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Volumn 99, Issue 3, 2015, Pages 1025-1038

The ligninolytic peroxidases in the genus Pleurotus: divergence in activities, expression, and potential applications

Author keywords

Diversity; Manganese peroxidase; Peroxidases; Pleurotus; Versatile peroxidase; White rot fungi

Indexed keywords

ENZYMES; FUNGI; GENES; SUBSTRATES;

EID: 84925482558     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6256-8     Document Type: Review
Times cited : (92)

References (117)
  • 1
    • 84869127100 scopus 로고    scopus 로고
    • Enhanced green fluorescent protein expression in Pleurotus ostreatus for in vivo analysis of fungal laccase promoter
    • COI: 1:CAS:528:DC%2BC38XhsFSgtL3L, PID: 22893518
    • Amore A, Honda Y, Faraco V (2012) Enhanced green fluorescent protein expression in Pleurotus ostreatus for in vivo analysis of fungal laccase promoter. Appl Biochem Biotechnol 168:761–769
    • (2012) Appl Biochem Biotechnol , vol.168 , pp. 761-769
    • Amore, A.1    Honda, Y.2    Faraco, V.3
  • 2
    • 84942371891 scopus 로고    scopus 로고
    • Hyper-production of manganese peroxidase by mutant Pleurotus ostreatus MTCC 142 and its applications in biodegradation of textile azo dyes
    • Arunkumara M, Sheik Abdullaa SH (2014) Hyper-production of manganese peroxidase by mutant Pleurotus ostreatus MTCC 142 and its applications in biodegradation of textile azo dyes. Desalin Water Treat. doi:10.1080/19443994.2014.937766
    • (2014) Desalin Water Treat
    • Arunkumara, M.1    Sheik Abdullaa, S.H.2
  • 3
    • 0029111892 scopus 로고
    • Structures of genomic and complementary DNAs coding for Pleurotus ostreatus manganese (II) peroxidase
    • PID: 7669812
    • Asada Y, Watanabe A, Irie T, Nakayama T, Kuwahara M (1995) Structures of genomic and complementary DNAs coding for Pleurotus ostreatus manganese (II) peroxidase. Biochim Biophys Acta 1251:205–209
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 205-209
    • Asada, Y.1    Watanabe, A.2    Irie, T.3    Nakayama, T.4    Kuwahara, M.5
  • 4
    • 84885010091 scopus 로고    scopus 로고
    • Novel catalytic and effluent decolorization functionalities of sol–gel immobilized Pleurotus ostreatus IBL-02 manganese peroxidase produced from bio-processing of wheat straw
    • COI: 1:CAS:528:DC%2BC3sXhvVyrsr7N
    • Asgher M, Aslam B, Iqbal HMN (2013) Novel catalytic and effluent decolorization functionalities of sol–gel immobilized Pleurotus ostreatus IBL-02 manganese peroxidase produced from bio-processing of wheat straw. Chin J Catal 34:1756–1761
    • (2013) Chin J Catal , vol.34 , pp. 1756-1761
    • Asgher, M.1    Aslam, B.2    Iqbal, H.M.N.3
  • 5
    • 84893878393 scopus 로고    scopus 로고
    • Molecular divergence and species delimitation of the cultivated oyster mushroom: integration of IGS1 and ITS
    • Avin FA, Bhassu S, Tan YS, Shahbazi P, Vikineswary S (2014) Molecular divergence and species delimitation of the cultivated oyster mushroom: integration of IGS1 and ITS. Sci World J. doi:10.1155/2014/793414
    • (2014) Sci World J
    • Avin, F.A.1    Bhassu, S.2    Tan, Y.S.3    Shahbazi, P.4    Vikineswary, S.5
  • 6
    • 84884669002 scopus 로고    scopus 로고
    • Production of laccase and manganese peroxidase by Pleurotus pulmonarius in solid-state cultures and application in dye decolorization
    • COI: 1:CAS:528:DC%2BC3sXhsFSlsL%2FI
    • Bazanella GCD, de Souza DF, Castoldi R, Oliveira RF, Bracht A, Peralta RM (2013) Production of laccase and manganese peroxidase by Pleurotus pulmonarius in solid-state cultures and application in dye decolorization. Folia Microbiol 58:641–647
    • (2013) Folia Microbiol , vol.58 , pp. 641-647
    • Bazanella, G.C.D.1    de Souza, D.F.2    Castoldi, R.3    Oliveira, R.F.4    Bracht, A.5    Peralta, R.M.6
  • 7
    • 0030861449 scopus 로고    scopus 로고
    • Enzymatic mechanisms involved in phenanthrene degradation by the white fungus Pleurotus ostreatus
    • COI: 1:CAS:528:DyaK2sXktlekur0%3D, PID: 16535634
    • Bezalel L, Hadar Y, Cerniglia CE (1997) Enzymatic mechanisms involved in phenanthrene degradation by the white fungus Pleurotus ostreatus. Appl Environ Microbiol 63:2495–2501
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2495-2501
    • Bezalel, L.1    Hadar, Y.2    Cerniglia, C.E.3
  • 8
    • 0001685601 scopus 로고
    • Screening wood decayed by white rot fungi for preferential lignin degradation
    • COI: 1:STN:280:DC%2BC3crotVWmtg%3D%3D, PID: 16346631
    • Blanchette RA (1984) Screening wood decayed by white rot fungi for preferential lignin degradation. Appl Environ Microbiol 48(3):647–653
    • (1984) Appl Environ Microbiol , vol.48 , Issue.3 , pp. 647-653
    • Blanchette, R.A.1
  • 9
    • 0035951308 scopus 로고    scopus 로고
    • Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism
    • COI: 1:CAS:528:DC%2BD3MXjvFyktg%3D%3D, PID: 11162097
    • Blodig W, Smith AT, Doyle WA, Piontek K (2001) Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism. J Mol Biol 305:851–861
    • (2001) J Mol Biol , vol.305 , pp. 851-861
    • Blodig, W.1    Smith, A.T.2    Doyle, W.A.3    Piontek, K.4
  • 10
    • 0030025920 scopus 로고    scopus 로고
    • Manganese-mediated lignin degradation by Pleurotus pulmonarius
    • COI: 1:CAS:528:DyaK28XhsVWqtrg%3D, PID: 16535257
    • Camarero S, Böckle B, Martínez MJ, Martínez AT (1996) Manganese-mediated lignin degradation by Pleurotus pulmonarius. Appl Environ Microbiol 62:1070–1072
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1070-1072
    • Camarero, S.1    Böckle, B.2    Martínez, M.J.3    Martínez, A.T.4
  • 11
    • 0033537844 scopus 로고    scopus 로고
    • Description of a versatile peroxidase in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
    • COI: 1:CAS:528:DyaK1MXis1GjtbY%3D, PID: 10187820
    • Camarero S, Sarkar S, Ruiz-Dueñas FJ, Martínez MJ, Martínez AT (1999) Description of a versatile peroxidase in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J Biol Chem 274:10324–10330
    • (1999) J Biol Chem , vol.274 , pp. 10324-10330
    • Camarero, S.1    Sarkar, S.2    Ruiz-Dueñas, F.J.3    Martínez, M.J.4    Martínez, A.T.5
  • 12
    • 0025687772 scopus 로고
    • Characterization of peroxidase secretion and subcellular organization of Phanerochaete chrysosporium INA-12 in the presence of various soybean phospholipid fractions
    • COI: 1:CAS:528:DyaK3MXjvV2htg%3D%3D, PID: 16348381
    • Capdevila C, Moukha S, Ghyczy M, Theilleus J, Gelie B, Delattre M, Corrieu G, Asther M (1990) Characterization of peroxidase secretion and subcellular organization of Phanerochaete chrysosporium INA-12 in the presence of various soybean phospholipid fractions. Appl Environ Microbiol 56:3811–3816
    • (1990) Appl Environ Microbiol , vol.56 , pp. 3811-3816
    • Capdevila, C.1    Moukha, S.2    Ghyczy, M.3    Theilleus, J.4    Gelie, B.5    Delattre, M.6    Corrieu, G.7    Asther, M.8
  • 13
    • 84883674268 scopus 로고    scopus 로고
    • The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase
    • COI: 1:CAS:528:DC%2BC3sXhs1Srs7%2FM, PID: 23948257
    • Carabajal M, Kellner H, Levin L, Jehmlich N, Hofrichter M, Ullrich R (2013) The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase. J Biotechnol 168:15–23
    • (2013) J Biotechnol , vol.168 , pp. 15-23
    • Carabajal, M.1    Kellner, H.2    Levin, L.3    Jehmlich, N.4    Hofrichter, M.5    Ullrich, R.6
  • 14
  • 16
    • 0036015795 scopus 로고    scopus 로고
    • 2+ regulation of peroxidase transcript levels in solid-state culture of Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD38XksVWqtbs%3D, PID: 12039783
    • 2+ regulation of peroxidase transcript levels in solid-state culture of Pleurotus ostreatus. Appl Environ Microbiol 68:3156–3158
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3156-3158
    • Cohen, R.1    Persky, L.2    Hadar, Y.3
  • 17
    • 0036222209 scopus 로고    scopus 로고
    • Biotechnological applications and potential of wood-degrading mushrooms of the genus Pleurotus
    • COI: 1:CAS:528:DC%2BD38Xjs12ktLs%3D, PID: 11956739
    • Cohen R, Persky L, Hadar Y (2002b) Biotechnological applications and potential of wood-degrading mushrooms of the genus Pleurotus. Appl Microbiol Biotechnol 58:582–594
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 582-594
    • Cohen, R.1    Persky, L.2    Hadar, Y.3
  • 18
    • 1842854104 scopus 로고    scopus 로고
    • 2+ alters peroxidase profiles and lignin degradation by the white-rot fungus Pleurotus ostreatus under different nutritional and growth conditions
    • PID: 12396142
    • 2+ alters peroxidase profiles and lignin degradation by the white-rot fungus Pleurotus ostreatus under different nutritional and growth conditions. Appl Biochem Biotechnol 102:415–429
    • (2002) Appl Biochem Biotechnol , vol.102 , pp. 415-429
    • Cohen, R.1    Persky, L.2    Hazan-Eitan, Z.3    Yarden, O.4    Hadar, Y.5
  • 19
    • 0028340896 scopus 로고
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida
    • COI: 1:CAS:528:DyaK2cXkslOqtb8%3D, PID: 16349330
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida. Appl Environ Microbiol 60:2524–2532
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2524-2532
    • Daniel, G.1    Volc, J.2    Kubátová, E.3
  • 20
    • 85007276131 scopus 로고    scopus 로고
    • Pleurotus ostreatus: an oyster mushroom with nutritional and medicinal properties
    • Deepalakshmi K, Mirunalini S (2014) Pleurotus ostreatus: an oyster mushroom with nutritional and medicinal properties. J Biochem Tech 5:718–726
    • (2014) J Biochem Tech , vol.5 , pp. 718-726
    • Deepalakshmi, K.1    Mirunalini, S.2
  • 21
    • 0032573035 scopus 로고    scopus 로고
    • Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis
    • COI: 1:CAS:528:DyaK1cXmsValtbY%3D, PID: 9790672
    • Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT (1998) Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37:15097–15105
    • (1998) Biochemistry , vol.37 , pp. 15097-15105
    • Doyle, W.A.1    Blodig, W.2    Veitch, N.C.3    Piontek, K.4    Smith, A.T.5
  • 22
    • 84859420715 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidise using isothermal titration calorimetry: insights into manganese peroxidase activation and lignin peroxidase inhibition
    • COI: 1:CAS:528:DC%2BC38XjsVGms78%3D, PID: 22586704
    • Ertan H, Siddiqui KS, Muenchhoff J, Charlton T, Cavicchioli R (2012) Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidise using isothermal titration calorimetry: insights into manganese peroxidase activation and lignin peroxidase inhibition. Biochimie 94:1221–1231
    • (2012) Biochimie , vol.94 , pp. 1221-1231
    • Ertan, H.1    Siddiqui, K.S.2    Muenchhoff, J.3    Charlton, T.4    Cavicchioli, R.5
  • 23
    • 34248326376 scopus 로고    scopus 로고
    • Identification of a new member of the dye-decolorizing peroxidase family from Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD2sXltVGqu7w%3D
    • 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
  • 24
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: an approach using the bootstrap
    • Felsenstein J (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783–791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 26
    • 84893370794 scopus 로고    scopus 로고
    • Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability
    • PID: 24387130
    • Fernández-Fueyo E, Ruiz-Dueñas FJ, Martínez MJ, Romero A, Hammel KE, Medrano FJ, Martínez AT (2014a) Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability. Biotechnol Biofuels 7:2–23
    • (2014) Biotechnol Biofuels , vol.7 , pp. 2-23
    • Fernández-Fueyo, E.1    Ruiz-Dueñas, F.J.2    Martínez, M.J.3    Romero, A.4    Hammel, K.E.5    Medrano, F.J.6    Martínez, A.T.7
  • 30
    • 84906351274 scopus 로고    scopus 로고
    • Gaskell J, Marty A, Mozuch M, Kersten PJ, Splinter S, Durant B, Sabat G, Azarpira A, Ralph J, Skyba O, Mansfield SD, Blanchette RA, Cullen D (2014) Influence of Populus genotype on gene expression by the wood decay fungus Phanerochaete chrysosporium. Appl Environ Microbiol 80:5828-5835
    • Gaskell J, Marty A, Mozuch M, Kersten PJ, Splinter S, Durant B, Sabat G, Azarpira A, Ralph J, Skyba O, Mansfield SD, Blanchette RA, Cullen D (2014) Influence of Populus genotype on gene expression by the wood decay fungus Phanerochaetechrysosporium. Appl Environ Microbiol 80:5828-5835
  • 31
    • 84871728901 scopus 로고    scopus 로고
    • Multi-catalysis reactions: new prospects and challenges of biotechnology to valorize lignin
    • COI: 1:CAS:528:DC%2BC38XhtF2rs7rK, PID: 22782247
    • Gasser CA, Hommes G, Schäffer A, Corvini PF-X (2012) Multi-catalysis reactions: new prospects and challenges of biotechnology to valorize lignin. Appl Microbiol Biotechnol 95:1115–1134
    • (2012) Appl Microbiol Biotechnol , vol.95 , pp. 1115-1134
    • Gasser, C.A.1    Hommes, G.2    Schäffer, A.3    Corvini, P.F.-X.4
  • 32
    • 0034176256 scopus 로고    scopus 로고
    • Manganese peroxidase isoenzymes produced by Pleurotus ostreatus grown on wood sawdust
    • COI: 1:CAS:528:DC%2BD3cXhvVKltbY%3D, PID: 10729203
    • Giardina P, Palmieri G, Fontanella B, Rivieccio V, Sannia G (2000) Manganese peroxidase isoenzymes produced by Pleurotus ostreatus grown on wood sawdust. Arch Biochem Biophys 376:171–179
    • (2000) Arch Biochem Biophys , vol.376 , pp. 171-179
    • Giardina, P.1    Palmieri, G.2    Fontanella, B.3    Rivieccio, V.4    Sannia, G.5
  • 33
    • 80051761213 scopus 로고    scopus 로고
    • Transformation of the recalcitrant pharmaceutical compound carbamazepine by Pleurotus ostreatus: role of cytochrome P450 monooxygenase and manganese peroxidase
    • COI: 1:CAS:528:DC%2BC3MXpt1CjtLs%3D, PID: 21744850
    • Golan-Rozen N, Chefetz B, Ben-Ari J, Geva J, Hadar Y (2011) Transformation of the recalcitrant pharmaceutical compound carbamazepine by Pleurotus ostreatus: role of cytochrome P450 monooxygenase and manganese peroxidase. Environ Sci Technol 45:6800–6805
    • (2011) Environ Sci Technol , vol.45 , pp. 6800-6805
    • Golan-Rozen, N.1    Chefetz, B.2    Ben-Ari, J.3    Geva, J.4    Hadar, Y.5
  • 35
    • 0028291491 scopus 로고
    • Anisaldehyde production and aryl-alcohol oxidase and dehydrogenase activities in ligninolytic fungi from the genus Pleurotus
    • PID: 8031078
    • Gutiérrez A, Caramelo L, Prieto A, Martínez MJ, Martínez AT (1994) Anisaldehyde production and aryl-alcohol oxidase and dehydrogenase activities in ligninolytic fungi from the genus Pleurotus. Appl Environ Microbiol 60:1783–1788
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1783-1788
    • Gutiérrez, A.1    Caramelo, L.2    Prieto, A.3    Martínez, M.J.4    Martínez, A.T.5
  • 38
    • 43849099090 scopus 로고    scopus 로고
    • Role of fungal peroxidases in biological ligninolysis
    • COI: 1:CAS:528:DC%2BD1cXmsVGlsr8%3D, PID: 18359268
    • Hammel KE, Cullen D (2008) Role of fungal peroxidases in biological ligninolysis. Curr Opin Plant Biol 11:349–355
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 349-355
    • Hammel, K.E.1    Cullen, D.2
  • 39
    • 0344734070 scopus 로고    scopus 로고
    • Transformation of industrial dyes by manganese peroxidase from Bjerkandera adusta and Pleurotus eryngii in a manganese-independent reaction
    • COI: 1:CAS:528:DyaK1cXlsVKhsro%3D, PID: 9687431
    • Heinfling A, Martínez MJ, Martínez AT, Bergbauer M, Szewzyk U (1998) Transformation of industrial dyes by manganese peroxidase from Bjerkandera adusta and Pleurotus eryngii in a manganese-independent reaction. Appl Environ Microbiol 64:2788–2793
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2788-2793
    • Heinfling, A.1    Martínez, M.J.2    Martínez, A.T.3    Bergbauer, M.4    Szewzyk, U.5
  • 40
    • 84857914934 scopus 로고    scopus 로고
    • Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation
    • PID: 22249717
    • Hernández-Ortega A, Ferreira P, Martínez AT (2012) Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation. Appl Microbiol Biotechnol 93:1395–1410
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 1395-1410
    • Hernández-Ortega, A.1    Ferreira, P.2    Martínez, A.T.3
  • 41
    • 16244401504 scopus 로고    scopus 로고
    • The two manganese peroxidases Pr–MnP2 and Pr–MnP3 of Phlebia radiata, a lignin-degrading basidiomycete, are phylogenetically and structurally divergent
    • PID: 15809005
    • Hildén K, Martínez AT, Hatakka A, Lundell T (2005) The two manganese peroxidases Pr–MnP2 and Pr–MnP3 of Phlebia radiata, a lignin-degrading basidiomycete, are phylogenetically and structurally divergent. Fungal Genet Biol 42:403–419
    • (2005) Fungal Genet Biol , vol.42 , pp. 403-419
    • Hildén, K.1    Martínez, A.T.2    Hatakka, A.3    Lundell, T.4
  • 42
    • 0037117763 scopus 로고    scopus 로고
    • Review: lignin conversion by manganese peroxidase (MnP)
    • COI: 1:CAS:528:DC%2BD38Xis1Oru7c%3D
    • Hofrichter M (2002) Review: lignin conversion by manganese peroxidase (MnP). Enzym Microb Technol 30:454–466
    • (2002) Enzym Microb Technol , vol.30 , pp. 454-466
    • Hofrichter, M.1
  • 43
    • 84896761350 scopus 로고    scopus 로고
    • Oxidations catalyzed by fungal peroxygenases
    • COI: 1:CAS:528:DC%2BC2cXntFyju78%3D
    • Hofrichter M, Ullrich R (2014) Oxidations catalyzed by fungal peroxygenases. Currt Opin Chem Biol 19:116–125
    • (2014) Currt Opin Chem Biol , vol.19 , pp. 116-125
    • Hofrichter, M.1    Ullrich, R.2
  • 45
    • 84874048873 scopus 로고    scopus 로고
    • Cytochrome P450 of wood-rotting basidiomycetes and biotechnological applications
    • COI: 1:CAS:528:DC%2BC3sXjtVCqtbo%3D, PID: 23586994
    • Ichinose H (2013) Cytochrome P450 of wood-rotting basidiomycetes and biotechnological applications. Biotechnol Appl Biochem 60(1):71–81
    • (2013) Biotechnol Appl Biochem , vol.60 , Issue.1 , pp. 71-81
    • Ichinose, H.1
  • 46
    • 0142135413 scopus 로고    scopus 로고
    • Isolation of cDNA and genome fragments the major manganese peroxidase isozyme from the white rot basidiomycete Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD3cXkslygsb0%3D
    • Irie T, Honda Y, Watanabe T, Kuwahara M (2000) Isolation of cDNA and genome fragments the major manganese peroxidase isozyme from the white rot basidiomycete Pleurotus ostreatus. J Wood Sci 46:230–233
    • (2000) J Wood Sci , vol.46 , pp. 230-233
    • Irie, T.1    Honda, Y.2    Watanabe, T.3    Kuwahara, M.4
  • 47
    • 4544239823 scopus 로고    scopus 로고
    • Production and induction of manganese peroxidase isoenzymes in a whit-rot fungus Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD2cXmsVCgtbs%3D, PID: 14767623
    • Kamitsuji H, Honda Y, Watanabe T, Kuwahara M (2004) Production and induction of manganese peroxidase isoenzymes in a whit-rot fungus Pleurotus ostreatus. Appl Microbiol Biotechnol 65:287–294
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 287-294
    • Kamitsuji, H.1    Honda, Y.2    Watanabe, T.3    Kuwahara, M.4
  • 48
    • 14844323717 scopus 로고    scopus 로고
    • Direct oxidation of polymeric substrate by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators
    • Kamitsuji H, Watanabe T, Honda Y, Kuwahara M (2005a) Direct oxidation of polymeric substrate by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators. Biochem J 385:387–393
    • (2005) Biochem J , vol.385 , pp. 387-393
    • Kamitsuji, H.1    Watanabe, T.2    Honda, Y.3    Kuwahara, M.4
  • 49
    • 11844251364 scopus 로고    scopus 로고
    • 2+ is dispensable for the production of active MnP2 by Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD2MXksFGisQ%3D%3D, PID: 15649426
    • 2+ is dispensable for the production of active MnP2 by Pleurotus ostreatus. Biochem Biophys Res Commun 327:871–876
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 871-876
    • Kamitsuji, H.1    Honda, Y.2    Watanabe, T.3    Kuwahara, M.4
  • 50
    • 0029088222 scopus 로고
    • Effect of manganese on preferential lignin degradation by Pleurotus ostreatus during solid-state fermentation
    • COI: 1:CAS:528:DyaK2MXnt1aiu70%3D, PID: 7487038
    • Kerem Z, Hadar Y (1995) Effect of manganese on preferential lignin degradation by Pleurotus ostreatus during solid-state fermentation. Appl Environ Microbiol 61:3057–3062
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3057-3062
    • Kerem, Z.1    Hadar, Y.2
  • 51
    • 84908547652 scopus 로고    scopus 로고
    • Copper radical oxidases and related extracellular oxidoreductases of wood-decay Agaricomycetes
    • PID: 24915038
    • Kersten P, Cullen D (2014) Copper radical oxidases and related extracellular oxidoreductases of wood-decay Agaricomycetes. Fungal Genet Biol. doi:10.1016/j.fgb.2014.05.011
    • (2014) Fungal Genet Biol
    • Kersten, P.1    Cullen, D.2
  • 52
    • 0023264566 scopus 로고
    • 2 production by Phanerochaete chrysosporium
    • COI: 1:CAS:528:DyaL2sXksFGnt7g%3D, PID: 3553159
    • 2 production by Phanerochaete chrysosporium. J Bacteriol 169:2195–2201
    • (1987) J Bacteriol , vol.169 , pp. 2195-2201
    • Kersten, P.J.1    Kirk, T.K.2
  • 53
    • 0029092882 scopus 로고
    • Characteristics of a newly isolated fungus, Geotrichum candidum Dec 1, which decolorizes various dyes
    • COI: 1:CAS:528:DyaK2MXmslKrtb8%3D
    • Kim SJ, Ishikawa K, Hirai M, Shoda M (1995) Characteristics of a newly isolated fungus, Geotrichum candidum Dec 1, which decolorizes various dyes. J Ferment Bioeng 79:601–607
    • (1995) J Ferment Bioeng , vol.79 , pp. 601-607
    • Kim, S.J.1    Ishikawa, K.2    Hirai, M.3    Shoda, M.4
  • 54
    • 0023478845 scopus 로고
    • Enzymatic ‘combustion’: the microbial degradation of lignin
    • COI: 1:CAS:528:DyaL2sXmtlalu7o%3D, PID: 3318677
    • Kirk TK, Farrell RL (1987) Enzymatic ‘combustion’: the microbial degradation of lignin. Annu Rev Microbiol 41:465–505
    • (1987) Annu Rev Microbiol , vol.41 , pp. 465-505
    • Kirk, T.K.1    Farrell, R.L.2
  • 55
    • 84905006343 scopus 로고    scopus 로고
    • 2+-deficiency reveals a key role for the Pleurotus ostreatus versatile peroxidase (VP4) in oxidation of aromatic compounds
    • COI: 1:CAS:528:DC%2BC2cXmsVChsrc%3D, PID: 24737058
    • 2+-deficiency reveals a key role for the Pleurotus ostreatus versatile peroxidase (VP4) in oxidation of aromatic compounds. Appl Microbiol Biotechnol 98:6795–6804
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 6795-6804
    • Knop, D.1    Ben-Ari, J.2    Salame, T.M.3    Levinson, D.4    Yarden, O.5    Hadar, Y.6
  • 56
    • 0000685943 scopus 로고
    • Arkil-aryl cleavage of phenolic β-O-4 lignin substructure model compound by Mn-peroxidase isolated from Pleurotus ostreatus
    • COI: 1:CAS:528:DyaK38XhtlWnsLw%3D
    • Kofujita H, Asada Y, Kuwahara M (1991) Arkil-aryl cleavage of phenolic β-O-4 lignin substructure model compound by Mn-peroxidase isolated from Pleurotus ostreatus. Mokuzai Gakkaishi 37:555–561
    • (1991) Mokuzai Gakkaishi , vol.37 , pp. 555-561
    • Kofujita, H.1    Asada, Y.2    Kuwahara, M.3
  • 57
    • 0000707892 scopus 로고
    • 2-dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium
    • COI: 1:CAS:528:DyaL2cXksFSmtLk%3D
    • 2-dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium. FEBS Lett 169:247–250
    • (1984) FEBS Lett , vol.169 , pp. 247-250
    • Kuwahara, M.1    Glenn, J.K.2    Morgan, M.A.3    Gold, M.H.4
  • 59
    • 84879419989 scopus 로고    scopus 로고
    • Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases
    • COI: 1:CAS:528:DC%2BC3sXpsFKjsbY%3D, PID: 23111597
    • Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, Steffen KT, Hofrichter M, Ullrich R (2013) Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases. 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    Steffen, K.T.6    Hofrichter, M.7    Ullrich, R.8
  • 60
    • 0037117789 scopus 로고    scopus 로고
    • Molecular biology and structure-function of lignin-degrading heme peroxidases
    • Martínez AT (2002) Molecular biology and structure-function of lignin-degrading heme peroxidases. Enzym Microb Technol 30:425–444
    • (2002) Enzym Microb Technol , vol.30 , pp. 425-444
    • Martínez, A.T.1
  • 61
    • 0029926079 scopus 로고    scopus 로고
    • Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii
    • PID: 8647081
    • Martínez MJ, Ruiz-Dueñas FJ, Guillén F, Martínez AT (1996a) 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
  • 63
    • 84870381055 scopus 로고    scopus 로고
    • Two oxidation sites for low redox potential substrates: a direct mutagenesis, kinetic, and, crystallographic study on Pleurotus eryngii versatile peroxidase
    • COI: 1:CAS:528:DC%2BC38XhslGjs7bO, PID: 23071108
    • Morales M, Mate MJ, Romero A, Martínez MJ, Martínez AT, Ruiz-Dueñas FJ (2012) Two oxidation sites for low redox potential substrates: a direct mutagenesis, kinetic, and, crystallographic study on Pleurotus eryngii versatile peroxidase. J Biol Chem 287:41053–41067
    • (2012) J Biol Chem , vol.287 , pp. 41053-41067
    • Morales, M.1    Mate, M.J.2    Romero, A.3    Martínez, M.J.4    Martínez, A.T.5    Ruiz-Dueñas, F.J.6
  • 65
    • 84865960579 scopus 로고    scopus 로고
    • Genetic diversity of the edible mushroom Pleurotus sp. by amplified fragment length polymorphism
    • COI: 1:CAS:528:DC%2BC38Xht1KmtL7O, PID: 22767319
    • Pawlik A, Janusz G, Koszerny J, Małek W, Rogalski J (2012) Genetic diversity of the edible mushroom Pleurotus sp. by amplified fragment length polymorphism. Curr Microbiol 65(4):438–445
    • (2012) Curr Microbiol , vol.65 , Issue.4 , pp. 438-445
    • Pawlik, A.1    Janusz, G.2    Koszerny, J.3    Małek, W.4    Rogalski, J.5
  • 66
    • 0026734519 scopus 로고
    • Roles of manganese and organic acid chelators in regulating lignin degradation and biosynthesis of peroxidase by Phanerochaete chrysosporium
    • COI: 1:CAS:528:DyaK38XlsVKqsLs%3D, PID: 1514788
    • Perez J, Jeffries TM (1992) Roles of manganese and organic acid chelators in regulating lignin degradation and biosynthesis of peroxidase by Phanerochaete chrysosporium. Appl Environ Microbiol 58:2402–2409
    • (1992) Appl Environ Microbiol , vol.58 , pp. 2402-2409
    • Perez, J.1    Jeffries, T.M.2
  • 68
    • 27644552270 scopus 로고    scopus 로고
    • Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways
    • PID: 16246366
    • Pérez-Boada M, Ruiz-Dueñas FJ, Pogni R, Basosi R, Choinowski T, Martínez MJ, Piontek K, Martínez AT (2005) Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways. J Mol Biol 354:385–402
    • (2005) J Mol Biol , vol.354 , pp. 385-402
    • Pérez-Boada, M.1    Ruiz-Dueñas, F.J.2    Pogni, R.3    Basosi, R.4    Choinowski, T.5    Martínez, M.J.6    Piontek, K.7    Martínez, A.T.8
  • 69
    • 0028084782 scopus 로고
    • Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 A resolution
    • COI: 1:CAS:528:DyaK2cXitFWnur0%3D, PID: 8112469
    • Petersen JF, Kadziola A, Larsen S (1994) Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 A resolution. FEBS Lett 339:291–296
    • (1994) FEBS Lett , vol.339 , pp. 291-296
    • Petersen, J.F.1    Kadziola, A.2    Larsen, S.3
  • 70
    • 59749098205 scopus 로고    scopus 로고
    • The Pleurotus ostreatus laccase multi-gene family: isolation and heterologous expression of new family members
    • COI: 1:CAS:528:DC%2BD1MXhtF2iu74%3D, PID: 19034452
    • Pezzella C, Autore F, Giardina P, Piscitelli A, Sannia G, Faraco V (2009) The Pleurotus ostreatus laccase multi-gene family: isolation and heterologous expression of new family members. Curr Genet 55:45–57
    • (2009) Curr Genet , vol.55 , pp. 45-57
    • Pezzella, C.1    Autore, F.2    Giardina, P.3    Piscitelli, A.4    Sannia, G.5    Faraco, V.6
  • 72
    • 0027514481 scopus 로고
    • Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution
    • COI: 1:CAS:528:DyaK3sXlsFSrsw%3D%3D, PID: 8417967
    • Piontek K, Glumoff T, Winterhalter K (1993) Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution. FEBS Lett 315:119–124
    • (1993) FEBS Lett , vol.315 , pp. 119-124
    • Piontek, K.1    Glumoff, T.2    Winterhalter, K.3
  • 73
    • 0027514159 scopus 로고
    • Crystallographic refinement of lignin peroxidase at 2 A
    • COI: 1:CAS:528:DyaK3sXitVynsb4%3D, PID: 8440725
    • Poulos TL, Edwards SL, Wariishi H, Gold MH (1993) Crystallographic refinement of lignin peroxidase at 2 A. J Biol Chem 268:4429–4440
    • (1993) J Biol Chem , vol.268 , pp. 4429-4440
    • Poulos, T.L.1    Edwards, S.L.2    Wariishi, H.3    Gold, M.H.4
  • 74
    • 84901642308 scopus 로고    scopus 로고
    • Enzymes as useful tools for environmental purposes
    • COI: 1:CAS:528:DC%2BC2cXlt1Wntw%3D%3D, PID: 24411841
    • Rao MA, Scelza R, Acevedo F, Diez MC, Gianfreda L (2014) Enzymes as useful tools for environmental purposes. Chemosphere 107:145–162
    • (2014) Chemosphere , vol.107 , pp. 145-162
    • Rao, M.A.1    Scelza, R.2    Acevedo, F.3    Diez, M.C.4    Gianfreda, L.5
  • 77
    • 33846173370 scopus 로고    scopus 로고
    • Manganese oxidation site in Pleurotus eryngii versatile peroxidase: a site-directed mutagenesis, kinetic, and crystallographic study
    • PID: 17198376
    • Ruiz-Dueñas FJ, Morales M, Pérez-Boada M, Choinowski T, Martínez MJ, Piontek K, Martínez AT (2007) Manganese oxidation site in Pleurotus eryngii versatile peroxidase: a site-directed mutagenesis, kinetic, and crystallographic study. Biochemistry 46:66–77
    • (2007) Biochemistry , vol.46 , pp. 66-77
    • Ruiz-Dueñas, F.J.1    Morales, M.2    Pérez-Boada, M.3    Choinowski, T.4    Martínez, M.J.5    Piontek, K.6    Martínez, A.T.7
  • 79
    • 80955142808 scopus 로고    scopus 로고
    • Pleurotus ostreatus heme peroxidases: an in silico analysis from the genome sequence to the enzyme molecular structure
    • Ruiz-Dueñas FJ, Fernández E, Martínez MJ, Martínez AT (2011) Pleurotus ostreatus heme peroxidases: an in silico analysis from the genome sequence to the enzyme molecular structure. C R Biolog 334:795–805
    • (2011) C R Biolog , vol.334 , pp. 795-805
    • Ruiz-Dueñas, F.J.1    Fernández, E.2    Martínez, M.J.3    Martínez, A.T.4
  • 81
    • 0027180723 scopus 로고
    • Extracellular enzyme production and synthetic lignin mineralization by Ceriporiopsis subvermispora
    • PID: 16348955
    • Rüttimann-Johnson C, Salas L, Vicuna R, Kirk TK (1993) Extracellular enzyme production and synthetic lignin mineralization by Ceriporiopsis subvermispora. Appl Environ Microbiol 59:1792–1797
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1792-1797
    • Rüttimann-Johnson, C.1    Salas, L.2    Vicuna, R.3    Kirk, T.K.4
  • 82
    • 77953580652 scopus 로고    scopus 로고
    • Pleurotus ostreatus manganese-dependent peroxidase silencing impairs decolourization of Orange II
    • COI: 1:CAS:528:DC%2BC3cXlslajsbo%3D, PID: 21255310
    • Salame TM, Yarden O, Hadar Y (2010) Pleurotus ostreatus manganese-dependent peroxidase silencing impairs decolourization of Orange II. Microb Biotechnol 3:93–106
    • (2010) Microb Biotechnol , vol.3 , pp. 93-106
    • Salame, T.M.1    Yarden, O.2    Hadar, Y.3
  • 83
    • 79251597602 scopus 로고    scopus 로고
    • RNAi as a potential tool for biotechnological applications in fungi
    • COI: 1:CAS:528:DC%2BC3MXnsVWksQ%3D%3D, PID: 20953869
    • Salame TM, Ziv C, Hadar Y, Yarden O (2011) RNAi as a potential tool for biotechnological applications in fungi. Appl Microbiol Biotechnol 89:501–512
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 501-512
    • Salame, T.M.1    Ziv, C.2    Hadar, Y.3    Yarden, O.4
  • 84
    • 84866145027 scopus 로고    scopus 로고
    • Predominance of a versatile-peroxidase-encoding gene, mnp4, as demonstrated by gene replacement via a gene targeting system for Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BC38XhtFWjsLrN, PID: 22636004
    • Salame TM, Knop D, Tal D, Levinson D, Yarden O, Hadar Y (2012a) Predominance of a versatile-peroxidase-encoding gene, mnp4, as demonstrated by gene replacement via a gene targeting system for Pleurotus ostreatus. Appl Environ Microbiol 78:5341–5352
    • (2012) Appl Environ Microbiol , vol.78 , pp. 5341-5352
    • Salame, T.M.1    Knop, D.2    Tal, D.3    Levinson, D.4    Yarden, O.5    Hadar, Y.6
  • 87
    • 84891627113 scopus 로고    scopus 로고
    • Inactivation of a Pleurotus ostreatus versatile peroxidase-encoding gene (mnp2) results in reduced lignin degradation
    • COI: 1:CAS:528:DC%2BC2cXlsFymtA%3D%3D, PID: 24119015
    • Salame TM, Knop D, Levinson D, Mabjeesh SJ, Yarden O, Hadar Y (2014) Inactivation of a Pleurotus ostreatus versatile peroxidase-encoding gene (mnp2) results in reduced lignin degradation. Environ Microbiol 16:265–277
    • (2014) Environ Microbiol , vol.16 , pp. 265-277
    • Salame, T.M.1    Knop, D.2    Levinson, D.3    Mabjeesh, S.J.4    Yarden, O.5    Hadar, Y.6
  • 89
    • 76649111369 scopus 로고    scopus 로고
    • Cultivation of Pleurotus ostreatus and other edible mushrooms
    • COI: 1:CAS:528:DC%2BC3cXmvVKjtQ%3D%3D, PID: 19956947
    • Sanchez C (2010) Cultivation of Pleurotus ostreatus and other edible mushrooms. Appl Microbiol Biotechnol 85:1321–1337
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1321-1337
    • Sanchez, C.1
  • 90
    • 0030939022 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus
    • COI: 1:CAS:528:DyaK2sXisVenu7o%3D
    • Sarkar S, Martínez AT, Martínez MJ (1997) Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus. BBA-Protein Struct Mol 1339:23–30
    • (1997) BBA-Protein Struct Mol , vol.1339 , pp. 23-30
    • Sarkar, S.1    Martínez, A.T.2    Martínez, M.J.3
  • 91
    • 84899659938 scopus 로고    scopus 로고
    • Induction, characterization, and heterologous expression of a carotenoid degrading versatile peroxidase from Pleurotus sapidus
    • Schüttmann I, Bouws H, Szweda RT, Suckow M, Czermak P, Zorn H (2014) Induction, characterization, and heterologous expression of a carotenoid degrading versatile peroxidase from Pleurotus sapidus. J Mol Catal B Enzym 103:79–84
    • (2014) J Mol Catal B Enzym , vol.103 , pp. 79-84
    • Schüttmann, I.1    Bouws, H.2    Szweda, R.T.3    Suckow, M.4    Czermak, P.5    Zorn, H.6
  • 92
    • 0242667669 scopus 로고
    • Biological chlorination. III. beta-Ketoadipate chlorinase: a soluble enzyme system
    • COI: 1:CAS:528:DyaF3cXhtFyjtw%3D%3D, PID: 14445652
    • Shaw PD, Hager LP (1959) Biological chlorination. III. beta-Ketoadipate chlorinase: a soluble enzyme system. J Biol Chem 234:2565–2569
    • (1959) J Biol Chem , vol.234 , pp. 2565-2569
    • Shaw, P.D.1    Hager, L.P.2
  • 93
    • 84893841912 scopus 로고    scopus 로고
    • The commercially cultivated edible oyster mushrooms Pleurotus sajor-caju and P. pulmonarius are two separated species, similar in morphology but reproductively isolated
    • COI: 1:CAS:528:DC%2BC38Xhs12gsbjL
    • Shnyreva AA, Sivolapova AB, Shnyreva AV (2012) The commercially cultivated edible oyster mushrooms Pleurotus sajor-caju and P. pulmonarius are two separated species, similar in morphology but reproductively isolated. Russ J Genet 48:1080–1088
    • (2012) Russ J Genet , vol.48 , pp. 1080-1088
    • Shnyreva, A.A.1    Sivolapova, A.B.2    Shnyreva, A.V.3
  • 94
    • 84896700846 scopus 로고    scopus 로고
    • Biotechnological applications of wood-rotting fungi: a review
    • COI: 1:CAS:528:DC%2BC2cXisFWlsbg%3D
    • Singh AP, Singh T (2014) Biotechnological applications of wood-rotting fungi: a review. Biomass Bioenergy 62:198–206
    • (2014) Biomass Bioenergy , vol.62 , pp. 198-206
    • Singh, A.P.1    Singh, T.2
  • 95
    • 0032042908 scopus 로고    scopus 로고
    • Substrate binding and catalysis in heme peroxidases
    • COI: 1:CAS:528:DyaK1cXjs1OltLg%3D, PID: 9667928
    • Smith AT, Veitch NC (1998) Substrate binding and catalysis in heme peroxidases. Curr Opin Chem Biol 2:269–278
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 269-278
    • Smith, A.T.1    Veitch, N.C.2
  • 96
    • 70349522119 scopus 로고    scopus 로고
    • Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase
    • COI: 1:CAS:528:DC%2BD1MXht1OjsbjJ, PID: 19805263
    • Smith AT, Doyle WA, Dorlet P, Ivancich A (2009) Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase. Proc Natl Acad Sci U S A 106:16084–16089
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16084-16089
    • Smith, A.T.1    Doyle, W.A.2    Dorlet, P.3    Ivancich, A.4
  • 98
    • 34248158096 scopus 로고    scopus 로고
    • Basidiomycetes laccase and manganese peroxidase activity in submerged fermentation of food industry wastes
    • COI: 1:CAS:528:DC%2BD2sXlt1aksrs%3D
    • Songulashvili G, Elisashvili V, Wasser SP, Nevo E, Hadar Y (2007) Basidiomycetes laccase and manganese peroxidase activity in submerged fermentation of food industry wastes. Enzym Microb Technol 41:57–61
    • (2007) Enzym Microb Technol , vol.41 , pp. 57-61
    • Songulashvili, G.1    Elisashvili, V.2    Wasser, S.P.3    Nevo, E.4    Hadar, Y.5
  • 99
    • 27844449531 scopus 로고    scopus 로고
    • Effect of different carbon and nitrogen sources on laccase and peroxidases production by selected Pleurotus species
    • Stajić M, Persky L, Friesem D, Hadar Y, Wasser SP, Eviatar N, Vukojevi J (2006) Effect of different carbon and nitrogen sources on laccase and peroxidases production by selected Pleurotus species. Enzym Microbiol Technol 38:65–73
    • (2006) Enzym Microbiol Technol , vol.38 , pp. 65-73
    • Stajić, M.1    Persky, L.2    Friesem, D.3    Hadar, Y.4    Wasser, S.P.5    Eviatar, N.6    Vukojevi, J.7
  • 100
    • 70349246899 scopus 로고    scopus 로고
    • Biology of Pleurotus eryngii and role in biotechnological processes: a review
    • PID: 19514895
    • Stajić M, Vukojević J, Duletić-Laušević S (2009) Biology of Pleurotus eryngii and role in biotechnological processes: a review. Crit Rev Biotechnol 29:55–66
    • (2009) Crit Rev Biotechnol , vol.29 , pp. 55-66
    • Stajić, M.1    Vukojević, J.2    Duletić-Laušević, S.3
  • 101
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • COI: 1:CAS:528:DC%2BD1MXksFGhtb0%3D, PID: 19099183
    • 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
  • 102
    • 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
    • COI: 1:CAS:528:DC%2BD2sXhsVSgtrfI, PID: 17928290
    • 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
  • 103
    • 0028587337 scopus 로고
    • The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution
    • COI: 1:CAS:528:DyaK2cXmvFGqtrk%3D, PID: 7806497
    • Sundaramoorthy M, Kishi K, Gold MH, Poulos TL (1994) The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J Biol Chem 269:32759–32767
    • (1994) J Biol Chem , vol.269 , pp. 32759-32767
    • Sundaramoorthy, M.1    Kishi, K.2    Gold, M.H.3    Poulos, T.L.4
  • 104
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 10:2731–2739
    • (2011) Mol Biol Evol , vol.10 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 105
    • 84896816799 scopus 로고    scopus 로고
    • Characterization of combined cross-linked enzyme aggregates from laccase, versatile peroxidase and glucose oxidase, and their utilization for the elimination of pharmaceuticals
    • COI: 1:CAS:528:DC%2BC2cXmtVahurY%3D, PID: 24589758
    • Touahar IE, Haroune I, Ba S, Bellenger JP, Cabana H (2014) Characterization of combined cross-linked enzyme aggregates from laccase, versatile peroxidase and glucose oxidase, and their utilization for the elimination of pharmaceuticals. Sci Total Environ 481:90–99
    • (2014) Sci Total Environ , vol.481 , pp. 90-99
    • Touahar, I.E.1    Haroune, I.2    Ba, S.3    Bellenger, J.P.4    Cabana, H.5
  • 106
    • 33750322286 scopus 로고    scopus 로고
    • Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD28XhtFeqt7fI, PID: 16820241
    • Tsukihara T, Honda Y, Watanabe T, Watanabe T (2006a) Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus. J Biotechnol 126:431–439
    • (2006) J Biotechnol , vol.126 , pp. 431-439
    • Tsukihara, T.1    Honda, Y.2    Watanabe, T.3    Watanabe, T.4
  • 107
    • 33744503666 scopus 로고    scopus 로고
    • Molecular breeding of white rot fungus Pleurotus ostreatus by homologous expression of its versatile peroxidase MnP2
    • COI: 1:CAS:528:DC%2BD28XltFWlur0%3D, PID: 16163536
    • Tsukihara T, Honda Y, Watanabe T, Watanabe T (2006b) Molecular breeding of white rot fungus Pleurotus ostreatus by homologous expression of its versatile peroxidase MnP2. Appl Microbiol Biotechnol 71:114–120
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 114-120
    • Tsukihara, T.1    Honda, Y.2    Watanabe, T.3    Watanabe, T.4
  • 108
    • 43049143502 scopus 로고    scopus 로고
    • Mechanism for oxidation of high-molecular-weight substrates by a fungal versatile peroxidase, MnP2
    • COI: 1:CAS:528:DC%2BD1cXlslChsr0%3D, PID: 18326680
    • Tsukihara T, Honda Y, Sakai R, Watanabe T (2008) Mechanism for oxidation of high-molecular-weight substrates by a fungal versatile peroxidase, MnP2. Appl Environ Microbiol 74:2873–2881
    • (2008) Appl Environ Microbiol , vol.74 , pp. 2873-2881
    • Tsukihara, T.1    Honda, Y.2    Sakai, R.3    Watanabe, T.4
  • 109
    • 4143095883 scopus 로고    scopus 로고
    • Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes
    • COI: 1:CAS:528:DC%2BD2cXms1eltLk%3D, PID: 15294788
    • Ullrich R, Nüske J, Scheibner K, Spantzel J, Hofrichter M (2004) Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes. Appl Environ Microbiol 70:4575–4581
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4575-4581
    • Ullrich, R.1    Nüske, J.2    Scheibner, K.3    Spantzel, J.4    Hofrichter, M.5
  • 110
    • 84906951526 scopus 로고    scopus 로고
    • Method for the stabilization and immobilization of enzymatic extracts and its application to the decolorization of textile dyes
    • PID: 24930109
    • Vásquez C, Anderson D, Oyarzún M, Carvajal A, Palma C (2014) Method for the stabilization and immobilization of enzymatic extracts and its application to the decolorization of textile dyes. Biotechnol Lett 36:1999–2010
    • (2014) Biotechnol Lett , vol.36 , pp. 1999-2010
    • Vásquez, C.1    Anderson, D.2    Oyarzún, M.3    Carvajal, A.4    Palma, C.5
  • 111
    • 0027380951 scopus 로고
    • Intersterility groups in the Pleurotus ostreatus complex from the continental United States and adjacent Canada
    • Vilgalys R, Smith A, Sun BL, Miller OK Jr (1993) Intersterility groups in the Pleurotus ostreatus complex from the continental United States and adjacent Canada. Can J Bot 71:113–128
    • (1993) Can J Bot , vol.71 , pp. 113-128
    • Vilgalys, R.1    Smith, A.2    Sun, B.L.3    Miller, O.K.4
  • 112
    • 0025002841 scopus 로고
    • Lignin peroxidase compound III. Mechanism of formation and decomposition
    • COI: 1:CAS:528:DyaK3cXhsFChtbo%3D, PID: 2298739
    • Wariishi H, Gold MH (1990) Lignin peroxidase compound III. Mechanism of formation and decomposition. J Biol Chem 265:2070–2077
    • (1990) J Biol Chem , vol.265 , pp. 2070-2077
    • Wariishi, H.1    Gold, M.H.2
  • 114
    • 84888884208 scopus 로고    scopus 로고
    • The white-rot fungus Pleurotus ostreatus transformant overproduced intracellular cAMP and laccase
    • COI: 1:CAS:528:DC%2BC3sXhvFWjs7nO, PID: 24200784
    • Yao Y, Sakamoto T, Honda Y, Kagotani Y, Izumitsu K, Suzuki K, Irie T (2013) The white-rot fungus Pleurotus ostreatus transformant overproduced intracellular cAMP and laccase. Biosci Biotechnol Biochem 77:2309–2311
    • (2013) Biosci Biotechnol Biochem , vol.77 , pp. 2309-2311
    • Yao, Y.1    Sakamoto, T.2    Honda, Y.3    Kagotani, Y.4    Izumitsu, K.5    Suzuki, K.6    Irie, T.7
  • 115
    • 0000531838 scopus 로고    scopus 로고
    • A pluralistic approach in the study of Pleurotus species with emphasis on compatibility and physiology of the European morphotaxa
    • Zervakis G, Balis C (1996) A pluralistic approach in the study of Pleurotus species with emphasis on compatibility and physiology of the European morphotaxa. Mycol Res 100:717–731
    • (1996) Mycol Res , vol.100 , pp. 717-731
    • Zervakis, G.1    Balis, C.2
  • 116
    • 34447287604 scopus 로고    scopus 로고
    • Study of biodegradation products from azo dyes in fungal degradation by capillary electrophoresis/electrospray mass spectrometry
    • COI: 1:CAS:528:DC%2BD2sXnslGgtb4%3D, PID: 17126346
    • Zhao X, Lu Y, Phillips DR, Hwang H-M, Hardin IR (2007) Study of biodegradation products from azo dyes in fungal degradation by capillary electrophoresis/electrospray mass spectrometry. J Chromatogr A 1159:217–224
    • (2007) J Chromatogr A , vol.1159 , pp. 217-224
    • Zhao, X.1    Lu, Y.2    Phillips, D.R.3    Hwang, H.-M.4    Hardin, I.R.5
  • 117
    • 28944455667 scopus 로고    scopus 로고
    • The secretome of Pleurotus sapidus
    • COI: 1:CAS:528:DC%2BD28Xktlemsg%3D%3D, PID: 16281184
    • Zorn H, Peters T, Nimtz M, Berger RG (2005) The secretome of Pleurotus sapidus. Proteomics 5:4832–4838
    • (2005) Proteomics , vol.5 , pp. 4832-4838
    • Zorn, H.1    Peters, T.2    Nimtz, M.3    Berger, R.G.4


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