccase from streptomyces coelicolor with unprecedented activity
    • Machczynski MC, Vijgenboom E, Samyn B, Canters GW (2004) Characterization of SLAC: A small laccase from Streptomyces coelicolor with unprecedented activity. Protein Sci 13:2388-2397
    • (2004) Protein Sci , vol.13 , pp. 2388-2397
    • Machczynski, M.C.1    Vijgenboom, E.2    Samyn, B.3    Canters, G.W.4
  • 27
    • 0042825653 scopus 로고    scopus 로고
    • Purification and characterization of the main laccase produced by the white-rot fungus Pleurotus pulmonarius on wheat bran solid state medium
    • Marques De Souza CG, Peralta RM (2003) Purification and characterization of the main laccase produced by the white-rot fungus Pleurotus pulmonarius on wheat bran solid state medium. J Basic Microbiol 43:278-286
    • (2003) J Basic Microbiol , vol.43 , pp. 278-286
    • Marques de Souza, C.G.1    Peralta, R.M.2
  • 28
    • 0029926079 scopus 로고    scopus 로고
    • Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii
    • Martínez MJ, Ruiz-Dueñas FJ, Guillén F, Martínez AT (1996) Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii. Eur J Biochem 237:424-432
    • (1996) Eur J Biochem , vol.237 , pp. 424-432
    • Martínez, M.J.1    Ruiz-Dueñas, F.J.2    Guillén, F.3    Martínez, A.T.4
  • 29
    • 0037166265 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat
    • Martins LO, Soares CM, Pereira MM, Teixeira M, Costa T, Jones GH, Henriques AO (2002) Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J Biol Chem 277:18849-18859
    • (2002) J Biol Chem , vol.277 , pp. 18849-18859
    • Martins, L.O.1    Soares, C.M.2    Pereira, M.M.3    Teixeira, M.4    Costa, T.5    Jones, G.H.6    Henriques, A.O.7
  • 30
    • 46149132278 scopus 로고
    • Polyphenol oxidases in plants-Recent progress
    • Mayer AM (1987) Polyphenol oxidases in plants-Recent progress. Phytochemistry 26:11-20
    • (1987) Phytochemistry , vol.26 , pp. 11-20
    • Mayer, A.M.1
  • 31
    • 0036166772 scopus 로고    scopus 로고
    • Evaluation of an endo-β-mannanase produced by Streptomyces ipomoea CECT 3341 for the biobleaching of pine kraft pulps
    • Montiel MD, Hernández M, Rodríguez J, Arias ME (2002) Evaluation of an endo-β-mannanase produced by Streptomyces ipomoea CECT 3341 for the biobleaching of pine kraft pulps. Appl Microbiol Biotechnol 58:67-72
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 67-72
    • Montiel, M.D.1    Hernández, M.2    Rodríguez, J.3    Arias, M.E.4
  • 32
    • 0030975668 scopus 로고    scopus 로고
    • Structural comparison of cupredoxin domains: Domain recycling to construct proteins with novel functions
    • Murphy ME, Lindley PF, Adman ET (1997) Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions. Protein Sci 6:761-770
    • (1997) Protein Sci , vol.6 , pp. 761-770
    • Murphy, M.E.1    Lindley, P.F.2    Adman, E.T.3
  • 33
    • 0021266784 scopus 로고
    • Ion gene-product of Escherichia coli is a heat-shock protein
    • Phillips TA, Vanbogelen RA, Neidhardt FC (1984) Ion gene-product of Escherichia coli is a heat-shock protein. J Bacteriol 159:283-287
    • (1984) J Bacteriol , vol.159 , pp. 283-287
    • Phillips, T.A.1    Vanbogelen, R.A.2    Neidhardt, F.C.3
  • 34
    • 17644363018 scopus 로고    scopus 로고
    • Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p
    • Quintanar L, Stoj C, Wang TP, Kosman DJ, Solomon EI (2005) Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p. Biochemistry 44:6081-6091
    • (2005) Biochemistry , vol.44 , pp. 6081-6091
    • Quintanar, L.1    Stoj, C.2    Wang, T.P.3    Kosman, D.J.4    Solomon, E.I.5
  • 35
    • 0037565099 scopus 로고    scopus 로고
    • Escherichia coli mechanisms of copper homeostasis in a changing environment
    • Rensing C, Grass G (2003) Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol Rev 27: 197-213
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 197-213
    • Rensing, C.1    Grass, G.2
  • 36
    • 11144268969 scopus 로고    scopus 로고
    • Influence of redox mediators and metal ions on synthetic acid dye decolourization by crude laccase from Trametes hirsuta
    • Rodríguez Couto S, Sanromán MA, Gübitz GM (2005) Influence of redox mediators and metal ions on synthetic acid dye decolourization by crude laccase from Trametes hirsuta. Chemosphere 58:417-422
    • (2005) Chemosphere , vol.58 , pp. 417-422
    • Rodríguez Couto, S.1    Sanromán, M.A.2    Gübitz, G.M.3
  • 37
    • 14544299249 scopus 로고    scopus 로고
    • Purification and characterization of a periplasmic laccase produced by Sinorhizobium meliloti
    • Rosconi F, Fraguas LF, Martínez-Drets G, Castro-Sowinski S (2005) Purification and characterization of a periplasmic laccase produced by Sinorhizobium meliloti. Enzyme Microb Technol 36:800-807
    • (2005) Enzyme Microb Technol , vol.36 , pp. 800-807
    • Rosconi, F.1    Fraguas, L.F.2    Martínez-Drets, G.3    Castro-Sowinski, S.4
  • 38
    • 4043056735 scopus 로고    scopus 로고
    • A cloned Bacillus halodurans multicopper oxidase exhibiting alkaline laccase activity
    • Ruijssenaars HJ, Hartmans S (2004) A cloned Bacillus halodurans multicopper oxidase exhibiting alkaline laccase activity. Appl Microbiol Biotechnol 65:177-182
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 177-182
    • Ruijssenaars, H.J.1    Hartmans, S.2
  • 39
    • 0004136246 scopus 로고    scopus 로고
    • 3rd ed, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Russell DW (2001) Molecular cloning, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2001) Molecular Cloning
    • Sambrook, J.1    Russell, D.W.2
  • 40
    • 0035810685 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a unique multipotent polyphenol oxidase from Marinomonas mediterranea
    • Sánchez-Amat A, Lucas-Elio P, Fernández E, García-Borrón JC, Solano F (2001) Molecular cloning and functional characterization of a unique multipotent polyphenol oxidase from Marinomonas mediterranea. BBA Protein Struct Mol Enzym 1547:104-116
    • (2001) BBA Protein Struct Mol Enzym , vol.1547 , pp. 104-116
    • Sánchez-Amat, A.1    Lucas-Elio, P.2    Fernández, E.3    García-Borrón, J.C.4    Solano, F.5
  • 41
    • 0031587399 scopus 로고    scopus 로고
    • A pluripotent polyphenol oxidase from the melanogenic marine Alteromonas sp. shares catalytic capabilities of tyrosinases and laccases
    • Sánchez-Amat A, Solano F (1997) A pluripotent polyphenol oxidase from the melanogenic marine Alteromonas sp. shares catalytic capabilities of tyrosinases and laccases. Biochem Biophys Res Commun 240:787-792
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 787-792
    • Sánchez-Amat, A.1    Solano, F.2
  • 43
    • 0035940069 scopus 로고    scopus 로고
    • Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R
    • Soares GMB, de Amorim MTP, Costa-Ferreira M (2001) Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R. J Biotechnol 89:123-129
    • (2001) J Biotechnol , vol.89 , pp. 123-129
    • Soares, G.M.B.1    de Amorim, M.T.P.2    Costa-Ferreira, M.3
  • 45
    • 1242343386 scopus 로고    scopus 로고
    • A thermostable laccase from Streptomyces lavendulae REN-7: Purification, characterization, nucleotide sequence, and expression
    • Suzuki T, Endo K, Ito M, Tsujibo H, Miyamoto K, Inamori Y (2003) A thermostable laccase from Streptomyces lavendulae REN-7: Purification, characterization, nucleotide sequence, and expression. Biosci Biotechnol Biochem 67:2167-2175
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 2167-2175
    • Suzuki, T.1    Endo, K.2    Ito, M.3    Tsujibo, H.4    Miyamoto, K.5    Inamori, Y.6
  • 46
    • 0037106449 scopus 로고    scopus 로고
    • Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments
    • Takami H, Takaki Y, Uchiyama I (2002) Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments. Nucleic Acids Res 30:3927-3935
    • (2002) Nucleic Acids Res , vol.30 , pp. 3927-3935
    • Takami, H.1    Takaki, Y.2    Uchiyama, I.3
  • 47
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston CF (1994) The structure and function of fungal laccases. Microbiology 140:19-26
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 48
    • 33645066356 scopus 로고    scopus 로고
    • The multicopper oxidase CutO confers copper tolerance to Rhodobacter capsulatus
    • Wiethaus J, Wildner GF, Masepohl B (2006) The multicopper oxidase CutO confers copper tolerance to Rhodobacter capsulatus. FEMS Microbiol Lett 256:67-74
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 67-74
    • Wiethaus, J.1    Wildner, G.F.2    Masepohl, B.3
  • 49
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu F (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J Biol Chem 272:924-928
    • (1997) J Biol Chem , vol.272 , pp. 924-928
    • Xu, F.1
  • 50
    • 0029937108 scopus 로고    scopus 로고
    • Oxidation of phenols, anilines, and benzenethiols by fungal laccases: Correlation between activity and redox potentials as well as halide inhibition
    • Xu F (1996) Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35:7608-7614
    • (1996) Biochemistry , vol.35 , pp. 7608-7614
    • Xu, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.