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Volumn 90, Issue , 2014, Pages 36-44

Production, purification, and characterization of a highly thermostable and humic acid biodegrading peroxidase from a decolorizing Streptomyces albidoflavus strain TN644 isolated from a Tunisian off-shore oil field

Author keywords

Acidic environment; Actinomycetes; Decolorizing activity; Humic acids; Peroxidase; Purification

Indexed keywords

2 ,4 DICHLOROPHENOL(2 ,4 DCP); ACIDIC ENVIRONMENT; ACTINOMYCETES; HUMIC ACID; MATRIX ASSISTED LASER DESORPTION; MICHAELIS-MENTEN KINETIC; PEROXIDASE; PHYSIOLOGICAL AND BIOCHEMICAL CHARACTERISTICS;

EID: 84896899267     PISSN: 09648305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibiod.2014.02.001     Document Type: Article
Times cited : (22)

References (24)
  • 1
    • 77957795368 scopus 로고    scopus 로고
    • Removal of natural humic acids by decolorizing actinomycetes isolated from different soils (Algeria) for application in water purification
    • Badis A., Ferradji F.Z., Boucherit A., Fodil D., Boutoumi H. Removal of natural humic acids by decolorizing actinomycetes isolated from different soils (Algeria) for application in water purification. Desalination 2010, 259:216-222.
    • (2010) Desalination , vol.259 , pp. 216-222
    • Badis, A.1    Ferradji, F.Z.2    Boucherit, A.3    Fodil, D.4    Boutoumi, H.5
  • 2
    • 33645241971 scopus 로고    scopus 로고
    • Purification and some properties of Mn peroxidase from Lentinula edodes
    • Boer C.G., Obici L., de Souza C.G.M., Peralta R.M. Purification and some properties of Mn peroxidase from Lentinula edodes. Process Biochem. 2006, 41:1203-1207.
    • (2006) Process Biochem. , vol.41 , pp. 1203-1207
    • Boer, C.G.1    Obici, L.2    de Souza, C.G.M.3    Peralta, R.M.4
  • 3
    • 0017184389 scopus 로고
    • Arapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Arapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0031805018 scopus 로고    scopus 로고
    • Use of azo dye ligand chromatography for the partial purification of a novel extracellular peroxidase from Streptomyces viridosporus T7A
    • Burke N.S., Crawford D.L. Use of azo dye ligand chromatography for the partial purification of a novel extracellular peroxidase from Streptomyces viridosporus T7A. Appl. Microbiol. Biotechnol. 1998, 49:523-530.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 523-530
    • Burke, N.S.1    Crawford, D.L.2
  • 5
    • 33745522520 scopus 로고    scopus 로고
    • Assessing the trihalomethane formation potential of aquatic fulvic and humic acids fractionated using thin-layer chromatography
    • Eish M.Y., Wells M.J. Assessing the trihalomethane formation potential of aquatic fulvic and humic acids fractionated using thin-layer chromatography. J.Chromatogr. 2006, 1116:272-276.
    • (2006) J.Chromatogr. , vol.1116 , pp. 272-276
    • Eish, M.Y.1    Wells, M.J.2
  • 6
    • 84890221279 scopus 로고    scopus 로고
    • Assessment of biotransformation of organic matter during co-composting of sewage sludge-lignocelullosic waste by chemical, FTIR analyses, and phytotoxicity tests
    • El Fels L., Zamama M., El Asli A., Hafidi M. Assessment of biotransformation of organic matter during co-composting of sewage sludge-lignocelullosic waste by chemical, FTIR analyses, and phytotoxicity tests. Int. Biodeterior. Biodegrad. 2014, 87:128-137.
    • (2014) Int. Biodeterior. Biodegrad. , vol.87 , pp. 128-137
    • El Fels, L.1    Zamama, M.2    El Asli, A.3    Hafidi, M.4
  • 8
    • 79953075507 scopus 로고    scopus 로고
    • Purification and characterization of two extracellular peroxidases from Streptomyces sp. strain AM2, a decolorizing actinomycetes responsible for the biodegradation of natural humic acids
    • Fodil D., Badis A., Jaouadi B., Zaraî N., Ferradji F.Z., Boutoumi H. Purification and characterization of two extracellular peroxidases from Streptomyces sp. strain AM2, a decolorizing actinomycetes responsible for the biodegradation of natural humic acids. Int. Biodeterior. Biodegrad. 2011, 65:470-478.
    • (2011) Int. Biodeterior. Biodegrad. , vol.65 , pp. 470-478
    • Fodil, D.1    Badis, A.2    Jaouadi, B.3    Zaraî, N.4    Ferradji, F.Z.5    Boutoumi, H.6
  • 9
    • 84858753048 scopus 로고    scopus 로고
    • Athermostable humic acid peroxidase from Streptomyces sp. strain AH4: purification and biochemical characterization
    • Fodil D., Jaouadi B., Badis A., Nadia Z.J., Ferradji F.Z., Bejar S., Boutoumi H. Athermostable humic acid peroxidase from Streptomyces sp. strain AH4: purification and biochemical characterization. Bioresour. Technol. 2012, 111:383-390.
    • (2012) Bioresour. Technol. , vol.111 , pp. 383-390
    • Fodil, D.1    Jaouadi, B.2    Badis, A.3    Nadia, Z.J.4    Ferradji, F.Z.5    Bejar, S.6    Boutoumi, H.7
  • 10
    • 49549084405 scopus 로고    scopus 로고
    • Lignin peroxidase from Streptomyces viridosporus T7A: enzyme concentration using ultrafiltration
    • Gottschalk L.M., Bon E.P., Nobrega R. Lignin peroxidase from Streptomyces viridosporus T7A: enzyme concentration using ultrafiltration. Appl. Biochem. Biotechnol. 2008, 147:23-32.
    • (2008) Appl. Biochem. Biotechnol. , vol.147 , pp. 23-32
    • Gottschalk, L.M.1    Bon, E.P.2    Nobrega, R.3
  • 11
    • 79953253563 scopus 로고    scopus 로고
    • Mechanisms of humic acids degradation by white rot fungi explored using 1H NMR spectroscopy and FTICR mass spectrometry
    • Grinhut T., Hertkorn N., Schmitt-Kopplin P., Hadar Y., Chen Y. Mechanisms of humic acids degradation by white rot fungi explored using 1H NMR spectroscopy and FTICR mass spectrometry. Environ. Sci. Technol. 2011, 45:2748-2754.
    • (2011) Environ. Sci. Technol. , vol.45 , pp. 2748-2754
    • Grinhut, T.1    Hertkorn, N.2    Schmitt-Kopplin, P.3    Hadar, Y.4    Chen, Y.5
  • 12
    • 22744435639 scopus 로고    scopus 로고
    • Purification, characterization and evaluation of extracellular peroxidase from two Coprinus species for aqueous phenol treatment
    • Ikehata K., Buchanan I.D., Pickard M.A., Smith D.W. Purification, characterization and evaluation of extracellular peroxidase from two Coprinus species for aqueous phenol treatment. Bioresour. Technol. 2005, 96:1758-1770.
    • (2005) Bioresour. Technol. , vol.96 , pp. 1758-1770
    • Ikehata, K.1    Buchanan, I.D.2    Pickard, M.A.3    Smith, D.W.4
  • 13
    • 67349231583 scopus 로고    scopus 로고
    • Functional expression of Coprinus cinereus peroxidase in Pichia pastoris
    • Kim S.J., Lee J.A., Won K., Kim Y.H., Song B.K. Functional expression of Coprinus cinereus peroxidase in Pichia pastoris. Process Biochem. 2009, 44:731-735.
    • (2009) Process Biochem. , vol.44 , pp. 731-735
    • Kim, S.J.1    Lee, J.A.2    Won, K.3    Kim, Y.H.4    Song, B.K.5
  • 14
    • 84879589523 scopus 로고    scopus 로고
    • Humic acid removal by electrocoagulation using aluminium sacrificial anode under influencing operational parameters
    • (in press)
    • Kourdali S., Badis A., Saiba A., Boucherit A., Boutoumi H. Humic acid removal by electrocoagulation using aluminium sacrificial anode under influencing operational parameters. Desalination Water Treat. 2013, 1-12. (in press). 10.1080/19443994.2013.814003.
    • (2013) Desalination Water Treat. , pp. 1-12
    • Kourdali, S.1    Badis, A.2    Saiba, A.3    Boucherit, A.4    Boutoumi, H.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0031239477 scopus 로고    scopus 로고
    • Amodel of peroxidase activity with inhibition by hydrogen peroxide
    • Nicell J.A., Wright H. Amodel of peroxidase activity with inhibition by hydrogen peroxide. Enzyme Microb. Technol. 1997, 21:302-310.
    • (1997) Enzyme Microb. Technol. , vol.21 , pp. 302-310
    • Nicell, J.A.1    Wright, H.2
  • 17
    • 4444235114 scopus 로고    scopus 로고
    • The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB
    • Ortiz de Orue Lucana D., Schaa T., Schrempf H. The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB. Microbiology 2004, 150:2575-2585.
    • (2004) Microbiology , vol.150 , pp. 2575-2585
    • Ortiz de Orue Lucana, D.1    Schaa, T.2    Schrempf, H.3
  • 19
    • 33947304611 scopus 로고    scopus 로고
    • Purification and characterization of olive (Olea europaea L.) peroxidase - evidence for the occurrence of a pectin binding peroxidase
    • Saraiva J.A., Nunes C.S., Coimbra M.A. Purification and characterization of olive (Olea europaea L.) peroxidase - evidence for the occurrence of a pectin binding peroxidase. Food Chem. 2007, 101:1571-1579.
    • (2007) Food Chem. , vol.101 , pp. 1571-1579
    • Saraiva, J.A.1    Nunes, C.S.2    Coimbra, M.A.3
  • 20
    • 33744917575 scopus 로고    scopus 로고
    • YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins
    • Sturm A., Schierhorn A., Lindenstrauss U., Lilie H., Bruser T. YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins. J.Biol. Chem. 2006, 281:13972-13978.
    • (2006) J.Biol. Chem. , vol.281 , pp. 13972-13978
    • Sturm, A.1    Schierhorn, A.2    Lindenstrauss, U.3    Lilie, H.4    Bruser, T.5
  • 21
    • 77950916127 scopus 로고    scopus 로고
    • Horseradish peroxidase production from Spodoptera frugiperda larvae: a simple and inexpensive method
    • Targovnik A.M., Romero L.V., Wolman F.J., Cascone O., Miranda M.V. Horseradish peroxidase production from Spodoptera frugiperda larvae: a simple and inexpensive method. Process Biochem. 2010, 45:835-840.
    • (2010) Process Biochem. , vol.45 , pp. 835-840
    • Targovnik, A.M.1    Romero, L.V.2    Wolman, F.J.3    Cascone, O.4    Miranda, M.V.5
  • 22
    • 77952889772 scopus 로고    scopus 로고
    • Arobust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily
    • van Bloois E., Torres Pazmino D.E., Winter R.T., Fraaije M.W. Arobust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl. Microbiol. Biotechnol. 2010, 86:1419-1430.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1419-1430
    • van Bloois, E.1    Torres Pazmino, D.E.2    Winter, R.T.3    Fraaije, M.W.4
  • 23
    • 84888068622 scopus 로고    scopus 로고
    • Production optimization and molecular structure characterization of a newly isolated novel laccase from Fusarium solani MAS2, an anthracene-degrading fungus
    • Wu Y.R., Nian D.L. Production optimization and molecular structure characterization of a newly isolated novel laccase from Fusarium solani MAS2, an anthracene-degrading fungus. Int. Biodeterior. Biodegrad. 2014, 86:382-389.
    • (2014) Int. Biodeterior. Biodegrad. , vol.86 , pp. 382-389
    • Wu, Y.R.1    Nian, D.L.2
  • 24
    • 0034063020 scopus 로고    scopus 로고
    • Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity
    • Yumoto I., Ichihashi D., Iwata H., Istokovics A., Ichise N., Matsuyama H., Okuyama H., Kawasaki K. Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity. J.Bacteriol. 2000, 182:1903-1909.
    • (2000) J.Bacteriol. , vol.182 , pp. 1903-1909
    • Yumoto, I.1    Ichihashi, D.2    Iwata, H.3    Istokovics, A.4    Ichise, N.5    Matsuyama, H.6    Okuyama, H.7    Kawasaki, K.8


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