메뉴 건너뛰기




Volumn 9, Issue 10, 2014, Pages

Application of a novel alkali-tolerant thermostable DyP-type peroxidase from saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTHRAQUINONIC DYE; AZO DYE; DYE; DYP TYPE PEROXIDASE; PEROXIDASE; POLYPEPTIDE; RECOMBINANT PROTEIN; TRIARYLMETHANE DYE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

EID: 84908180918     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0110319     Document Type: Article
Times cited : (61)

References (57)
  • 2
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder KG (1992) Superfamily of plant, fungal and bacterial peroxidases. Curr Opin Struc Biol 2: 388-393.
    • (1992) Curr Opin Struc Biol , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 3
    • 69749084914 scopus 로고
    • Lignin peroxidase of Phanerochaete chrysosporium
    • Tien M, Kirk TK (1988) Lignin peroxidase of Phanerochaete chrysosporium. Method Enzymol 161: 238-249.
    • (1988) Method Enzymol , vol.161 , pp. 238-249
    • Tien, M.1    Kirk, T.K.2
  • 4
    • 0027096634 scopus 로고
    • Manganese (II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators
    • Wariishi H, Valli K, Gold MH (1992) Manganese (II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators. J Biol Chem 267: 23688-23695.
    • (1992) J Biol Chem , vol.267 , pp. 23688-23695
    • Wariishi, H.1    Valli, K.2    Gold, M.H.3
  • 5
    • 20144380279 scopus 로고    scopus 로고
    • Tryptophan-based radical in the catalytic mechanism of versatile peroxidase from Bjerkandera adusta
    • Pogni R, Baratto MC, Giansanti S, Teutloff C, Verdin J, et al. (2005) Tryptophan-based radical in the catalytic mechanism of versatile peroxidase from Bjerkandera adusta. Biochemistry 44: 4267-4274.
    • (2005) Biochemistry , vol.44 , pp. 4267-4274
    • Pogni, R.1    Baratto, M.C.2    Giansanti, S.3    Teutloff, C.4    Verdin, J.5
  • 7
    • 84858704829 scopus 로고    scopus 로고
    • Identification and molecular characterization of a novel DyP-type peroxidase from Pseudomonas aeruginosa PKE117
    • Li J, Liu C, Li B, Yuan H, Yang J, et al. (2012) Identification and molecular characterization of a novel DyP-type peroxidase from Pseudomonas aeruginosa PKE117. Appl Biochem Biotech 166: 774-785.
    • (2012) Appl Biochem Biotech , vol.166 , pp. 774-785
    • Li, J.1    Liu, C.2    Li, B.3    Yuan, H.4    Yang, J.5
  • 8
    • 84879834878 scopus 로고    scopus 로고
    • Characterization of a novel dye-decolorizing peroxidase (DyP)-Type Enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw
    • Salvachúa D, Prieto A, Martínez Á T, Martínez MJ (2013) Characterization of a novel dye-decolorizing peroxidase (DyP)-Type Enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw. Appl Environ Microbiol 79: 4316-4324.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 4316-4324
    • Salvachúa, D.1    Prieto, A.2    Martínez, A.T.3    Martínez, M.J.4
  • 9
    • 4143128834 scopus 로고    scopus 로고
    • A unique dyedecolorizing peroxidase, DyP, from Thanatephorus cucumeris Dec 1: Heterologous expression, crystallization and preliminary X-ray analysis
    • Sato T, Hara S, Matsui T, Sazaki G, Saijo S, et al. (2004) A unique dyedecolorizing peroxidase, DyP, from Thanatephorus cucumeris Dec 1: heterologous expression, crystallization and preliminary X-ray analysis. Acta Crystallogr D 60: 149-152.
    • (2004) Acta Crystallogr D , vol.60 , pp. 149-152
    • Sato, T.1    Hara, S.2    Matsui, T.3    Sazaki, G.4    Saijo, S.5
  • 10
    • 0037992681 scopus 로고    scopus 로고
    • High performance degradation of azo dye acid orange 7 and sulfanilic acid in laboratory scale reactor after seeding with cultured bacterial strains
    • Coughlin MF, Kinkle BK, Bishop PL (2003) High performance degradation of azo dye acid orange 7 and sulfanilic acid in laboratory scale reactor after seeding with cultured bacterial strains. Water Res 37: 2757-2763.
    • (2003) Water Res , vol.37 , pp. 2757-2763
    • Coughlin, M.F.1    Kinkle, B.K.2    Bishop, P.L.3
  • 11
    • 60949094155 scopus 로고    scopus 로고
    • Purification and characterization of two DyP isozymes from Thanatephorus cucumeris Dec 1 specifically expressed in an air-membrane surface bioreactor
    • Shimokawa T, Shoda M, Sugano Y (2009) Purification and characterization of two DyP isozymes from Thanatephorus cucumeris Dec 1 specifically expressed in an air-membrane surface bioreactor. J Biosci Bioeng 107: 113-115.
    • (2009) J Biosci Bioeng , vol.107 , pp. 113-115
    • Shimokawa, T.1    Shoda, M.2    Sugano, Y.3
  • 12
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • Sugano Y (2009) DyP-type peroxidases comprise a novel heme peroxidase family. Cell Mol Life Sci 66: 1387-1403.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1387-1403
    • Sugano, Y.1
  • 14
    • 84879419989 scopus 로고    scopus 로고
    • Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood-and litterdegrading agaricomycetes compared to other fungal and plant hemeperoxidases
    • Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, et al. (2013) Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood-and litterdegrading agaricomycetes compared to other fungal and plant hemeperoxidases. Appl Microbiol Biotechnol 97: 5839-5849.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 5839-5849
    • Liers, C.1    Pecyna, M.J.2    Kellner, H.3    Worrich, A.4    Zorn, H.5
  • 15
    • 84896691646 scopus 로고    scopus 로고
    • New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: Towards biotechnological applications
    • Santos A, Mendes S, Brissos V, Martins LO (2014) New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications. Appl Microbiol Biotechnol 98: 2053-2065.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 2053-2065
    • Santos, A.1    Mendes, S.2    Brissos, V.3    Martins, L.O.4
  • 16
    • 72949091861 scopus 로고    scopus 로고
    • Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. Strain PCC 7120
    • Ogola HJO, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, et al. (2009) Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. Appl Environ Microbiol 75: 7509-7518.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 7509-7518
    • Hjo, O.1    Kamiike, T.2    Hashimoto, N.3    Ashida, H.4    Ishikawa, T.5
  • 17
    • 79958856367 scopus 로고    scopus 로고
    • Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase
    • Ahmad M, Roberts JN, Hardiman EM, Singh R, Eltis LD, et al. (2011) Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase. Biochemistry 50: 5096-5107.
    • (2011) Biochemistry , vol.50 , pp. 5096-5107
    • Ahmad, M.1    Roberts, J.N.2    Hardiman, E.M.3    Singh, R.4    Eltis, L.D.5
  • 18
    • 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 FZ, et al. (2011) Purification and characterization of two extracellular peroxidases from Streptomyces sp. strain AM2, a decolorizing actinomycetes responsible for the biodegradation of natural humic acids. Int Biodeter Biodegr 65: 470-478.
    • (2011) Int Biodeter Biodegr , vol.65 , pp. 470-478
    • Fodil, D.1    Badis, A.2    Jaouadi, B.3    Zaraî, N.4    Ferradji, F.Z.5
  • 19
    • 84858753048 scopus 로고    scopus 로고
    • A thermostable humic acid peroxidase from Streptomyces sp. Strain AH4: Purification and biochemical characterization
    • Fodil D, Jaouadi B, Badis A, Nadia ZJ, Ferradji FZ, et al. (2012) A thermostable humic acid peroxidase from Streptomyces sp. strain AH4: Purification and biochemical characterization. Bioresource Technol 111: 383-390.
    • (2012) Bioresource Technol , vol.111 , pp. 383-390
    • Fodil, D.1    Jaouadi, B.2    Badis, A.3    Nadia, Z.J.4    Ferradji, F.Z.5
  • 21
    • 77952889772 scopus 로고    scopus 로고
    • A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily
    • van Bloois E, Pazmiño DET, Winter RT, Fraaije MW (2010) A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl Microbiol Biotechnol 86: 1419-1430.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1419-1430
    • Van Bloois, E.1    Pazmiño, D.E.T.2    Winter, R.T.3    Fraaije, M.W.4
  • 22
    • 0034798976 scopus 로고    scopus 로고
    • The use of extracellular enzymes from Streptomyces albus ATCC 3005 for the bleaching of eucalyptus kraft pulp
    • Antonopoulos V, Hernandez M, Arias M, Mavrakos E, Ball A (2001) The use of extracellular enzymes from Streptomyces albus ATCC 3005 for the bleaching of eucalyptus kraft pulp. Appl Microbiol Biotechnol 57: 92-97.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 92-97
    • Antonopoulos, V.1    Hernandez, M.2    Arias, M.3    Mavrakos, E.4    Ball, A.5
  • 23
    • 0033952763 scopus 로고    scopus 로고
    • Purification and properties of three endo-β-1, 4-xylanases produced by Streptomyces sp. Strain S38 which differ in their ability to enhance the bleaching of kraft pulps
    • Georis J, Giannotta F, De Buyl E, Granier Bt, Frère J-M (2000) Purification and properties of three endo-β-1, 4-xylanases produced by Streptomyces sp. strain S38 which differ in their ability to enhance the bleaching of kraft pulps. Enzyme Microb Tech 26: 178-186.
    • (2000) Enzyme Microb Tech , vol.26 , pp. 178-186
    • Georis, J.1    Giannotta, F.2    De Buyl, E.3    Granier Bt.4    Frère, J.-M.5
  • 24
    • 0242661223 scopus 로고    scopus 로고
    • White-rot fungi and their enzymes for the treatment of industrial dye effluents
    • Wesenberg D, Kyriakides I, Agathos SN (2003) White-rot fungi and their enzymes for the treatment of industrial dye effluents. Biotechnol Adv 22: 161-187.
    • (2003) Biotechnol Adv , vol.22 , pp. 161-187
    • Wesenberg, D.1    Kyriakides, I.2    Agathos, S.N.3
  • 25
    • 0032101040 scopus 로고    scopus 로고
    • Effects of manganese peroxidase on residual lignin of softwood kraft pulp
    • Reid ID, Paice MG (1998) Effects of manganese peroxidase on residual lignin of softwood kraft pulp. Appl Environ Microbiol 64: 2273-2274.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2273-2274
    • Reid, I.D.1    Paice, M.G.2
  • 26
    • 0034307657 scopus 로고    scopus 로고
    • Enhanced production of a thermostable xylanase from Streptomyces sp. QG-11-3 and its application in biobleaching of eucalyptus kraft pulp
    • Beg QK, Bhushan B, Kapoor M, Hoondal G (2000) Enhanced production of a thermostable xylanase from Streptomyces sp. QG-11-3 and its application in biobleaching of eucalyptus kraft pulp. Enzyme Microb Techn 27: 459-466.
    • (2000) Enzyme Microb Techn , vol.27 , pp. 459-466
    • Beg, Q.K.1    Bhushan, B.2    Kapoor, M.3    Hoondal, G.4
  • 27
    • 0030070308 scopus 로고    scopus 로고
    • Bleaching of hardwood kraft pulp with manganese peroxidase from Phanerochaete sordida YK-624 without addition of MnSO (inf4)
    • Harazono K, Kondo R, Sakai K (1996) Bleaching of hardwood kraft pulp with manganese peroxidase from Phanerochaete sordida YK-624 without addition of MnSO (inf4). Appl Environ Microbiol 62: 913-917.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 913-917
    • Harazono, K.1    Kondo, R.2    Sakai, K.3
  • 28
    • 0012369897 scopus 로고    scopus 로고
    • Metabolism of pentachlorophenol by Saccharomonospora viridis strains isolated from mushroom compost
    • Webb MD, Ewbank G, Perkins J, McCarthy AJ (2001) Metabolism of pentachlorophenol by Saccharomonospora viridis strains isolated from mushroom compost. Soil Biol Biochem 33: 1903-1914.
    • (2001) Soil Biol Biochem , vol.33 , pp. 1903-1914
    • Webb, M.D.1    Ewbank, G.2    Perkins, J.3    McCarthy, A.J.4
  • 29
    • 80053475268 scopus 로고    scopus 로고
    • Complete genome sequence of Saccharomonospora viridis type strain (P101T)
    • Pati A, Sikorski J, Nolan M, Lapidus A, Copeland A, et al. (2009) Complete genome sequence of Saccharomonospora viridis type strain (P101T). Stand Genomic Sci 1: 141-149.
    • (2009) Stand Genomic Sci , vol.1 , pp. 141-149
    • Pati, A.1    Sikorski, J.2    Nolan, M.3    Lapidus, A.4    Copeland, A.5
  • 30
    • 34548809711 scopus 로고    scopus 로고
    • Crystal structures of two novel dye-decolorizing peroxidases reveal a b-barrel fold with a conserved heme-binding motif
    • Zubieta C, Krishna S, Kapoor M, Kozbial P, McMullan D, et al. (2007) Crystal structures of two novel dye-decolorizing peroxidases reveal a b-barrel fold with a conserved heme-binding motif. Proteins: Structure, Function, and Bioinformatics 69: 223-233.
    • (2007) Proteins: Structure, Function, and Bioinformatics , vol.69 , pp. 223-233
    • Zubieta, C.1    Krishna, S.2    Kapoor, M.3    Kozbial, P.4    McMullan, D.5
  • 31
    • 79958818206 scopus 로고    scopus 로고
    • Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1
    • Roberts JN, Singh R, Grigg JC, Murphy ME, Bugg TD, et al. (2011) Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1. Biochemistry 50: 5108-5119.
    • (2011) Biochemistry , vol.50 , pp. 5108-5119
    • Roberts, J.N.1    Singh, R.2    Grigg, J.C.3    Murphy, M.E.4    Bugg, T.D.5
  • 32
    • 79955445197 scopus 로고    scopus 로고
    • Crystal structure and biochemical features of EfeB/YcdB from Escherichia coli O157 ASP235 plays divergent roles in different enzyme-catalyzed processes
    • Liu X, Du Q, Wang Z, Zhu D, Huang Y, et al. (2011) Crystal structure and biochemical features of EfeB/YcdB from Escherichia coli O157 ASP235 plays divergent roles in different enzyme-catalyzed processes. J Biol Chem 286: 14922-14931.
    • (2011) J Biol Chem , vol.286 , pp. 14922-14931
    • Liu, X.1    Du, Q.2    Wang, Z.3    Zhu, D.4    Huang, Y.5
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 22: 4673-4680.
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S, Nei M, Dudley J, Tamura K (2008) MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinform 9: 299-306.
    • (2008) Brief Bioinform , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 35
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 37
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucl Acids Res 31: 3381-3385.
    • (2003) Nucl Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 38
    • 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
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 32944464376 scopus 로고    scopus 로고
    • Production and characterization of a bacterial single-chain antibody fragment specific to B-cellactivating factor of the TNF family
    • Cao P, Tang XM, Guan ZB, Diao ZY, Zhang SQ (2005) Production and characterization of a bacterial single-chain antibody fragment specific to B-cellactivating factor of the TNF family. Protein Expr Purif 43: 157-164.
    • (2005) Protein Expr Purif , vol.43 , pp. 157-164
    • Cao, P.1    Tang, X.M.2    Guan, Z.B.3    Diao, Z.Y.4    Zhang, S.Q.5
  • 41
    • 0034127006 scopus 로고    scopus 로고
    • Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1
    • Sugano Y, Nakano R, Sasaki K, Shoda M (2000) Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1. Appl Environ Microbiol 66: 1754-1758.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1754-1758
    • Sugano, Y.1    Nakano, R.2    Sasaki, K.3    Shoda, M.4
  • 42
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56: 658-666.
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 43
    • 0028110409 scopus 로고
    • Bleaching of hardwood kraft pulp with manganese peroxidase secreted from Phanerochaete sordida YK-624
    • Kondo R, Harazono K, Sakai K (1994) Bleaching of hardwood kraft pulp with manganese peroxidase secreted from Phanerochaete sordida YK-624. Appl Environ Microbiol 60: 4359-4363.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4359-4363
    • Kondo, R.1    Harazono, K.2    Sakai, K.3
  • 44
    • 0345472013 scopus 로고    scopus 로고
    • Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes
    • Kim SJ, Shoda M (1999) Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes. Appl Environ Microbiol 65: 1029-1035.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1029-1035
    • Kim, S.J.1    Shoda, M.2
  • 45
    • 0026714617 scopus 로고
    • A new assay for lignin-type peroxidases employing the dye azure B
    • Archibald FS (1992) A new assay for lignin-type peroxidases employing the dye azure B. Appl Environ Microbiol 58: 3110-3116.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3110-3116
    • Archibald, F.S.1
  • 46
    • 0025400073 scopus 로고
    • Modification of paper properties by the pretreatment of pulp with Saccharomonospora viridis xylanase
    • Roberts JC, McCarthy AJ, Flynn NJ, Broda P (1990) Modification of paper properties by the pretreatment of pulp with Saccharomonospora viridis xylanase. Enzyme Microb Tech 12: 210-213.
    • (1990) Enzyme Microb Tech , vol.12 , pp. 210-213
    • Roberts, J.C.1    McCarthy, A.J.2    Flynn, N.J.3    Broda, P.4
  • 47
    • 84864046095 scopus 로고    scopus 로고
    • A novel, alkali-tolerant thermostable xylanase from Saccharomonospora viridis: Direct gene cloning, expression and enzyme characterization
    • Wang Z, Jin Y, Wu H, Tian Z, Wu Y, et al. (2012) A novel, alkali-tolerant thermostable xylanase from Saccharomonospora viridis: direct gene cloning, expression and enzyme characterization. World J Microbiol Biotechnol 28: 2741-2748.
    • (2012) World J Microbiol Biotechnol , vol.28 , pp. 2741-2748
    • Wang, Z.1    Jin, Y.2    Wu, H.3    Tian, Z.4    Wu, Y.5
  • 48
    • 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, Brüser T (2006) YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins. J Biol Chem 281: 13972-13978.
    • (2006) J Biol Chem , vol.281 , pp. 13972-13978
    • Sturm, A.1    Schierhorn, A.2    Lindenstrauss, U.3    Lilie, H.4    Brüser, T.5
  • 49
    • 0036085435 scopus 로고    scopus 로고
    • Decolorization of triphenylmethane and azo dyes by Citrobacter sp
    • An S-Y, Min S-K, Cha I-H, Choi Y-L, Cho Y-S, et al. (2002) Decolorization of triphenylmethane and azo dyes by Citrobacter sp. Biotechnol Lett 24: 1037-1040.
    • (2002) Biotechnol Lett , vol.24 , pp. 1037-1040
    • An, S.-Y.1    Min, S.-K.2    Cha, I.-H.3    Choi, Y.-L.4    Cho, Y.-S.5
  • 50
    • 33749846244 scopus 로고    scopus 로고
    • Decolorization of triphenylmethane, azo, and anthraquinone dyes by a newly isolated Aeromonas hydrophila strain
    • Ren S, Guo J, Zeng G, Sun G (2006) Decolorization of triphenylmethane, azo, and anthraquinone dyes by a newly isolated Aeromonas hydrophila strain. Appl Microbiol Biotechnol 72: 1316-1321.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 1316-1321
    • Ren, S.1    Guo, J.2    Zeng, G.3    Sun, G.4
  • 51
    • 0344141459 scopus 로고    scopus 로고
    • Decolorization of triphenylmethane dyes and textile and dye-stuff effluent by Kurthia sp
    • Sani RK, Banerjee UC (1999) Decolorization of triphenylmethane dyes and textile and dye-stuff effluent by Kurthia sp. Enzyme and Microbial Technology 24: 433-437.
    • (1999) Enzyme and Microbial Technology , vol.24 , pp. 433-437
    • Sani, R.K.1    Banerjee, U.C.2
  • 53
    • 33750380299 scopus 로고    scopus 로고
    • Biological decolorization of dye solution containing Malachite Green by microalgae Cosmarium sp
    • Daneshvar N, Ayazloo M, Khataee A, Pourhassan M (2007) Biological decolorization of dye solution containing Malachite Green by microalgae Cosmarium sp. Bioresource Technol 98: 1176-1182.
    • (2007) Bioresource Technol , vol.98 , pp. 1176-1182
    • Daneshvar, N.1    Ayazloo, M.2    Khataee, A.3    Pourhassan, M.4
  • 54
    • 0038650943 scopus 로고    scopus 로고
    • Decolorization of malachite green and crystal violet by waterborne pathogenic mycobacteria
    • Jones JJ, Falkinham JO (2003) Decolorization of malachite green and crystal violet by waterborne pathogenic mycobacteria. Antimicrob Agents Chemother 47: 2323-2326.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2323-2326
    • Jones, J.J.1    Falkinham, J.O.2
  • 55
    • 37549031745 scopus 로고    scopus 로고
    • DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family ASP171 replaces the distal histidine of classical peroxidases
    • Sugano Y, Muramatsu R, Ichiyanagi A, Sato T, Shoda M (2007) DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family ASP171 replaces the distal histidine of classical peroxidases J Biol Chem 282: 36652-36658.
    • (2007) J Biol Chem , vol.282 , pp. 36652-36658
    • Sugano, Y.1    Muramatsu, R.2    Ichiyanagi, A.3    Sato, T.4    Shoda, M.5
  • 56
    • 33745213542 scopus 로고    scopus 로고
    • Statistical optimization of thermo-tolerant xylanase activity from Amazon isolated Bacillus circulans on solid-state cultivation
    • Heck JX, Flores SH, Hertz PF, Ayub MA (2006) Statistical optimization of thermo-tolerant xylanase activity from Amazon isolated Bacillus circulans on solid-state cultivation. Bioresource Technol 97: 1902-1906.
    • (2006) Bioresource Technol , vol.97 , pp. 1902-1906
    • Heck, J.X.1    Flores, S.H.2    Hertz, P.F.3    Ayub, M.A.4
  • 57
    • 84872154522 scopus 로고    scopus 로고
    • Characterization of three novel thermophilic xylanases from Humicola insolens Y1 with application potentials in the brewing industry
    • Du Y, Shi P, Huang H, Zhang X, Luo H, et al. (2013) Characterization of three novel thermophilic xylanases from Humicola insolens Y1 with application potentials in the brewing industry. Bioresource Technol 130: 161-167.
    • (2013) Bioresource Technol , vol.130 , pp. 161-167
    • Du, Y.1    Shi, P.2    Huang, H.3    Zhang, X.4    Luo, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.