메뉴 건너뛰기




Volumn 79, Issue 14, 2013, Pages 4316-4324

Characterization of a novel dye-decolorizing peroxidase (DyP)-type enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGICAL APPLICATIONS; BIOTECHNOLOGICAL POTENTIALS; CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; IMPROVED ACTIVITIES; N-TERMINAL SEQUENCES; PEPTIDE MASS FINGERPRINTING; WHITE-ROT BASIDIOMYCETES;

EID: 84879834878     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00699-13     Document Type: Article
Times cited : (125)

References (42)
  • 1
    • 84869132485 scopus 로고    scopus 로고
    • Degradation of alkylphenols by white rot fungus Irpex lacteus and its manganese peroxidase.
    • Moon DS, Song HG. 2012. Degradation of alkylphenols by white rot fungus Irpex lacteus and its manganese peroxidase. Appl. Biochem. Biotechnol. 168:542-549.
    • (2012) Appl.Biochem.Biotechnol. , vol.168 , pp. 542-549
    • Moon, D.S.1    Song, H.G.2
  • 2
    • 84864415242 scopus 로고    scopus 로고
    • Biodecolorization and biodegradation of reactive Levafix Blue E-RA granulate dye by the white rot fungus Irpex lacteus.
    • Kalpana D, Velmurugan N, Shim JH, Oh BT, Senthil K, Lee YS. 2012. Biodecolorization and biodegradation of reactive Levafix Blue E-RA granulate dye by the white rot fungus Irpex lacteus. J. Environ. Manage. 111: 142-149.
    • (2012) J.Environ.Manage. , vol.111 , pp. 142-149
    • Kalpana, D.1    Velmurugan, N.2    Shim, J.H.3    Oh, B.T.4    Senthil, K.5    Lee, Y.S.6
  • 7
    • 2442462261 scopus 로고    scopus 로고
    • The role of enzymes produced by white-rot fungus Irpex lacteus in the decolorization of the textile industry effluent.
    • Shin KW. 2004. The role of enzymes produced by white-rot fungus Irpex lacteus in the decolorization of the textile industry effluent. J. Microbiol. 42:37-41.
    • (2004) J.Microbiol. , vol.42 , pp. 37-41
    • Shin, K.W.1
  • 10
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases.
    • Welinder KG. 1992. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 2:388-393.
    • (1992) Curr.Opin.Struct.Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 12
    • 37549031745 scopus 로고    scopus 로고
    • DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family.
    • Sugano Y, Muramatsu R, Ichiyanagi A, Sato T, Shoda M. 2007. DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family. 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
  • 13
    • 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
  • 15
    • 84895209619 scopus 로고    scopus 로고
    • Structural and functional features of peroxidases with a potential as industrial biocatalysts
    • In Torres E, AyalaM(ed), Biocatalysts based on heme peroxidases. Springer, Berlin, Germany.
    • Ruiz-Dueñas FJ, Martínez AT. 2010. Structural and functional features of peroxidases with a potential as industrial biocatalysts, p 37-59. In Torres E, AyalaM(ed), Biocatalysts based on heme peroxidases. Springer, Berlin, Germany.
    • (2010) , pp. 37-59
    • Ruiz-Dueñas, F.J.1    Martínez, A.T.2
  • 16
  • 17
    • 76849083614 scopus 로고    scopus 로고
    • DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidizing non- phenolic lignin model compounds and high redox potential dyes.
    • Liers C, Bobeth C, Pecyna M, Ullrich M, Hofrichter M. 2010. DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidizing non- phenolic lignin model compounds and high redox potential dyes. Appl. Microbiol. Biotechnol. 85:1869-1879.
    • (2010) Appl.Microbiol.Biotechnol. , vol.85 , pp. 1869-1879
    • Liers, C.1    Bobeth, C.2    Pecyna, M.3    Ullrich, M.4    Hofrichter, M.5
  • 18
    • 70449130799 scopus 로고    scopus 로고
    • Novel enzymes for use in enzymatic bleaching of food products.
    • patent 7,981,636 B2.
    • Zorn H, Scheibner M, Hulsdau B, Berger RG, de Boer L, Meima RB. July 2011. Novel enzymes for use in enzymatic bleaching of food products. US patent 7,981,636 B2.
    • (2011)
    • Zorn, H.1    Scheibner, M.2    Hulsdau, B.3    Berger, R.G.4    De Boer, L.5    Meima, R.B.6
  • 19
    • 34248326376 scopus 로고    scopus 로고
    • Identification of a new member of the dye-decolorizing peroxidase family from Pleurotus ostreatus.
    • Faraco V, Piscitelli A, Sannia G, Giardina P. 2007. Identification of a new member of the dye-decolorizing peroxidase family from Pleurotus ostreatus. World J. Microbiol. Biotechnol. 23: 889-893.
    • (2007) World J. Microbiol. Biotechnol. , vol.23 , pp. 889-893
    • Faraco, V.1    Piscitelli, A.2    Sannia, G.3    Giardina, P.4
  • 20
    • 67349200794 scopus 로고    scopus 로고
    • Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1.
    • Sugano Y, Matsushima Y, Tsuchiya K, Aoki H, Hirai M, Shoda M. 2009. Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1. Biodegradation 20: 433-440.
    • (2009) Biodegradation , vol.20 , pp. 433-440
    • Sugano, Y.1    Matsushima, Y.2    Tsuchiya, K.3    Aoki, H.4    Hirai, M.5    Shoda, M.6
  • 21
    • 84879419989 scopus 로고    scopus 로고
    • Substrate oxidation by dyedecolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.
    • doi:10.1007/s00253-012-4521-2
    • Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, Steffen KT, Hofrichter M, Ullrich R. 31 October 2012. Substrate oxidation by dyedecolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases. Appl. Microbiol. Biotechnol. doi:10.1007/s00253-012-4521-2.
    • (2012) Appl.Microbiol.Biotechnol.
    • Liers, C.1    Pecyna, M.J.2    Kellner, H.3    Worrich, A.4    Zorn, H.5    Steffen, K.T.6    Hofrichter, M.7    Ullrich, R.8
  • 23
    • 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
  • 25
    • 79959321050 scopus 로고    scopus 로고
    • The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue.
    • Yoshida T, Tsuge H, Konno H, Hisabori T, Sugano Y. 2011. The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue. FEBS J. 278:2387-2394.
    • (2011) FEBS J. , vol.278 , pp. 2387-2394
    • Yoshida, T.1    Tsuge, H.2    Konno, H.3    Hisabori, T.4    Sugano, Y.5
  • 26
    • 31444447716 scopus 로고    scopus 로고
    • Expression on wood, molecular cloning and characterization of three lignin peroxidase (LiP) encoding genes of the white rot fungus Phlebia radiata.
    • Hilden KS, Makela MR, Hakala TK, Hatakka A, Lundell T. 2006. Expression on wood, molecular cloning and characterization of three lignin peroxidase (LiP) encoding genes of the white rot fungus Phlebia radiata. Curr. Genet. 49:97-105.
    • (2006) Curr.Genet. , vol.49 , pp. 97-105
    • Hilden, K.S.1    Makela, M.R.2    Hakala, T.K.3    Hatakka, A.4    Lundell, T.5
  • 28
    • 0037117774 scopus 로고    scopus 로고
    • Purification and characterization of manganese peroxidases from the litter-decomposing basidiomycetes Agrocybe praecox and Stropharia coronilla.
    • Steffen KT, Hofrichter M, Hatakka A. 2002. Purification and characterization of manganese peroxidases from the litter-decomposing basidiomycetes Agrocybe praecox and Stropharia coronilla. Enzyme Microb. Technol. 30:550-555.
    • (2002) Enzyme Microb.Technol. , vol.30 , pp. 550-555
    • Steffen, K.T.1    Hofrichter, M.2    Hatakka, A.3
  • 29
    • 0038702590 scopus 로고    scopus 로고
    • Isolation and cDNA cloning of novel hydrogen peroxide-dependent phenol oxidase from the basidiomycete Termitomyces albuminosus.
    • Johjima T, Ohkuma M, Kudo T. 2003. Isolation and cDNA cloning of novel hydrogen peroxide-dependent phenol oxidase from the basidiomycete Termitomyces albuminosus. Appl. Microbiol. Biotechnol. 61:220-225.
    • (2003) Appl.Microbiol.Biotechnol. , vol.61 , pp. 220-225
    • Johjima, T.1    Ohkuma, M.2    Kudo, T.3
  • 30
    • 0032936257 scopus 로고    scopus 로고
    • cDNA cloning and genetic analysis of a novel decolorizing enzyme, peroxidase gene dyp from Geotrichum candidum Dec 1.
    • Sugano Y, Sasaki K, Shoda M. 1999. cDNA cloning and genetic analysis of a novel decolorizing enzyme, peroxidase gene dyp from Geotrichum candidum Dec 1. J. Biosci. Bioeng. 87:411-417.
    • (1999) J.Biosci.Bioeng. , vol.87 , pp. 411-417
    • Sugano, Y.1    Sasaki, K.2    Shoda, M.3
  • 31
    • 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
  • 33
    • 30744455476 scopus 로고    scopus 로고
    • Purification and characterization of manganese peroxidase of the white-rot fungus Irpex lacteus.
    • Shin KS, Kim YH, Lim JS. 2005. Purification and characterization of manganese peroxidase of the white-rot fungus Irpex lacteus. J. Microbiol. 43:503-509.
    • (2005) J.Microbiol. , vol.43 , pp. 503-509
    • Shin, K.S.1    Kim, Y.H.2    Lim, J.S.3
  • 35
    • 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
  • 36
    • 0040914374 scopus 로고    scopus 로고
    • Mechanism of peroxidase inactivation in liquid cultures of the ligninolytic fungus Pleurotus pulmonarius.
    • Böckle B, Martínez MJ, Guillén F, Martínez AT. 1999. Mechanism of peroxidase inactivation in liquid cultures of the ligninolytic fungus Pleurotus pulmonarius. Appl. Environ. Microbiol. 65:923-928.
    • (1999) Appl.Environ.Microbiol. , vol.65 , pp. 923-928
    • Böckle, B.1    Martínez, M.J.2    Guillén, F.3    Martínez, A.T.4
  • 38
    • 19544374902 scopus 로고    scopus 로고
    • Influence of Pb contamination in boreal forest soil on the growth and ligninolytic activity of litter-decomposing fungi.
    • Tuomela M, Steffen KT, Kerko E, Hartikainen H, Hofrichter M, Hatakka A. 2005. Influence of Pb contamination in boreal forest soil on the growth and ligninolytic activity of litter-decomposing fungi. FEMS Microbiol. Ecol. 53:179-186.
    • (2005) FEMS Microbiol.Ecol. , vol.53 , pp. 179-186
    • Tuomela, M.1    Steffen, K.T.2    Kerko, E.3    Hartikainen, H.4    Hofrichter, M.5    Hatakka, A.6
  • 40
    • 77949873759 scopus 로고    scopus 로고
    • Production of bioethanol from wheat straw: An overview on pretreatment, hydrolysis and fermentation.
    • Talebnia F, Karakashev D, Angelidaki I. 2010. Production of bioethanol from wheat straw: an overview on pretreatment, hydrolysis and fermentation. Bioresour. Technol. 101:4744-4753.
    • (2010) Bioresour.Technol. , vol.101 , pp. 4744-4753
    • Talebnia, F.1    Karakashev, D.2    Angelidaki, I.3
  • 41
    • 80053623434 scopus 로고    scopus 로고
    • The promoting effect of byproducts from Irpex lacteus on subsequent enzymatic hydrolysis of bio-pretreated cornstalks.
    • doi:10.1186/1754-6834-4-37.
    • Du W, Yu H, Song L, Zhang J, Weng C, Ma F, Zhang X. 2011. The promoting effect of byproducts from Irpex lacteus on subsequent enzymatic hydrolysis of bio-pretreated cornstalks. Biotechnol. Biofuels 4:37.
    • (2011) Biotechnol.Biofuels , vol.4 , pp. 37
    • Du, W.1    Yu, H.2    Song, L.3    Zhang, J.4    Weng, C.5    Ma, F.6    Zhang, X.7
  • 42
    • 84879815273 scopus 로고    scopus 로고
    • Method for modifying non-starch carbohydrate material using peroxidase enzyme.
    • Patent WO2009EP58871.
    • Zorn H, Szweda R, Kumar M, Wilms J. July 2009. Method for modifying non-starch carbohydrate material using peroxidase enzyme. Patent WO2009EP58871.
    • (2009)
    • Zorn, H.1    Szweda, R.2    Kumar, M.3    Wilms, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.