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Volumn 53, Issue 6-7, 2013, Pages 427-437

Characterization of cellobiose dehydrogenase and its FAD-domain from the ligninolytic basidiomycete Pycnoporus sanguineus

Author keywords

Cellobiose dehydrogenase; Fungi; Gene; Pycnoporus

Indexed keywords

ANTIOXIDANT PROPERTIES; CARBOHYDRATE CONTENT; CELLOBIOSE DEHYDROGENASE; CULTURE SUPERNATANT; FULL-LENGTH CDNA; ISO-ELECTRIC POINTS; PYCNOPORUS; PYCNOPORUS SANGUINEUS;

EID: 84886420926     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.09.007     Document Type: Article
Times cited : (22)

References (88)
  • 2
    • 84255189470 scopus 로고    scopus 로고
    • Phylogenetic classification of Trametes (Basidiomycota, Polyporales) based on a five-marker dataset
    • Justo A., Hibbett D.S. Phylogenetic classification of Trametes (Basidiomycota, Polyporales) based on a five-marker dataset. Taxon. 2011, 60:1567-1583.
    • (2011) Taxon. , vol.60 , pp. 1567-1583
    • Justo, A.1    Hibbett, D.S.2
  • 3
    • 0028968589 scopus 로고
    • Antibacterial activity of a substance produced by the fungus Pycnoporus sanguineus (Fr.) Murr
    • Smania A., Monache F.D., Smania E.F., Gil M.L., Benchetrit L.C., Cruz F.S. Antibacterial activity of a substance produced by the fungus Pycnoporus sanguineus (Fr.) Murr. J Ethnopharmacol 1995, 45:177-181.
    • (1995) J Ethnopharmacol , vol.45 , pp. 177-181
    • Smania, A.1    Monache, F.D.2    Smania, E.F.3    Gil, M.L.4    Benchetrit, L.C.5    Cruz, F.S.6
  • 4
    • 0242268439 scopus 로고    scopus 로고
    • Toxicity and antiviral activity of cinnabarin obtained from Pycnoporus sanguineus (Fr.) Murr
    • Smania A., Marques C.J., Smania E.F., Zanetti C.R., Carobrez S.G., Tramonte R., et al. Toxicity and antiviral activity of cinnabarin obtained from Pycnoporus sanguineus (Fr.) Murr. Phytother Res 2003, 17:1069-1072.
    • (2003) Phytother Res , vol.17 , pp. 1069-1072
    • Smania, A.1    Marques, C.J.2    Smania, E.F.3    Zanetti, C.R.4    Carobrez, S.G.5    Tramonte, R.6
  • 6
    • 41849124220 scopus 로고    scopus 로고
    • Biosorption of cadmium (II) ions by immobilized cells of Pycnoporus sanguineus from aqueous solution
    • Mashitah M.D., Yus Azila Y., Bhatia S. Biosorption of cadmium (II) ions by immobilized cells of Pycnoporus sanguineus from aqueous solution. Bioresour Technol 2008, 99:4742-4748.
    • (2008) Bioresour Technol , vol.99 , pp. 4742-4748
    • Mashitah, M.D.1    Yus Azila, Y.2    Bhatia, S.3
  • 7
    • 0035134272 scopus 로고    scopus 로고
    • Heavy metals removal in fixed-bed column by the macro fungus Pycnoporus sanguineus
    • Zulfadhly Z., Mashitah M.D., Bhatia S. Heavy metals removal in fixed-bed column by the macro fungus Pycnoporus sanguineus. Environ Pollut 2001, 112:463-470.
    • (2001) Environ Pollut , vol.112 , pp. 463-470
    • Zulfadhly, Z.1    Mashitah, M.D.2    Bhatia, S.3
  • 10
    • 77954828271 scopus 로고    scopus 로고
    • Derivatization of the azole 1-aminobenzotriazole using laccase of Pycnoporus cinnabarinus and Myceliophthora thermophila: influence of methanol on the reaction and biological evaluation of the derivatives
    • Hahn V., Mikolasch A., Wende K., Bartrow H., Lindequist U., Schauer F. Derivatization of the azole 1-aminobenzotriazole using laccase of Pycnoporus cinnabarinus and Myceliophthora thermophila: influence of methanol on the reaction and biological evaluation of the derivatives. Biotechnol Appl Biochem 2010, 56:43-48.
    • (2010) Biotechnol Appl Biochem , vol.56 , pp. 43-48
    • Hahn, V.1    Mikolasch, A.2    Wende, K.3    Bartrow, H.4    Lindequist, U.5    Schauer, F.6
  • 11
    • 0032935214 scopus 로고    scopus 로고
    • Enhanced degradation of polyvinyl alcohol by Pycnoporus cinnabarinus after pretreatment with Fenton's reagent
    • Larking D.M., Crawford R.J., Christie G.B., Lonergan G.T. Enhanced degradation of polyvinyl alcohol by Pycnoporus cinnabarinus after pretreatment with Fenton's reagent. Appl Environ Microbiol 1999, 65:1798-1800.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1798-1800
    • Larking, D.M.1    Crawford, R.J.2    Christie, G.B.3    Lonergan, G.T.4
  • 12
    • 0035936935 scopus 로고    scopus 로고
    • Phenyl propenoic side chain degradation of ferulic acid by Pycnoporus cinnabarinus - elucidation of metabolic pathways using [5-2H]-ferulic acid
    • Krings U., Pilawa S., Theobald C., Berger R.G. Phenyl propenoic side chain degradation of ferulic acid by Pycnoporus cinnabarinus - elucidation of metabolic pathways using [5-2H]-ferulic acid. J Biotechnol 2001, 85:305-314.
    • (2001) J Biotechnol , vol.85 , pp. 305-314
    • Krings, U.1    Pilawa, S.2    Theobald, C.3    Berger, R.G.4
  • 13
    • 84864623329 scopus 로고    scopus 로고
    • Simultaneous laccase production and color removal by culturing fungus Pycnoporus sp. SYBC-L3 in a textile wastewater effluent supplemented with a lignocellulosic waste Phragmites australis
    • Liu J., Cai Y., Liao X., Huang Q., Hao Z., Hu M., et al. Simultaneous laccase production and color removal by culturing fungus Pycnoporus sp. SYBC-L3 in a textile wastewater effluent supplemented with a lignocellulosic waste Phragmites australis. Bull Environ Contam Toxicol 2012, 89:269-273.
    • (2012) Bull Environ Contam Toxicol , vol.89 , pp. 269-273
    • Liu, J.1    Cai, Y.2    Liao, X.3    Huang, Q.4    Hao, Z.5    Hu, M.6
  • 14
    • 0034237336 scopus 로고    scopus 로고
    • Transformation and degradation of the disazo dye Chicago Sky Blue by a purified laccase from Pycnoporus cinnabarinus
    • Schliephake K., Mainwaring D.E., Lonergan G.T., Jones I.K., Baker W.L. Transformation and degradation of the disazo dye Chicago Sky Blue by a purified laccase from Pycnoporus cinnabarinus. Enzyme Microb Technol 2000, 27:100-107.
    • (2000) Enzyme Microb Technol , vol.27 , pp. 100-107
    • Schliephake, K.1    Mainwaring, D.E.2    Lonergan, G.T.3    Jones, I.K.4    Baker, W.L.5
  • 17
    • 67650248272 scopus 로고    scopus 로고
    • Fusion of a family 1 carbohydrate binding module of Aspergillus niger to the Pycnoporus cinnabarinus laccase for efficient softwood kraft pulp biobleaching
    • Ravalason H., Herpoel-Gimbert I., Record E., Bertaud F., Grisel S., de Weert S., et al. Fusion of a family 1 carbohydrate binding module of Aspergillus niger to the Pycnoporus cinnabarinus laccase for efficient softwood kraft pulp biobleaching. J Biotechnol 2009, 142:220-226.
    • (2009) J Biotechnol , vol.142 , pp. 220-226
    • Ravalason, H.1    Herpoel-Gimbert, I.2    Record, E.3    Bertaud, F.4    Grisel, S.5    de Weert, S.6
  • 18
    • 2942620243 scopus 로고    scopus 로고
    • Peptides and proteins from fungi
    • Ng T.B. Peptides and proteins from fungi. Peptides 2004, 25:1055-1073.
    • (2004) Peptides , vol.25 , pp. 1055-1073
    • Ng, T.B.1
  • 19
    • 84954897156 scopus 로고
    • Purification and properties of laccase excreted by Pycnoporus coccineus
    • Oda Y., Adachi K., Aita I., Ito M., Aso Y., Igarashi H. Purification and properties of laccase excreted by Pycnoporus coccineus. Agric Biol Chem 1991, 55:1393-1395.
    • (1991) Agric Biol Chem , vol.55 , pp. 1393-1395
    • Oda, Y.1    Adachi, K.2    Aita, I.3    Ito, M.4    Aso, Y.5    Igarashi, H.6
  • 20
    • 77952183363 scopus 로고    scopus 로고
    • High redox potential laccases from the ligninolytic fungi Pycnoporus coccineus and Pycnoporus sanguineus suitable for white biotechnology: from gene cloning to enzyme characterization and applications
    • Uzan E., Nousiainen P., Balland V., Sipila J., Piumi F., Navarro D., et al. High redox potential laccases from the ligninolytic fungi Pycnoporus coccineus and Pycnoporus sanguineus suitable for white biotechnology: from gene cloning to enzyme characterization and applications. J Appl Microbiol 2010, 108:2199-2213.
    • (2010) J Appl Microbiol , vol.108 , pp. 2199-2213
    • Uzan, E.1    Nousiainen, P.2    Balland, V.3    Sipila, J.4    Piumi, F.5    Navarro, D.6
  • 21
    • 34248562665 scopus 로고    scopus 로고
    • Potential of a Pycnoporus sanguineus laccase in bioremediation of wastewater and kinetic activation in the presence of an anthraquinonic acid dye
    • Trovaslet M., Enaud E., Guiavarc'h Y., Corbisier A.M., Vanhulle S. Potential of a Pycnoporus sanguineus laccase in bioremediation of wastewater and kinetic activation in the presence of an anthraquinonic acid dye. Enzyme Microb Technol 2007, 41:368-376.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 368-376
    • Trovaslet, M.1    Enaud, E.2    Guiavarc'h, Y.3    Corbisier, A.M.4    Vanhulle, S.5
  • 22
    • 0018944476 scopus 로고
    • Substrate specificity of carboxyl proteinase from Pycnoporus coccineus, a wood-deteriorating fungus
    • Ichishima E., Kumagai H., Tomoda K. Substrate specificity of carboxyl proteinase from Pycnoporus coccineus, a wood-deteriorating fungus. Curr Microbiol 1980, 3:333-337.
    • (1980) Curr Microbiol , vol.3 , pp. 333-337
    • Ichishima, E.1    Kumagai, H.2    Tomoda, K.3
  • 23
    • 0003269033 scopus 로고
    • Acid carboxypeptidase from a wood-deteriorating basidiomycete, Pycnoporus sanguineus
    • Ichishima E., Yoshimura K., Tomoda K. Acid carboxypeptidase from a wood-deteriorating basidiomycete, Pycnoporus sanguineus. Phytochemistry 1983, 22:825-829.
    • (1983) Phytochemistry , vol.22 , pp. 825-829
    • Ichishima, E.1    Yoshimura, K.2    Tomoda, K.3
  • 24
    • 77957063365 scopus 로고
    • Chitinase and β-N-acetylhexosaminidase from Pycnoporus cinnabarinus
    • Academic Press, A. Willis, S.T.K. Wood (Eds.)
    • Ohtakara A. Chitinase and β-N-acetylhexosaminidase from Pycnoporus cinnabarinus. Methods in Enzymology 1988, 462-470. Academic Press. A. Willis, S.T.K. Wood (Eds.).
    • (1988) Methods in Enzymology , pp. 462-470
    • Ohtakara, A.1
  • 25
    • 0042589982 scopus 로고
    • 1,2-Alpha-d-mannosidase from a wood-rotting basidiomycete, Pycnoporus sanguineus
    • Ichishima E., Ito Y., Takeuchi M. 1,2-Alpha-d-mannosidase from a wood-rotting basidiomycete, Pycnoporus sanguineus. Phytochemistry 1985, 24:2835-2837.
    • (1985) Phytochemistry , vol.24 , pp. 2835-2837
    • Ichishima, E.1    Ito, Y.2    Takeuchi, M.3
  • 26
    • 0001448532 scopus 로고
    • Purification and enzymatic-properties of alpha-galactosidase from Pycnoporus cinnabarinus
    • Ohtakara A., Mitsutomi M., Uchida Y. Purification and enzymatic-properties of alpha-galactosidase from Pycnoporus cinnabarinus. Agric Biol Chem 1984, 48:1319-1327.
    • (1984) Agric Biol Chem , vol.48 , pp. 1319-1327
    • Ohtakara, A.1    Mitsutomi, M.2    Uchida, Y.3
  • 27
    • 0000634771 scopus 로고
    • Immobilization of thermostable alpha-galactosidase from Pycnoporus cinnabarinus on chitosan beads and its application to the hydrolysis of raffinose in beet sugar molasses
    • Ohtakara A., Mitsutomi M. Immobilization of thermostable alpha-galactosidase from Pycnoporus cinnabarinus on chitosan beads and its application to the hydrolysis of raffinose in beet sugar molasses. J Ferment Technol 1987, 65:493-498.
    • (1987) J Ferment Technol , vol.65 , pp. 493-498
    • Ohtakara, A.1    Mitsutomi, M.2
  • 28
    • 11144334644 scopus 로고
    • Purification and some properties of acid beta-galactosidase from Pycnoporus cinnabarinus
    • Ohtakara A., Hayashi N., Mitsutomi M. Purification and some properties of acid beta-galactosidase from Pycnoporus cinnabarinus. J Ferment Technol 1981, 59:325-328.
    • (1981) J Ferment Technol , vol.59 , pp. 325-328
    • Ohtakara, A.1    Hayashi, N.2    Mitsutomi, M.3
  • 29
    • 0036843820 scopus 로고    scopus 로고
    • Lignocellulolytic and hemicellulolytic system of Pycnoporus cinnabarinus: isolation and characterization of a cellobiose dehydrogenase and a new xylanase
    • Sigoillot C., Lomascolo A., Record E., Robert J.L., Asther M., Sigoillot J.C. Lignocellulolytic and hemicellulolytic system of Pycnoporus cinnabarinus: isolation and characterization of a cellobiose dehydrogenase and a new xylanase. Enzyme Microb Technol 2002, 31:876-883.
    • (2002) Enzyme Microb Technol , vol.31 , pp. 876-883
    • Sigoillot, C.1    Lomascolo, A.2    Record, E.3    Robert, J.L.4    Asther, M.5    Sigoillot, J.C.6
  • 30
    • 0036496897 scopus 로고    scopus 로고
    • Efficient enzymatic delignification of wheat straw pulp by a sequential xylanase-laccase mediator treatment
    • Herpoel I., Jeller H., Fang G., Petit-Conil M., Bourbonnais R., Robert J.L., et al. Efficient enzymatic delignification of wheat straw pulp by a sequential xylanase-laccase mediator treatment. J Pulp Pap Sci 2002, 28:67-71.
    • (2002) J Pulp Pap Sci , vol.28 , pp. 67-71
    • Herpoel, I.1    Jeller, H.2    Fang, G.3    Petit-Conil, M.4    Bourbonnais, R.5    Robert, J.L.6
  • 31
    • 0033010480 scopus 로고    scopus 로고
    • Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase
    • Moukha S.M., Dumonceaux T.J., Record E., Archibald F.S. Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase. Gene 1999, 234:23-33.
    • (1999) Gene , vol.234 , pp. 23-33
    • Moukha, S.M.1    Dumonceaux, T.J.2    Record, E.3    Archibald, F.S.4
  • 32
    • 84868636487 scopus 로고    scopus 로고
    • Recombinantly produced cellobiose dehydrogenase from Corynascus thermophilus for glucose biosensors and biofuel cells
    • Harreither W., Felice A.K., Paukner R., Gorton L., Ludwig R., Sygmund C. Recombinantly produced cellobiose dehydrogenase from Corynascus thermophilus for glucose biosensors and biofuel cells. Biotechnol J 2012, 7:1359-1366.
    • (2012) Biotechnol J , vol.7 , pp. 1359-1366
    • Harreither, W.1    Felice, A.K.2    Paukner, R.3    Gorton, L.4    Ludwig, R.5    Sygmund, C.6
  • 33
    • 80053096980 scopus 로고    scopus 로고
    • Biological pretreatment with a cellobiose dehydrogenase-deficient strain of Trametes versicolor enhances the biofuel potential of canola straw
    • Canam T., Town J.R., Tsang A., McAllister T.A., Dumonceaux T.J. Biological pretreatment with a cellobiose dehydrogenase-deficient strain of Trametes versicolor enhances the biofuel potential of canola straw. Bioresour Technol 2011, 102:10020-10027.
    • (2011) Bioresour Technol , vol.102 , pp. 10020-10027
    • Canam, T.1    Town, J.R.2    Tsang, A.3    McAllister, T.A.4    Dumonceaux, T.J.5
  • 34
    • 84455208197 scopus 로고    scopus 로고
    • A novel combined thermometric and amperometric biosensor for lactose determination based on immobilised cellobiose dehydrogenase
    • Yakovleva M., Buzas O., Matsumura H., Samejima M., Igarashi K., Larsson P.O., et al. A novel combined thermometric and amperometric biosensor for lactose determination based on immobilised cellobiose dehydrogenase. Biosens Bioelectron 2012, 31:251-256.
    • (2012) Biosens Bioelectron , vol.31 , pp. 251-256
    • Yakovleva, M.1    Buzas, O.2    Matsumura, H.3    Samejima, M.4    Igarashi, K.5    Larsson, P.O.6
  • 35
    • 79955157028 scopus 로고    scopus 로고
    • A third generation glucose biosensor based on cellobiose dehydrogenase from Corynascus thermophilus and single-walled carbon nanotubes
    • Tasca F., Zafar M.N., Harreither W., Noll G., Ludwig R., Gorton L. A third generation glucose biosensor based on cellobiose dehydrogenase from Corynascus thermophilus and single-walled carbon nanotubes. Analyst 2011, 136:2033-2036.
    • (2011) Analyst , vol.136 , pp. 2033-2036
    • Tasca, F.1    Zafar, M.N.2    Harreither, W.3    Noll, G.4    Ludwig, R.5    Gorton, L.6
  • 36
    • 30744439064 scopus 로고    scopus 로고
    • Third-generation biosensor for lactose based on newly discovered cellobiose dehydrogenase
    • Stoica L., Ludwig R., Haltrich D., Gorton L. Third-generation biosensor for lactose based on newly discovered cellobiose dehydrogenase. Anal Chem 2006, 78:393-398.
    • (2006) Anal Chem , vol.78 , pp. 393-398
    • Stoica, L.1    Ludwig, R.2    Haltrich, D.3    Gorton, L.4
  • 37
    • 17444365446 scopus 로고    scopus 로고
    • Colour remediation of pulp mill effluent using purified fungal cellobiose dehydrogenase: reaction optimisation and mechanism of degradation
    • Wingate K.G., Stuthridge T., Mansfield S.D. Colour remediation of pulp mill effluent using purified fungal cellobiose dehydrogenase: reaction optimisation and mechanism of degradation. Biotechnol Bioeng 2005, 90:95-106.
    • (2005) Biotechnol Bioeng , vol.90 , pp. 95-106
    • Wingate, K.G.1    Stuthridge, T.2    Mansfield, S.D.3
  • 38
    • 0033166956 scopus 로고    scopus 로고
    • Degradation of chemicals by reactive radicals produced by cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Cameron M.D., Aust S.D. Degradation of chemicals by reactive radicals produced by cellobiose dehydrogenase from Phanerochaete chrysosporium. Arch Biochem Biophys 1999, 367:115-121.
    • (1999) Arch Biochem Biophys , vol.367 , pp. 115-121
    • Cameron, M.D.1    Aust, S.D.2
  • 39
    • 84866483946 scopus 로고    scopus 로고
    • Enzymatic decolorization of spent textile dyeing baths composed by mixtures of synthetic dyes and additives
    • Ciullini I., Gullotto A., Tilli S., Sannia G., Basosi R., Scozzafava A., et al. Enzymatic decolorization of spent textile dyeing baths composed by mixtures of synthetic dyes and additives. Appl Microbiol Biotechnol 2012, 96:395-405.
    • (2012) Appl Microbiol Biotechnol , vol.96 , pp. 395-405
    • Ciullini, I.1    Gullotto, A.2    Tilli, S.3    Sannia, G.4    Basosi, R.5    Scozzafava, A.6
  • 40
    • 80054695246 scopus 로고    scopus 로고
    • Differential decolorization of textile dyes in mixtures and the joint effect of laccase and cellobiose dehydrogenase activities present in extracellular extracts from Funalia trogii
    • Tilli S., Ciullini I., Scozzafava A., Briganti F. Differential decolorization of textile dyes in mixtures and the joint effect of laccase and cellobiose dehydrogenase activities present in extracellular extracts from Funalia trogii. Enzyme Microb Technol 2011, 49:465-471.
    • (2011) Enzyme Microb Technol , vol.49 , pp. 465-471
    • Tilli, S.1    Ciullini, I.2    Scozzafava, A.3    Briganti, F.4
  • 41
    • 84870364865 scopus 로고    scopus 로고
    • Cellulose oxidation and bleaching processes based on recombinant Myriococcum thermophilum cellobiose dehydrogenase
    • Flitsch A., Prasetyo E.N., Sygmund C., Ludwig R., Nyanhongo G.S., Guebitz G.M. Cellulose oxidation and bleaching processes based on recombinant Myriococcum thermophilum cellobiose dehydrogenase. Enzyme Microb Technol 2013, 52:60-67.
    • (2013) Enzyme Microb Technol , vol.52 , pp. 60-67
    • Flitsch, A.1    Prasetyo, E.N.2    Sygmund, C.3    Ludwig, R.4    Nyanhongo, G.S.5    Guebitz, G.M.6
  • 42
    • 79551625647 scopus 로고    scopus 로고
    • In situ generation of hydrogen peroxide by carbohydrate oxidase and cellobiose dehydrogenase for bleaching purposes
    • Pricelius S., Ludwig R., Lant N.J., Haltrich D., Guebitz G.M. In situ generation of hydrogen peroxide by carbohydrate oxidase and cellobiose dehydrogenase for bleaching purposes. Biotechnol J 2011, 6:224-230.
    • (2011) Biotechnol J , vol.6 , pp. 224-230
    • Pricelius, S.1    Ludwig, R.2    Lant, N.J.3    Haltrich, D.4    Guebitz, G.M.5
  • 43
    • 84875230725 scopus 로고    scopus 로고
    • An antioxidant regenerating system for continuous quenching of free radicals in chronic wounds
    • Nyanhongo G.S., Sygmund C., Ludwig R., Prasetyo E.N., Guebitz G.M. An antioxidant regenerating system for continuous quenching of free radicals in chronic wounds. Eur J Pharm Biopharm 2013, 83:396-404.
    • (2013) Eur J Pharm Biopharm , vol.83 , pp. 396-404
    • Nyanhongo, G.S.1    Sygmund, C.2    Ludwig, R.3    Prasetyo, E.N.4    Guebitz, G.M.5
  • 44
    • 84861155519 scopus 로고    scopus 로고
    • Functional analysis of the degradation of cellulosic substrates by a Chaetomium globosum endophytic isolate
    • Longoni P., Rodolfi M., Pantaleoni L., Doria E., Concia L., Picco A.M., et al. Functional analysis of the degradation of cellulosic substrates by a Chaetomium globosum endophytic isolate. Appl Environ Microbiol 2012, 78:3693-3705.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 3693-3705
    • Longoni, P.1    Rodolfi, M.2    Pantaleoni, L.3    Doria, E.4    Concia, L.5    Picco, A.M.6
  • 45
    • 84863175956 scopus 로고    scopus 로고
    • A novel biochemical route for fuels and chemicals production from cellulosic biomass
    • Fan Z., Wu W., Hildebrand A., Kasuga T., Zhang R., Xiong X. A novel biochemical route for fuels and chemicals production from cellulosic biomass. PLoS ONE 2012, 7:e31693.
    • (2012) PLoS ONE , vol.7
    • Fan, Z.1    Wu, W.2    Hildebrand, A.3    Kasuga, T.4    Zhang, R.5    Xiong, X.6
  • 46
    • 84455173789 scopus 로고    scopus 로고
    • Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes
    • Bey M., Berrin J.G., Poidevin L., Sigoillot J.C. Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes. Microb Cell Fact 2011, 10:113.
    • (2011) Microb Cell Fact , vol.10 , pp. 113
    • Bey, M.1    Berrin, J.G.2    Poidevin, L.3    Sigoillot, J.C.4
  • 47
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase - a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
    • Zamocky M., Ludwig R., Peterbauer C., Hallberg B.M., Divne C., Nicholls P., et al. Cellobiose dehydrogenase - a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi. Curr Protein Pept Sci 2006, 7:255-280.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 255-280
    • Zamocky, M.1    Ludwig, R.2    Peterbauer, C.3    Hallberg, B.M.4    Divne, C.5    Nicholls, P.6
  • 49
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg B.M., Henriksson G., Pettersson G., Divne C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J Mol Biol 2002, 315:421-434.
    • (2002) J Mol Biol , vol.315 , pp. 421-434
    • Hallberg, B.M.1    Henriksson, G.2    Pettersson, G.3    Divne, C.4
  • 50
    • 77952240274 scopus 로고    scopus 로고
    • Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli
    • Desriani Ferri S., Sode K. Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli. Biotechnol Lett 2010, 32:855-859.
    • (2010) Biotechnol Lett , vol.32 , pp. 855-859
    • Desriani Ferri, S.1    Sode, K.2
  • 51
    • 78049264739 scopus 로고    scopus 로고
    • Expression of cellobiose dehydrogenase from Neurospora crassa in Pichia pastoris and its purification and characterization
    • Zhang R., Fan Z., Kasuga T. Expression of cellobiose dehydrogenase from Neurospora crassa in Pichia pastoris and its purification and characterization. Protein Expr Purif 2011, 75:63-69.
    • (2011) Protein Expr Purif , vol.75 , pp. 63-69
    • Zhang, R.1    Fan, Z.2    Kasuga, T.3
  • 52
    • 0022349301 scopus 로고
    • The purification and properties of cellobiose dehydrogenase from Sclerotium rolfsii and its role in cellulolysis
    • Sadana J.C., Patil R.V. The purification and properties of cellobiose dehydrogenase from Sclerotium rolfsii and its role in cellulolysis. J Gen Microbiol 1985, 131:1917-1923.
    • (1985) J Gen Microbiol , vol.131 , pp. 1917-1923
    • Sadana, J.C.1    Patil, R.V.2
  • 53
    • 0002616144 scopus 로고
    • Occurrence of tyrosinase and laccase in fruit bodies and mycelia of some Hymenomycetes
    • Lindeberg G., Holm G. Occurrence of tyrosinase and laccase in fruit bodies and mycelia of some Hymenomycetes. Physiol Plant 1952, 5:100-114.
    • (1952) Physiol Plant , vol.5 , pp. 100-114
    • Lindeberg, G.1    Holm, G.2
  • 54
    • 0032695182 scopus 로고    scopus 로고
    • Optimization of cellobiose dehydrogenase production by Schizophyllum commune and effect of the enzyme on kraft pulp bleaching by ligninases
    • Fang J., Huang F., Gao P. Optimization of cellobiose dehydrogenase production by Schizophyllum commune and effect of the enzyme on kraft pulp bleaching by ligninases. Process Biochem 1999, 34:957-961.
    • (1999) Process Biochem , vol.34 , pp. 957-961
    • Fang, J.1    Huang, F.2    Gao, P.3
  • 55
    • 0035318377 scopus 로고    scopus 로고
    • Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii
    • Baminger U., Subramaniam S.S., Renganathan V., Haltrich D. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl Environ Microbiol 2001, 67:1766-1774.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1766-1774
    • Baminger, U.1    Subramaniam, S.S.2    Renganathan, V.3    Haltrich, D.4
  • 56
    • 28444457376 scopus 로고    scopus 로고
    • Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26(-) and comparison with basidiomycetous cellobiose dehydrogenases
    • Karapetyan K.N., Fedorova T.V., Vasil'chenko L.G., Ludwig R., Haltrich D., Rabinovich M.L. Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26(-) and comparison with basidiomycetous cellobiose dehydrogenases. J Biotechnol 2006, 121:34-48.
    • (2006) J Biotechnol , vol.121 , pp. 34-48
    • Karapetyan, K.N.1    Fedorova, T.V.2    Vasil'chenko, L.G.3    Ludwig, R.4    Haltrich, D.5    Rabinovich, M.L.6
  • 57
    • 0025865802 scopus 로고
    • Cellobiose dehydrogenases of Sporotrichum (Chrysosporium) thermophile
    • Canevascini G., Borer P., Dreyer J.L. Cellobiose dehydrogenases of Sporotrichum (Chrysosporium) thermophile. Eur J Biochem 1991, 198:43-52.
    • (1991) Eur J Biochem , vol.198 , pp. 43-52
    • Canevascini, G.1    Borer, P.2    Dreyer, J.L.3
  • 58
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 59
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 60
    • 33947488027 scopus 로고
    • Quantitative determination of monosaccharides as their alditol acetates by gas liquid chromatography
    • Sawardek J.S., Sloneker J.H., Jeanes A. Quantitative determination of monosaccharides as their alditol acetates by gas liquid chromatography. Anal Chem 1965, 37:1602-1604.
    • (1965) Anal Chem , vol.37 , pp. 1602-1604
    • Sawardek, J.S.1    Sloneker, J.H.2    Jeanes, A.3
  • 61
    • 0038201596 scopus 로고    scopus 로고
    • Determination of antioxidant activity of phenolic antioxidants in a Fenton-type reaction system by chemiluminescence assay
    • Cheng Z.Y., Yan G.T., Li Y.Z., Chang W.B. Determination of antioxidant activity of phenolic antioxidants in a Fenton-type reaction system by chemiluminescence assay. Anal Bioanal Chem 2003, 375:376-380.
    • (2003) Anal Bioanal Chem , vol.375 , pp. 376-380
    • Cheng, Z.Y.1    Yan, G.T.2    Li, Y.Z.3    Chang, W.B.4
  • 66
    • 42749088544 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase production by the mycelial culture of the mushroom Termitomyces clypeatus
    • Saha T., Ghosh D., Mukherjee S., Bose S., Mukherjee M. Cellobiose dehydrogenase production by the mycelial culture of the mushroom Termitomyces clypeatus. Process Biochem 2008, 43:634-641.
    • (2008) Process Biochem , vol.43 , pp. 634-641
    • Saha, T.1    Ghosh, D.2    Mukherjee, S.3    Bose, S.4    Mukherjee, M.5
  • 67
    • 0032519528 scopus 로고    scopus 로고
    • Characterization of a cellobiose dehydrogenase from Humicola insolens
    • Schou C., Christensen M.H., Schulein M. Characterization of a cellobiose dehydrogenase from Humicola insolens. Biochem J 1998, 330(Pt 1):565-571.
    • (1998) Biochem J , vol.330 , Issue.PART 1 , pp. 565-571
    • Schou, C.1    Christensen, M.H.2    Schulein, M.3
  • 68
    • 34248147969 scopus 로고    scopus 로고
    • Role of ethanol on growth, laccase production and protease activity in Pycnoporus cinnabarinus ss3
    • Meza J.C., Auria R., Lomascolo A., Sigoillot J.C., Casalat L. Role of ethanol on growth, laccase production and protease activity in Pycnoporus cinnabarinus ss3. Enzyme Microb Technol 2007, 41:162-168.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 162-168
    • Meza, J.C.1    Auria, R.2    Lomascolo, A.3    Sigoillot, J.C.4    Casalat, L.5
  • 69
    • 0020076027 scopus 로고
    • Initial sites of insulin cleavage and stereospecificity of carboxyl proteinases from Aspergillus sojae and Pycnoporus coccineus
    • Ichishima E., Emi M., Majima E., Mayumi Y., Kumagai H., Hayashi K., et al. Initial sites of insulin cleavage and stereospecificity of carboxyl proteinases from Aspergillus sojae and Pycnoporus coccineus. Biochim Biophys Acta 1982, 700:247-253.
    • (1982) Biochim Biophys Acta , vol.700 , pp. 247-253
    • Ichishima, E.1    Emi, M.2    Majima, E.3    Mayumi, Y.4    Kumagai, H.5    Hayashi, K.6
  • 70
    • 0029860128 scopus 로고    scopus 로고
    • Purification and characterization of cellobiose dehydrogenases from the white rot fungus Trametes versicolor
    • Roy B.P., Dumonceaux T., Koukoulas A.A., Archibald F.S. Purification and characterization of cellobiose dehydrogenases from the white rot fungus Trametes versicolor. Appl Environ Microbiol 1996, 62:4417-4427.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4417-4427
    • Roy, B.P.1    Dumonceaux, T.2    Koukoulas, A.A.3    Archibald, F.S.4
  • 71
    • 33746449143 scopus 로고    scopus 로고
    • Purification and characterization of cellobiose dehydrogenase from white-rot basidiomycete Trametes hirsuta
    • Nakagame S., Furujyo A., Sugiura J. Purification and characterization of cellobiose dehydrogenase from white-rot basidiomycete Trametes hirsuta. Biosci Biotechnol Biochem 2006, 70:1629-1635.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1629-1635
    • Nakagame, S.1    Furujyo, A.2    Sugiura, J.3
  • 72
    • 0346024080 scopus 로고    scopus 로고
    • Isolation and characterization of a cellobiose dehydrogenase formed by a nonsporulating mycelial fungus INBI 2-26(-)
    • Karapetyan K.N., Yachkova S.N., Vasil'chenko L.G., Borzykh M.N., Rabinovich M.L. Isolation and characterization of a cellobiose dehydrogenase formed by a nonsporulating mycelial fungus INBI 2-26(-). Appl Biochem Microbiol 2003, 39:564-572.
    • (2003) Appl Biochem Microbiol , vol.39 , pp. 564-572
    • Karapetyan, K.N.1    Yachkova, S.N.2    Vasil'chenko, L.G.3    Borzykh, M.N.4    Rabinovich, M.L.5
  • 73
    • 2342432133 scopus 로고    scopus 로고
    • Characterisation of cellobiose dehydrogenases from the white-rot fungi Trametes pubescens and Trametes villosa
    • Ludwig R., Salamon A., Varga J., Zamocky M., Peterbauer C.K., Kulbe K.D., et al. Characterisation of cellobiose dehydrogenases from the white-rot fungi Trametes pubescens and Trametes villosa. Appl Microbiol Biotechnol 2004, 64:213-222.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 213-222
    • Ludwig, R.1    Salamon, A.2    Varga, J.3    Zamocky, M.4    Peterbauer, C.K.5    Kulbe, K.D.6
  • 74
    • 84874490704 scopus 로고    scopus 로고
    • Chemical modifications of laccase from white-rot basidiomycete Cerrena unicolor
    • Kucharzyk K.H., Janusz G., Karczmarczyk I., Rogalski J. Chemical modifications of laccase from white-rot basidiomycete Cerrena unicolor. Appl Biochem Biotechnol 2012, 168:1989-2003.
    • (2012) Appl Biochem Biotechnol , vol.168 , pp. 1989-2003
    • Kucharzyk, K.H.1    Janusz, G.2    Karczmarczyk, I.3    Rogalski, J.4
  • 76
    • 0037446732 scopus 로고    scopus 로고
    • Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Rotsaert F.A.J., Renganathan V., Gold M.H. Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium. Biochemistry 2003, 42:4049-4056.
    • (2003) Biochemistry , vol.42 , pp. 4049-4056
    • Rotsaert, F.A.J.1    Renganathan, V.2    Gold, M.H.3
  • 77
    • 0036068415 scopus 로고    scopus 로고
    • Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions
    • Galhaup C., Goller S., Peterbauer C.K., Strauss J., Haltrich D. Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. Microbiology 2002, 148:2159-2169.
    • (2002) Microbiology , vol.148 , pp. 2159-2169
    • Galhaup, C.1    Goller, S.2    Peterbauer, C.K.3    Strauss, J.4    Haltrich, D.5
  • 78
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 2011, 8:785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 80
    • 0029928876 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium
    • Li B., Nagalla S.R., Renganathan V. Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium. Appl Environ Microbiol 1996, 62:1329-1335.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1329-1335
    • Li, B.1    Nagalla, S.R.2    Renganathan, V.3
  • 81
    • 0027237670 scopus 로고
    • Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium
    • Habu N., Samejima M., Dean J.F., Eriksson K.E. Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium. FEBS Lett 1993, 327:161-164.
    • (1993) FEBS Lett , vol.327 , pp. 161-164
    • Habu, N.1    Samejima, M.2    Dean, J.F.3    Eriksson, K.E.4
  • 82
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase-a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
    • Zamocky M., Ludwig R., Peterbauer C., Hallberg B.M., Divne C., Nicholls P., et al. Cellobiose dehydrogenase-a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi. Curr Protein Pept Sci 2006, 7:255-280.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 255-280
    • Zamocky, M.1    Ludwig, R.2    Peterbauer, C.3    Hallberg, B.M.4    Divne, C.5    Nicholls, P.6
  • 83
    • 0021235185 scopus 로고
    • Lariat RNA's as intermediates and products in the splicing of messenger RNA precursors
    • Padgett R.A., Konarska M.M., Grabowski P.J., Hardy S.F., Sharp P.A. Lariat RNA's as intermediates and products in the splicing of messenger RNA precursors. Science 1984, 225:898-903.
    • (1984) Science , vol.225 , pp. 898-903
    • Padgett, R.A.1    Konarska, M.M.2    Grabowski, P.J.3    Hardy, S.F.4    Sharp, P.A.5
  • 84
    • 0030980047 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase from Phanerochaete chrysosporium is encoded by two allelic variants
    • Li B., Nagalla S.R., Renganathan V. Cellobiose dehydrogenase from Phanerochaete chrysosporium is encoded by two allelic variants. Appl Environ Microbiol 1997, 63:796-799.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 796-799
    • Li, B.1    Nagalla, S.R.2    Renganathan, V.3
  • 85
    • 84859294636 scopus 로고    scopus 로고
    • Antioxidant activity of the extracts from Pycnoporus sanguineus mycelium
    • Borderes J., Costa A., Guedes A., Tavares L.B.B. Antioxidant activity of the extracts from Pycnoporus sanguineus mycelium. Braz Arch Biol Technol 2011, 54:1167-1174.
    • (2011) Braz Arch Biol Technol , vol.54 , pp. 1167-1174
    • Borderes, J.1    Costa, A.2    Guedes, A.3    Tavares, L.B.B.4
  • 86
    • 0026674531 scopus 로고
    • Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium
    • Kremer S.M., Wood P.M. Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium. Eur J Biochem 1992, 208:807-814.
    • (1992) Eur J Biochem , vol.208 , pp. 807-814
    • Kremer, S.M.1    Wood, P.M.2
  • 87
    • 0030812766 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase, an active agent in cellulose depolymerization
    • Mansfield S.D., De Jong E., Saddler J.N. Cellobiose dehydrogenase, an active agent in cellulose depolymerization. Appl Environ Microbiol 1997, 63:3804-3809.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3804-3809
    • Mansfield, S.D.1    De Jong, E.2    Saddler, J.N.3
  • 88
    • 0031855898 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase from Schizophyllum commune: purification and study of some catalytic, inactivation and cellulose binding properties
    • Fang J., Liu W., Gao P.J. Cellobiose dehydrogenase from Schizophyllum commune: purification and study of some catalytic, inactivation and cellulose binding properties. Arch Biochem Biophys 1998, 353:37-46.
    • (1998) Arch Biochem Biophys , vol.353 , pp. 37-46
    • Fang, J.1    Liu, W.2    Gao, P.J.3


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