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Volumn 19, Issue 4, 2003, Pages 1292-1299

Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus

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EID: 0042009610     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp034040t     Document Type: Article
Times cited : (36)

References (41)
  • 1
    • 0347938866 scopus 로고    scopus 로고
    • Catalase: An enzyme with growing industrial potential
    • Dhaese, P. Catalase: An enzyme with growing industrial potential. Chim. Oggi 1996, 14 (1-2), 19-21.
    • (1996) Chim. Oggi , vol.14 , Issue.1-2 , pp. 19-21
    • Dhaese, P.1
  • 2
    • 0025961559 scopus 로고
    • Hydrogen peroxide - An environmentally acceptable textile bleaching agent
    • Weck, M. Hydrogen peroxide - an environmentally acceptable textile bleaching agent. Text. Prax. Int. 1991, 2, 144-147.
    • (1991) Text. Prax. Int. , vol.2 , pp. 144-147
    • Weck, M.1
  • 3
    • 0035940062 scopus 로고    scopus 로고
    • Thermo-alkali-stable catalases from newly isolated Bacillus sp. for the treatment and recycling of textile bleaching effluents
    • Paar, A.; Costa, S.; Tzanov, T.; Gudelj, M.; Robra, K-H.; Cavaco-Paulo, A.; Gubitz, G. M. Thermo-alkali-stable catalases from newly isolated Bacillus sp. for the treatment and recycling of textile bleaching effluents. J. Biotechnol. 2001, 89, 147-153.
    • (2001) J. Biotechnol. , vol.89 , pp. 147-153
    • Paar, A.1    Costa, S.2    Tzanov, T.3    Gudelj, M.4    Robra, K.-H.5    Cavaco-Paulo, A.6    Gubitz, G.M.7
  • 4
    • 0032765978 scopus 로고    scopus 로고
    • Die abwasser situation in der deutschen papier-, textil-, und lederindustrie
    • Hillenbrand, T. Die abwasser situation in der deutschen papier-, textil-, und lederindustrie. GWF, Wasser/Abwasser 1999, 140 (4), 267-273.
    • (1999) GWF, Wasser/Abwasser , vol.140 , Issue.4 , pp. 267-273
    • Hillenbrand, T.1
  • 5
    • 0037210586 scopus 로고    scopus 로고
    • An immobilized catalase peroxidase from the alkalothermophilic Bacillus SF for the treatment of textile-bleaching effluents
    • Fruhwirth, G. O.; Paar, A.; Gudelj, M.; Cavaco-Paulo, A.; Robra, K.-H.; Gubitz, G. M. An immobilized catalase peroxidase from the alkalothermophilic Bacillus SF for the treatment of textile-bleaching effluents. Appl. Microbiol. Biotechnol. 2002, 60, 313-319.
    • (2002) Appl. Microbiol. Biotechnol. , vol.60 , pp. 313-319
    • Fruhwirth, G.O.1    Paar, A.2    Gudelj, M.3    Cavaco-Paulo, A.4    Robra, K.-H.5    Gubitz, G.M.6
  • 7
    • 12444268088 scopus 로고    scopus 로고
    • The mechanism of hydrogen peroxide bleaching
    • Spiro, M. C.; Criffith, P. W. The mechanism of hydrogen peroxide bleaching. Text. Chem. Color 1997, 11, 29.
    • (1997) Text. Chem. Color , vol.11 , pp. 29
    • Spiro, M.C.1    Criffith, P.W.2
  • 8
    • 0024407187 scopus 로고
    • Biochemistry of oxygen toxicity
    • Cadenas, E. Biochemistry of oxygen toxicity. Annu. Rev. Biochem. 1989, 58, 79-110.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 79-110
    • Cadenas, E.1
  • 9
    • 0025069762 scopus 로고
    • How to characterize a biological antioxidant
    • Halliwell, B. How to characterize a biological antioxidant, Free Radical Res. Commun. 1990, 9, 1-32.
    • (1990) Free Radical Res. Commun. , vol.9 , pp. 1-32
    • Halliwell, B.1
  • 10
    • 0006198640 scopus 로고
    • Hydrogen peroxide-inducible proteins in Samonella typhimurium overlap with heat shock and other stress proteins
    • Morgan, R. W.; Christman, M. F.; Jacobson, F. S.; Storz, G.; Ames, B. N. Hydrogen peroxide-inducible proteins in Samonella typhimurium overlap with heat shock and other stress proteins. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 8059-8063.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8059-8063
    • Morgan, R.W.1    Christman, M.F.2    Jacobson, F.S.3    Storz, G.4    Ames, B.N.5
  • 11
    • 12444288289 scopus 로고
    • Catalase 1.11.1.6
    • Springer-Verlag: Berlin, Heidelberg
    • Catalase 1.11.1.6. In Enzyme Handbook; Schomburg, D., Salzmann, M., Stephan, D., Eds.; Springer-Verlag: Berlin, Heidelberg; 1994, Vol. 7.
    • (1994) Enzyme Handbook , vol.7
    • Schomburg, D.1    Salzmann, M.2    Stephan, D.3
  • 12
    • 0023007996 scopus 로고
    • Characterization of a manganese-containing catalase from the obligate thermophile Thermoleophilum album
    • Allgood, G. S.; Perry, J. J. Characterization of a manganese-containing catalase from the obligate thermophile Thermoleophilum album. J. Bacteriol. 1986, 168 (2), 563-567.
    • (1986) J. Bacteriol. , vol.168 , Issue.2 , pp. 563-567
    • Allgood, G.S.1    Perry, J.J.2
  • 14
    • 1542270004 scopus 로고
    • Isolation and characterization of the cyanide-resistant and azide-resistant catalase of Lactobacillus plantarum
    • Kono, Y.; I. Fridovich, Isolation and characterization of the cyanide-resistant and azide-resistant catalase of Lactobacillus plantarum. J. Bacteriol. 1965, 90, 352-356.
    • (1965) J. Bacteriol. , vol.90 , pp. 352-356
    • Kono, Y.1    Fridovich, I.2
  • 15
    • 0028588511 scopus 로고
    • Characterization of the major catalase from Streptomyces coelicolor ATCC 10147
    • Kim, H.; Lee, J. S.; Hah, Y. C.; Roe, J. H. Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. Microbiology 1994, 140, 3391-3397.
    • (1994) Microbiology , vol.140 , pp. 3391-3397
    • Kim, H.1    Lee, J.S.2    Hah, Y.C.3    Roe, J.H.4
  • 17
    • 0018367454 scopus 로고
    • Purification of the o-dianisidine peroxidase from Escherichia coli B
    • Claiborne, A.; Fridovich, I. Purification of the o-dianisidine peroxidase from Escherichia coli B. J. Biol. Chem. 1979, 254 (10), 4245-4252.
    • (1979) J. Biol. Chem. , vol.254 , Issue.10 , pp. 4245-4252
    • Claiborne, A.1    Fridovich, I.2
  • 18
    • 0035490144 scopus 로고    scopus 로고
    • Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • Kengen, S. W. M.; Bikker, F. J.; Hagen, W. R.; de Vos, W. M.; van der Oost, J. Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus. Extremophiles 2001, 5, 323-332.
    • (2001) Extremophiles , vol.5 , pp. 323-332
    • Kengen, S.W.M.1    Bikker, F.J.2    Hagen, W.R.3    De Vos, W.M.4    Van Der Oost, J.5
  • 19
    • 0034938922 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable intracellular enzyme with peroxidase activity from Bacillus sphaericus
    • Apitz, A.; van Pee, K. H. Isolation and characterization of a thermostable intracellular enzyme with peroxidase activity from Bacillus sphaericus. Arch. Microbiol. 2001, 175, 405-412.
    • (2001) Arch. Microbiol. , vol.175 , pp. 405-412
    • Apitz, A.1    Van Pee, K.H.2
  • 20
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder, K. G, Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 1992, 2, 388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 21
    • 0031969230 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable catalase from culture broth of Thermoascus aurantiacus
    • Wang, H.; Tokusige, Y.; Shinoyama, H.; Fujii, T.; Urakami, T. Purification and characterization of a thermostable catalase from culture broth of Thermoascus aurantiacus. J. Ferment. Bioeng. 1998, 85 (2), 169-173.
    • (1998) J. Ferment. Bioeng. , vol.85 , Issue.2 , pp. 169-173
    • Wang, H.1    Tokusige, Y.2    Shinoyama, H.3    Fujii, T.4    Urakami, T.5
  • 22
    • 0035751685 scopus 로고    scopus 로고
    • A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents
    • Gudelj, M.; Fruhwirth, G. O.; Paar, A.; Lottspeich, F.; Robra, K. H.; Cavaco-Paulo, A.; Gubitz, G. M. A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents. Extremophiles 2001, 5, 423-429.
    • (2001) Extremophiles , vol.5 , pp. 423-429
    • Gudelj, M.1    Fruhwirth, G.O.2    Paar, A.3    Lottspeich, F.4    Robra, K.H.5    Cavaco-Paulo, A.6    Gubitz, G.M.7
  • 23
    • 0023758686 scopus 로고
    • Thermostable peroxidase from Bacillus stearothermophilus
    • Loprasert, S.; Negoro, S.; Okada, H. Thermostable peroxidase from Bacillus stearothermophilus. J. Gen. Microbiol. 1988, 134, 1971-1976.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1971-1976
    • Loprasert, S.1    Negoro, S.2    Okada, H.3
  • 25
    • 0000612080 scopus 로고
    • Phenotypic characterization
    • Gerhardt, P., Murray, R. G. E., Wood, W. A., Krieg, N. R., Eds.; American Society for Microbiology: Washington, DC
    • Smibert, R. M. and Krieg, N. R. Phenotypic characterization. In Methods for General and Molecular Bacteriology; Gerhardt, P., Murray, R. G. E., Wood, W. A., Krieg, N. R., Eds.; American Society for Microbiology: Washington, DC, 1994; p 614.
    • (1994) Methods for General and Molecular Bacteriology , pp. 614
    • Smibert, R.M.1    Krieg, N.R.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R. F., Jr.; Sizer, I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 1952, 195, 276-287.
    • (1952) J. Biol. Chem. , vol.195 , pp. 276-287
    • Beers R.F., Jr.1    Sizer, I.W.2
  • 28
    • 0016701378 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate (NADP)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes
    • Hildebrandt, A. G.; Roots, I. Reduced nicotinamide adenine dinucleotide phosphate (NADP)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Arch. Biochem. Biophys. 1975, 171, 385-397.
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 385-397
    • Hildebrandt, A.G.1    Roots, I.2
  • 30
    • 0025049510 scopus 로고
    • Purification and characterization of catalase from a facultative alkalophilic Bacillus
    • Yumoto, L; Fukumori, Y.; Yamanaka, T. Purification and characterization of catalase from a facultative alkalophilic Bacillus. J. Biochem. 1990, 108, 583-587.
    • (1990) J. Biochem. , vol.108 , pp. 583-587
    • Yumoto, L.1    Fukumori, Y.2    Yamanaka, T.3
  • 31
    • 0028814066 scopus 로고
    • Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium
    • Brown-Peterson, N. J.; Salin, M. L. Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium. J. Bacteriol. 1995, 177 (2), 378-384.
    • (1995) J. Bacteriol. , vol.177 , Issue.2 , pp. 378-384
    • Brown-Peterson, N.J.1    Salin, M.L.2
  • 32
    • 0025274717 scopus 로고
    • Purification, partial characterization and possible role of catalase in the bacterium Vitreoscilla
    • Abrams, J. J.; Webster, D. A. Purification, partial characterization and possible role of catalase in the bacterium Vitreoscilla. Arch. Biochem. Biophys. 1990, 279 (1), 54-59.
    • (1990) Arch. Biochem. Biophys. , vol.279 , Issue.1 , pp. 54-59
    • Abrams, J.J.1    Webster, D.A.2
  • 33
    • 0031587989 scopus 로고    scopus 로고
    • Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans
    • Obinger, C.; Regelsberger, G.; Strasser, G.; Burner, U.; Peschek, G. A. Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans. Biochem. Biophys. Res. Commun. 1997, 235, 545-552.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 545-552
    • Obinger, C.1    Regelsberger, G.2    Strasser, G.3    Burner, U.4    Peschek, G.A.5
  • 36
    • 0031029149 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis
    • Johnsson, K.; Froland, W. A.; Schultz, P. G. Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis. J. Biol. Chem. 1997, 272 (5), 2834-2840.
    • (1997) J. Biol. Chem. , vol.272 , Issue.5 , pp. 2834-2840
    • Johnsson, K.1    Froland, W.A.2    Schultz, P.G.3
  • 38
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam, C. D.; Arvai, A. S.; Bourne, Y.; Tainer, J. A. Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 2000, 296, 295-309.
    • (2000) J. Mol. Biol. , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 41
    • 0030571599 scopus 로고    scopus 로고
    • Reaction of E. coli catalase HPII with cyanide as ligand and as inhibitor
    • Maj, M.; Nicholls, P.; Obinger, C.; Hillar, A.; Loewen, P. C. Reaction of E. coli catalase HPII with cyanide as ligand and as inhibitor. Biochim. Biophys. Acta 1996, 1298, 241-249.
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 241-249
    • Maj, M.1    Nicholls, P.2    Obinger, C.3    Hillar, A.4    Loewen, P.C.5


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