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Volumn 240, Issue 6, 2014, Pages 1225-1236

First laccase in green algae: purification and characterization of an extracellular phenol oxidase from Tetracystis aeria

Author keywords

Algae; Dyes; Laccase; Laccase mediator system; Phenol oxidase; Quaternary structure

Indexed keywords

ALGAE; CHLOROPHYTA; EMBRYOPHYTA; FUNGI; TETRACYSTIS AERIA;

EID: 84919884396     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-014-2144-9     Document Type: Article
Times cited : (78)

References (61)
  • 1
    • 33645027271 scopus 로고    scopus 로고
    • Fungal laccases—occurrence and properties
    • COI: 1:CAS:528:DC%2BD28Xit1Sjs74%3D, PID: 16472305
    • Baldrian P (2006) Fungal laccases—occurrence and properties. FEMS Microbiol Rev 30:215–242. doi:10.1111/j.1574-4976.2005.00010.x
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 215-242
    • Baldrian, P.1
  • 3
    • 84870841026 scopus 로고    scopus 로고
    • Cellulose degradation and assimilation by the unicellular phototrophic eukaryote Chlamydomonas reinhardtii
    • PID: 23169055
    • Blifernez-Klassen O, Klassen V, Doebbe A, Kersting K, Grimm P, Wobbe L, Kruse O (2012) Cellulose degradation and assimilation by the unicellular phototrophic eukaryote Chlamydomonas reinhardtii. Nat Commun 3:1214. doi:10.1038/ncomms2210
    • (2012) Nat Commun , vol.3 , pp. 1214
    • Blifernez-Klassen, O.1    Klassen, V.2    Doebbe, A.3    Kersting, K.4    Grimm, P.5    Wobbe, L.6    Kruse, O.7
  • 4
    • 0023102759 scopus 로고
    • A kinetic study of the melanization pathway between l-tyrosine and dopachrome
    • COI: 1:CAS:528:DyaL2sXhtlGrtrY%3D, PID: 3101741
    • Cabanes J, García-Cánovas F, Lozano JA, García-Carmona F (1987) A kinetic study of the melanization pathway between l-tyrosine and dopachrome. Biochim Biophys Acta 923:187–195. doi:10.1016/0304-4165(87)90003-1
    • (1987) Biochim Biophys Acta , vol.923 , pp. 187-195
    • Cabanes, J.1    García-Cánovas, F.2    Lozano, J.A.3    García-Carmona, F.4
  • 5
    • 17444419429 scopus 로고    scopus 로고
    • Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes
    • COI: 1:CAS:528:DC%2BD2MXjsVOqt7s%3D
    • Camarero S, Ibarra D, Martínez MJ, Martínez ÁT (2005) Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes. Appl Environ Microb 71:1775–1784. doi:10.1128/AEM.71.4.1775-1784.2005
    • (2005) Appl Environ Microb , vol.71 , pp. 1775-1784
    • Camarero, S.1    Ibarra, D.2    Martínez, M.J.3    Martínez, Á.T.4
  • 6
    • 82955233021 scopus 로고    scopus 로고
    • Engineered tobacco and microalgae secreting the fungal laccase POXA1b reduce phenol content in olive oil mill wastewater
    • COI: 1:CAS:528:DC%2BC3MXhsFegur7E
    • Chiaiese P, Palomba F, Tatino F, Lanzillo C, Pinto G, Pollio A, Filippone E (2011) Engineered tobacco and microalgae secreting the fungal laccase POXA1b reduce phenol content in olive oil mill wastewater. Enzyme Microb Tech 49:540–546. doi:10.1016/j.enzmictec.2011.06.002
    • (2011) Enzyme Microb Tech , vol.49 , pp. 540-546
    • Chiaiese, P.1    Palomba, F.2    Tatino, F.3    Lanzillo, C.4    Pinto, G.5    Pollio, A.6    Filippone, E.7
  • 7
    • 0016425962 scopus 로고
    • The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen
    • COI: 1:STN:280:DyaE28%2FmtFGjtg%3D%3D, PID: 1191252
    • Childs RE, Bardsley WG (1975) The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen. Biochem J 145:93–103
    • (1975) Biochem J , vol.145 , pp. 93-103
    • Childs, R.E.1    Bardsley, W.G.2
  • 8
    • 1242322589 scopus 로고    scopus 로고
    • Laccases: structure, reactions, distribution
    • COI: 1:CAS:528:DC%2BD2cXptV2ltA%3D%3D, PID: 15036303
    • Claus H (2004) Laccases: structure, reactions, distribution. Micron 35:93–96. doi:10.1016/j.micron.2003.10.029
    • (2004) Micron , vol.35 , pp. 93-96
    • Claus, H.1
  • 9
    • 0030945592 scopus 로고    scopus 로고
    • Purification and characterization of Fet3 protein, a yeast homologue of ceruloplasmin
    • PID: 9162052
    • De Silva D, Davis-Kaplan S, Fergestad J, Kaplan J (1997) Purification and characterization of Fet3 protein, a yeast homologue of ceruloplasmin. J Biol Chem 272:14208–14213. doi:10.1074/jbc.272.22.14208
    • (1997) J Biol Chem , vol.272 , pp. 14208-14213
    • De Silva, D.1    Davis-Kaplan, S.2    Fergestad, J.3    Kaplan, J.4
  • 10
    • 0344735710 scopus 로고
    • Laccase and the deposition of lignin in vascular plants
    • COI: 1:CAS:528:DyaK2cXhvVOiurk%3D
    • Dean JF, Eriksson KEL (1994) Laccase and the deposition of lignin in vascular plants. Holzforschung 48:21–33. doi:10.1515/hfsg.1994.48.s1.21
    • (1994) Holzforschung , vol.48 , pp. 21-33
    • Dean, J.F.1    Eriksson, K.E.L.2
  • 11
    • 0033920889 scopus 로고    scopus 로고
    • Purification and characterization of the first bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum
    • COI: 1:CAS:528:DC%2BD3cXltVCrur8%3D
    • Diamantidis G, Effosse A, Potier P, Bally R (2000) Purification and characterization of the first bacterial laccase in the rhizospheric bacterium Azospirillum lipoferum. Soil Biol Biochem 32:919–927. doi:10.1016/S0038-0717(99)00221-7
    • (2000) Soil Biol Biochem , vol.32 , pp. 919-927
    • Diamantidis, G.1    Effosse, A.2    Potier, P.3    Bally, R.4
  • 12
    • 38049120256 scopus 로고    scopus 로고
    • Heterologous expression of heterodimeric laccase from Pleurotus ostreatus in Kluyveromyces lactis
    • COI: 1:CAS:528:DC%2BD1cXhsFSjtrc%3D, PID: 18043917
    • Faraco V, Ercole C, Festa G, Giardina P, Piscitelli A, Sannia G (2008) Heterologous expression of heterodimeric laccase from Pleurotus ostreatus in Kluyveromyces lactis. Appl Microbiol Biotechnol 77:1329–1335. doi:10.1007/s00253-007-1265-5
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 1329-1335
    • Faraco, V.1    Ercole, C.2    Festa, G.3    Giardina, P.4    Piscitelli, A.5    Sannia, G.6
  • 13
    • 84905393613 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the small subunit of the heterodimeric laccase POXA3b from Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BC2cXhsVCis7w%3D
    • Ferraroni M, Scozzafava A, Ullah S, Tron T, Piscitelli A, Sannia G (2014) Crystallization and preliminary X-ray crystallographic analysis of the small subunit of the heterodimeric laccase POXA3b from Pleurotus ostreatus. Acta Cryst F 70:76–79. doi:10.1107/S2053230X13032810
    • (2014) Acta Cryst F , vol.70 , pp. 76-79
    • Ferraroni, M.1    Scozzafava, A.2    Ullah, S.3    Tron, T.4    Piscitelli, A.5    Sannia, G.6
  • 14
    • 76849084273 scopus 로고    scopus 로고
    • Kinetic and biochemical properties of high and low redox potential laccases from fungal and plant origin
    • COI: 1:CAS:528:DC%2BC3cXis1Sjsb0%3D
    • Frasconi M, Favero G, Boer H, Koivula A, Mazzei F (2010) Kinetic and biochemical properties of high and low redox potential laccases from fungal and plant origin. BBA Proteins Proteom 1804:899–908. doi:10.1016/j.bbapap.2009.12.018
    • (2010) BBA Proteins Proteom , vol.1804 , pp. 899-908
    • Frasconi, M.1    Favero, G.2    Boer, H.3    Koivula, A.4    Mazzei, F.5
  • 15
    • 20444424950 scopus 로고    scopus 로고
    • Tissue localization of cytokinin dehydrogenase in maize: possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction
    • COI: 1:CAS:528:DC%2BD2MXkvVWqurw%3D, PID: 15746157
    • Galuszka P, Frébortová J, Luhová L, Bilyeu KD, English JT, Frébort I (2005) Tissue localization of cytokinin dehydrogenase in maize: possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction. Plant Cell Physiol 46:716–728. doi:10.1093/pcp/pci074
    • (2005) Plant Cell Physiol , vol.46 , pp. 716-728
    • Galuszka, P.1    Frébortová, J.2    Luhová, L.3    Bilyeu, K.D.4    English, J.T.5    Frébort, I.6
  • 16
    • 80053573337 scopus 로고    scopus 로고
    • The biotransformation, biodegradation, and bioremediation of organic compounds by microalgae
    • COI: 1:CAS:528:DC%2BC3MXhtl2rurvI
    • Ghasemi Y, Rasoul-Amini S, Fotooh-Abadi E (2011) The biotransformation, biodegradation, and bioremediation of organic compounds by microalgae. J Phycol 47:969–980. doi:10.1111/j.1529-8817.2011.01051.x
    • (2011) J Phycol , vol.47 , pp. 969-980
    • Ghasemi, Y.1    Rasoul-Amini, S.2    Fotooh-Abadi, E.3
  • 17
    • 34250870755 scopus 로고    scopus 로고
    • Structural characterization of heterodimeric laccases from Pleurotus ostreatus
    • COI: 1:CAS:528:DC%2BD2sXmvVKntL0%3D, PID: 17429621
    • Giardina P, Autore F, Faraco V, Festa G, Palmieri G, Piscitelli A, Sannia G (2007) Structural characterization of heterodimeric laccases from Pleurotus ostreatus. Appl Microbiol Biotechnol 75:1293–1300. doi:10.1007/s00253-007-0954-4
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 1293-1300
    • Giardina, P.1    Autore, F.2    Faraco, V.3    Festa, G.4    Palmieri, G.5    Piscitelli, A.6    Sannia, G.7
  • 19
    • 0000910972 scopus 로고
    • Syringaldazine, an effective reagent for detecting laccase and peroxidase in fungi
    • COI: 1:CAS:528:DyaE3sXktl2qt7Y%3D
    • Harkin JM, Obst JR (1973) Syringaldazine, an effective reagent for detecting laccase and peroxidase in fungi. Experientia 29:381–387. doi:10.1007/BF01926734
    • (1973) Experientia , vol.29 , pp. 381-387
    • Harkin, J.M.1    Obst, J.R.2
  • 20
    • 0016067464 scopus 로고
    • Use of syringaldazine for detection of laccase in sporophores of wood rotting fungi
    • COI: 1:CAS:528:DyaE2MXhtlGltw%3D%3D, PID: 4210374
    • Harkin JM, Larsen MJ, Obst JR (1974) Use of syringaldazine for detection of laccase in sporophores of wood rotting fungi. Mycologia 66:469–476
    • (1974) Mycologia , vol.66 , pp. 469-476
    • Harkin, J.M.1    Larsen, M.J.2    Obst, J.R.3
  • 21
    • 1642444735 scopus 로고    scopus 로고
    • Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera
    • COI: 1:CAS:528:DC%2BD2cXltFWlsw%3D%3D
    • Hoopes JT, Dean JF (2004) Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera. Plant Physiol Bioch 42:27–33. doi:10.1016/j.plaphy.2003.10.011
    • (2004) Plant Physiol Bioch , vol.42 , pp. 27-33
    • Hoopes, J.T.1    Dean, J.F.2
  • 22
    • 0026615449 scopus 로고
    • Degradation of azo dyes by algae
    • COI: 1:STN:280:DC%2BD2c7psFCqtw%3D%3D, PID: 15092015
    • Jinqi L, Houtian L (1992) Degradation of azo dyes by algae. Environ Pollut 75:273–278. doi:10.1016/0269-7491(92)90127-V
    • (1992) Environ Pollut , vol.75 , pp. 273-278
    • Jinqi, L.1    Houtian, L.2
  • 23
    • 1842368595 scopus 로고
    • Laccase in Anacardiaceae
    • COI: 1:CAS:528:DyaE1cXls1Sjur0%3D
    • Joel DM, Marbach I, Mayer AM (1978) Laccase in Anacardiaceae. Phytochemistry 17:796–797. doi:10.1016/S0031-9422(00)94231-6
    • (1978) Phytochemistry , vol.17 , pp. 796-797
    • Joel, D.M.1    Marbach, I.2    Mayer, A.M.3
  • 24
    • 80755132287 scopus 로고    scopus 로고
    • Potential of Gonium spp. in synthetic reactive dye removal, possible role of laccases and stimulation by triacontanol hormone
    • Kılıç NK, Karatay SE, Duygu E, Dönmez G (2011) Potential of Gonium spp. in synthetic reactive dye removal, possible role of laccases and stimulation by triacontanol hormone. Water Air Soil Pollut 222:297–303. doi:10.1007/s11270-011-0824-7
    • (2011) Water Air Soil Pollut , vol.222 , pp. 297-303
    • Kılıç, N.K.1    Karatay, S.E.2    Duygu, E.3    Dönmez, G.4
  • 25
    • 0036777691 scopus 로고    scopus 로고
    • Copper-dependent iron assimilation pathway in the model photosynthetic eukaryote Chlamydomonas reinhardtii
    • PID: 12455693
    • La Fontaine S, Quinn JM, Nakamoto SS, Page MD, Göhre V, Moseley JL, Kropat J, Merchant S (2002) Copper-dependent iron assimilation pathway in the model photosynthetic eukaryote Chlamydomonas reinhardtii. Eukaryot Cell 1:736–757. doi:10.1128/EC.1.5.736-757.2002
    • (2002) Eukaryot Cell , vol.1 , pp. 736-757
    • La Fontaine, S.1    Quinn, J.M.2    Nakamoto, S.S.3    Page, M.D.4    Göhre, V.5    Moseley, J.L.6    Kropat, J.7    Merchant, S.8
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D, PID: 5432063
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 83655193550 scopus 로고    scopus 로고
    • Dimeric and monomeric laccases of soil-stabilizing lichen Solorina crocea: purification, properties and reactions with humic acids
    • COI: 1:CAS:528:DC%2BC3MXhs1CrtLvO
    • Lisov A, Zavarzina A, Zavarzin A, Demin V, Leontievsky A (2012) Dimeric and monomeric laccases of soil-stabilizing lichen Solorina crocea: purification, properties and reactions with humic acids. Soil Biol Biochem 45:161–167. doi:10.1016/j.soilbio.2011.11.004
    • (2012) Soil Biol Biochem , vol.45 , pp. 161-167
    • Lisov, A.1    Zavarzina, A.2    Zavarzin, A.3    Demin, V.4    Leontievsky, A.5
  • 29
    • 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 (1996) Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii. Eur J Biochem 237:424–432. doi:10.1111/j.1432-1033.1996.0424k.x
    • (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
  • 30
    • 22444432126 scopus 로고    scopus 로고
    • Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana
    • COI: 1:CAS:528:DC%2BD2MXmtVymsbk%3D, PID: 15940465
    • McCaig BC, Meagher RB, Dean JF (2005) Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana. Planta 221:619–636. doi:10.1007/s00425-004-1472-6
    • (2005) Planta , vol.221 , pp. 619-636
    • McCaig, B.C.1    Meagher, R.B.2    Dean, J.F.3
  • 31
    • 77953904715 scopus 로고    scopus 로고
    • Decolorization of simulated textile dye baths by crude laccases from Trametes hirsuta and Cerrena unicolor
    • COI: 1:CAS:528:DC%2BC3cXpsVKmsrg%3D
    • Moilanen U, Osma JF, Winquist E, Leisola M, Couto SR (2010) Decolorization of simulated textile dye baths by crude laccases from Trametes hirsuta and Cerrena unicolor. Eng Life Sci 10:242–247. doi:10.1002/elsc.200900095
    • (2010) Eng Life Sci , vol.10 , pp. 242-247
    • Moilanen, U.1    Osma, J.F.2    Winquist, E.3    Leisola, M.4    Couto, S.R.5
  • 33
    • 34548676867 scopus 로고    scopus 로고
    • Laccase-mediator systems and their applications: a review
    • COI: 1:CAS:528:DC%2BD2sXhtVChurzE
    • Morozova OV, Shumakovich GP, Shleev SV, Yaropolov YI (2007b) Laccase-mediator systems and their applications: a review. Appl Biochem Micro 43:523–535. doi:10.1134/S0003683807050055
    • (2007) Appl Biochem Micro , vol.43 , pp. 523-535
    • Morozova, O.V.1    Shumakovich, G.P.2    Shleev, S.V.3    Yaropolov, Y.I.4
  • 34
    • 0013492803 scopus 로고
    • Studies on laccases of lacquer trees I. comparison of laccases obtained from Rhus vernicifera and Rhus succedanea
    • COI: 1:STN:280:DyaF38%2FotlGhuw%3D%3D, PID: 14482008
    • Omura T (1961) Studies on laccases of lacquer trees I. comparison of laccases obtained from Rhus vernicifera and Rhus succedanea. J Biochem 50:264–272
    • (1961) J Biochem , vol.50 , pp. 264-272
    • Omura, T.1
  • 35
    • 77956232051 scopus 로고    scopus 로고
    • First description of a laccase-like enzyme in soil algae
    • COI: 1:CAS:528:DC%2BC3cXhtVaqtLnK, PID: 20623267
    • Otto B, Schlosser D, Reisser W (2010) First description of a laccase-like enzyme in soil algae. Arch Microbiol 192:759–768. doi:10.1007/s00203-010-0603-7
    • (2010) Arch Microbiol , vol.192 , pp. 759-768
    • Otto, B.1    Schlosser, D.2    Reisser, W.3
  • 36
    • 0142075817 scopus 로고    scopus 로고
    • Atypical laccase isoenzymes from copper supplemented Pleurotus ostreatus cultures
    • COI: 1:CAS:528:DC%2BD3sXlvVWisrs%3D
    • Palmieri G, Cennamo G, Faraco V, Amoresano A, Sannia G, Giardina P (2003) Atypical laccase isoenzymes from copper supplemented Pleurotus ostreatus cultures. Enzyme Microb Tech 33:220–230. doi:10.1016/S0141-0229(03)00117-0
    • (2003) Enzyme Microb Tech , vol.33 , pp. 220-230
    • Palmieri, G.1    Cennamo, G.2    Faraco, V.3    Amoresano, A.4    Sannia, G.5    Giardina, P.6
  • 37
    • 57349092971 scopus 로고    scopus 로고
    • Enzymatic biotransformation of the azo dye Sudan Orange G with bacterial CotA-laccase
    • COI: 1:CAS:528:DC%2BD1cXhsV2ltrrJ, PID: 18938200
    • Pereira L, Coelho AV, Viegas CA, Santos MM, Robalo MP, Martins LO (2009) Enzymatic biotransformation of the azo dye Sudan Orange G with bacterial CotA-laccase. J Biotechnol 139:68–77. doi:10.1016/j.jbiotec.2008.09.001
    • (2009) J Biotechnol , vol.139 , pp. 68-77
    • Pereira, L.1    Coelho, A.V.2    Viegas, C.A.3    Santos, M.M.4    Robalo, M.P.5    Martins, L.O.6
  • 38
    • 84873987088 scopus 로고    scopus 로고
    • Transcriptional analysis of Pleurotus ostreatus laccase genes
    • COI: 1:CAS:528:DC%2BC3sXosFSgtw%3D%3D, PID: 22395908
    • Pezzella C, Lettera V, Piscitelli A, Giardina P, Sannia G (2013) Transcriptional analysis of Pleurotus ostreatus laccase genes. Appl Microbiol Biotechnol 97:705–717. doi:10.1007/s00253-012-3980-9
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 705-717
    • Pezzella, C.1    Lettera, V.2    Piscitelli, A.3    Giardina, P.4    Sannia, G.5
  • 39
    • 84872356068 scopus 로고    scopus 로고
    • Changes in phenolic compounds and cellular ultrastructure of Arctic and Antarctic strains of Zygnema (Zygnematophyceae, Streptophyta) after exposure to experimentally enhanced UV to PAR ratio
    • PID: 22903087
    • Pichrtová M, Remias D, Lewis LA, Holzinger A (2013) Changes in phenolic compounds and cellular ultrastructure of Arctic and Antarctic strains of Zygnema (Zygnematophyceae, Streptophyta) after exposure to experimentally enhanced UV to PAR ratio. Microb Ecol 65:68–83. doi:10.1007/s00248-012-0096-9
    • (2013) Microb Ecol , vol.65 , pp. 68-83
    • Pichrtová, M.1    Remias, D.2    Lewis, L.A.3    Holzinger, A.4
  • 40
    • 84885390284 scopus 로고    scopus 로고
    • Dirigent proteins: molecular characteristics and potential biotechnological applications
    • COI: 1:CAS:528:DC%2BC3sXhtlGltrjM, PID: 23989917
    • Pickel B, Schaller A (2013) Dirigent proteins: molecular characteristics and potential biotechnological applications. Appl Microbiol Biotechnol 97:8427–8438. doi:10.1007/s00253-013-5167-4
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 8427-8438
    • Pickel, B.1    Schaller, A.2
  • 41
    • 33344460777 scopus 로고    scopus 로고
    • TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat
    • COI: 1:CAS:528:DC%2BD2MXht1OgtLvK, PID: 16243908
    • Pourcel L, Routaboul JM, Kerhoas L, Caboche M, Lepiniec L, Debeaujon I (2005) TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat. Plant Cell 17:2966–2980. doi:10.1105/tpc.105.035154
    • (2005) Plant Cell , vol.17 , pp. 2966-2980
    • Pourcel, L.1    Routaboul, J.M.2    Kerhoas, L.3    Caboche, M.4    Lepiniec, L.5    Debeaujon, I.6
  • 42
    • 84865757418 scopus 로고    scopus 로고
    • Polyphenol oxidases in Physcomitrella: functional PPO1 knockout modulates cytokinin-dependent development in the moss Physcomitrella patens
    • COI: 1:CAS:528:DC%2BC38Xht1ygsrnF, PID: 22865913
    • Richter H, Lieberei R, Strnad M, Novák O, Gruz J, Rensing SA, von Schwartzenberg K (2012) Polyphenol oxidases in Physcomitrella: functional PPO1 knockout modulates cytokinin-dependent development in the moss Physcomitrella patens. J Exp Bot 63:5121–5135. doi:10.1093/jxb/ers169
    • (2012) J Exp Bot , vol.63 , pp. 5121-5135
    • Richter, H.1    Lieberei, R.2    Strnad, M.3    Novák, O.4    Gruz, J.5    Rensing, S.A.6    von Schwartzenberg, K.7
  • 43
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: blue enzymes for green chemistry
    • COI: 1:CAS:528:DC%2BD28XktVeiu7s%3D, PID: 16574262
    • Riva S (2006) Laccases: blue enzymes for green chemistry. Trends Biotechnol 24:219–226. doi:10.1016/j.tibtech.2006.03.006
    • (2006) Trends Biotechnol , vol.24 , pp. 219-226
    • Riva, S.1
  • 44
    • 84912282589 scopus 로고
    • Untersuchungen über Oxydase, Peroxydase und Ascorbinsäure in einigen Meeresalgen. Dissertation, University of Lund; C
    • Lindström: Lund
    • Rönnerstrand S (1943) Untersuchungen über Oxydase, Peroxydase und Ascorbinsäure in einigen Meeresalgen. Dissertation, University of Lund; C. W. Lindström, Lund
    • (1943)
    • Rönnerstrand, S.1
  • 45
    • 0032958739 scopus 로고    scopus 로고
    • Biodegradation of aromatic compounds by microalgae
    • COI: 1:CAS:528:DyaK1MXosFWhtw%3D%3D
    • Semple KT, Cain RB, Schmidt S (1999) Biodegradation of aromatic compounds by microalgae. FEMS Microbiol Lett 170:291–300. doi:10.1111/j.1574-6968.1999.tb13386.x
    • (1999) FEMS Microbiol Lett , vol.170 , pp. 291-300
    • Semple, K.T.1    Cain, R.B.2    Schmidt, S.3
  • 46
    • 0034333635 scopus 로고    scopus 로고
    • Oxidation of isoeugenol and coniferyl alcohol catalyzed by laccases isolated from Rhus vernicifera Stokes and Pycnoporus coccineus
    • COI: 1:CAS:528:DC%2BD3cXlvV2rs74%3D
    • Shiba T, Xiao L, Miyakoshi T, Chen CL (2000) Oxidation of isoeugenol and coniferyl alcohol catalyzed by laccases isolated from Rhus vernicifera Stokes and Pycnoporus coccineus. J Mol Catal B Enzym 10:605–615. doi:10.1016/S1381-1177(00)00184-3
    • (2000) J Mol Catal B Enzym , vol.10 , pp. 605-615
    • Shiba, T.1    Xiao, L.2    Miyakoshi, T.3    Chen, C.L.4
  • 47
    • 0035940069 scopus 로고    scopus 로고
    • Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R
    • COI: 1:CAS:528:DC%2BD3MXlslChtL8%3D, PID: 11500205
    • Soares G, De Amorim MT, Costa-Ferreira M (2001) Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R. J Biotechnol 89:123–129. doi:10.1016/S0168-1656(01)00302-9
    • (2001) J Biotechnol , vol.89 , pp. 123-129
    • Soares, G.1    De Amorim, M.T.2    Costa-Ferreira, M.3
  • 48
    • 0000232190 scopus 로고
    • Laccase from sycamore maple (Acer pseudoplatanus) polymerizes monolignols
    • COI: 1:CAS:528:DyaK38XlsVOhtbo%3D, PID: 16668984
    • Sterjiades R, Dean JF, Eriksson KEL (1992) Laccase from sycamore maple (Acer pseudoplatanus) polymerizes monolignols. Plant Physiol 99:1162–1168. doi:10.1104/pp.99.3.1162
    • (1992) Plant Physiol , vol.99 , pp. 1162-1168
    • Sterjiades, R.1    Dean, J.F.2    Eriksson, K.E.L.3
  • 49
    • 34250082818 scopus 로고
    • Extracellular laccases and peroxidases from sycamore maple (Acer pseudoplatanus) cell-suspension cultures
    • COI: 1:CAS:528:DyaK3sXks1Khu7Y%3D
    • Sterjiades R, Dean JF, Gamble G, Himmelsbach DS, Eriksson KEL (1993) Extracellular laccases and peroxidases from sycamore maple (Acer pseudoplatanus) cell-suspension cultures. Planta 190:75–87. doi:10.1007/BF00195678
    • (1993) Planta , vol.190 , pp. 75-87
    • Sterjiades, R.1    Dean, J.F.2    Gamble, G.3    Himmelsbach, D.S.4    Eriksson, K.E.L.5
  • 50
    • 33847670407 scopus 로고
    • Ferrozine—a new spectrophotometric reagent for iron
    • COI: 1:CAS:528:DyaE3cXkt1WjtL8%3D
    • Stookey LL (1970) Ferrozine—a new spectrophotometric reagent for iron. Anal Chem 42:779–781. doi:10.1021/ac60289a016
    • (1970) Anal Chem , vol.42 , pp. 779-781
    • Stookey, L.L.1
  • 51
    • 84870193427 scopus 로고    scopus 로고
    • Mixotrophic cyanobacteria and microalgae as distinctive biological agents for organic pollutant degradation
    • COI: 1:CAS:528:DC%2BC3sXhvVCksQ%3D%3D, PID: 23201778
    • Subashchandrabose SR, Ramakrishnan B, Megharaj M, Venkateswarlu K, Naidu R (2013) Mixotrophic cyanobacteria and microalgae as distinctive biological agents for organic pollutant degradation. Environ Int 51:59–72. doi:10.1016/j.envint.2012.10.007
    • (2013) Environ Int , vol.51 , pp. 59-72
    • Subashchandrabose, S.R.1    Ramakrishnan, B.2    Megharaj, M.3    Venkateswarlu, K.4    Naidu, R.5
  • 53
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • COI: 1:CAS:528:DyaK2cXkt12lsrs%3D
    • Thurston CF (1994) The structure and function of fungal laccases. Microbiology 140:19–26. doi:10.1099/13500872-140-1-19
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 54
    • 3042825330 scopus 로고    scopus 로고
    • Ex planta phytoremediation of trichlorophenol and phenolic allelochemicals via an engineered secretory laccase
    • PID: 15195102
    • Wang GD, Li QJ, Luo B, Chen XY (2004) Ex planta phytoremediation of trichlorophenol and phenolic allelochemicals via an engineered secretory laccase. Nat Biotechnol 22:893–897. doi:10.1038/nbt982
    • (2004) Nat Biotechnol , vol.22 , pp. 893-897
    • Wang, G.D.1    Li, Q.J.2    Luo, B.3    Chen, X.Y.4
  • 55
    • 36849036714 scopus 로고    scopus 로고
    • Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE
    • COI: 1:CAS:528:DC%2BD2sXht1ymtrjN
    • Xia K, Manning M, Hesham H, Lin Q, Bystroff C, Colón W (2007) Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE. P Natl Acad Sci USA 104:17329–17334. doi:10.1073/pnas.0705417104
    • (2007) P Natl Acad Sci USA , vol.104 , pp. 17329-17334
    • Xia, K.1    Manning, M.2    Hesham, H.3    Lin, Q.4    Bystroff, C.5    Colón, W.6
  • 56
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • COI: 1:CAS:528:DyaK2sXmtFGjsw%3D%3D, PID: 8995383
    • Xu F (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J Biol Chem 272:924–928. doi:10.1074/jbc.272.2.924
    • (1997) J Biol Chem , vol.272 , pp. 924-928
    • Xu, F.1
  • 57
    • 0030025889 scopus 로고    scopus 로고
    • A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
    • Xu F, Shin W, Brown SH, Wahleithner JA, Sundaram UM, Solomon EI (1996) A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. BBA Protein Struct M 1292:303–311. doi:10.1016/0167-4838(95)00210-3
    • (1996) BBA Protein Struct M , vol.1292 , pp. 303-311
    • Xu, F.1    Shin, W.2    Brown, S.H.3    Wahleithner, J.A.4    Sundaram, U.M.5    Solomon, E.I.6
  • 58
    • 34848826800 scopus 로고
    • LXIII.—chemistry of lacquer (Urushi). Part I. communication from the chemical society of Tokio
    • COI: 1:CAS:528:DyaD28Xmt1Glug%3D%3D
    • Yoshida H (1883) LXIII.—chemistry of lacquer (Urushi). Part I. communication from the chemical society of Tokio. J Chem Soc Trans 43:472–486. doi:10.1039/CT8834300472
    • (1883) J Chem Soc Trans , vol.43 , pp. 472-486
    • Yoshida, H.1
  • 60
    • 0002846832 scopus 로고
    • Zur quantitativen Analyse der Chloroplastenpigmente
    • COI: 1:CAS:528:DyaF28XhtVKksLw%3D
    • Ziegler R, Egle K (1965) Zur quantitativen Analyse der Chloroplastenpigmente. Beitr Biol Pflanzen 41:11–37
    • (1965) Beitr Biol Pflanzen , vol.41 , pp. 11-37
    • Ziegler, R.1    Egle, K.2


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