메뉴 건너뛰기




Volumn 50, Issue 1, 2010, Pages 72-82

Two laccase isoforms of the basidiomycete Cerrena unicolor VKMF-3196. Induction, isolation and properties

Author keywords

Cerrena unicolor; Laccase induction; N terminal amino acid sequences; Purification of isoforms

Indexed keywords

CARBOHYDRATE; FUNGAL PROTEIN; ISOENZYME; LACCASE;

EID: 77049102400     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.200900382     Document Type: Article
Times cited : (38)

References (45)
  • 1
    • 34848846870 scopus 로고    scopus 로고
    • Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
    • Sakurai, T. and Kataoka, K., 2007. Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. The Chemical Record, 7, 220-229.
    • (2007) The Chemical Record , vol.7 , pp. 220-229
    • Sakurai, T.1    Kataoka, K.2
  • 2
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston, C.F., 1994. The structure and function of fungal laccases. Microbiology, 140, 19-26.
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 3
    • 33645027271 scopus 로고    scopus 로고
    • Fungal laccases - occurrence and properties
    • Baldrian, P., 2006. Fungal laccases - occurrence and properties. FEMS Microbiol Rev., 30, 215-242.
    • (2006) Fems Microbiol Rev , vol.30 , pp. 215-242
    • Baldrian, P.1
  • 4
  • 5
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: New functions for an old enzyme
    • Mayer, A.M. and Staples, R.C., 2002. Laccase: new functions for an old enzyme. Phytochemistry, 60, 551-565.
    • (2002) Phytochemistry , vol.60 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 7
    • 0029947617 scopus 로고    scopus 로고
    • The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: Purification and characterization of the laccase
    • Eggert, C., Temp, U. and Eriksson, K.-E.L., 1996. The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase. Appl. Environ. Microbiol., 62, 1151-1158.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 1151-1158
    • Eggert, C.1    Temp, U.2    Eriksson, K.-E.L.3
  • 8
    • 0000326191 scopus 로고    scopus 로고
    • Laccases: A useful group of oxidoreductive enzymes
    • Gianfreda, L., Xu, F. and Bollag, J.-M., 1999. Laccases: a useful group of oxidoreductive enzymes. J. Bioremediation, 3, 1-25.
    • (1999) J. Bioremediation , vol.3 , pp. 1-25
    • Gianfreda, L.1    Xu, F.2    Bollag, J.-M.3
  • 9
    • 1042290552 scopus 로고    scopus 로고
    • Biotransformation of soil humic acids by blue laccase of Panus tigrinus 8/18: An in vitro study
    • Zavarzina, A.G., Leontievsky, A.A., Golovleva, L.A. and Trofimov, S.Y., 2004. Biotransformation of soil humic acids by blue laccase of Panus tigrinus 8/18: an in vitro study. Soil Biol. Biochem., 36, 359-369.
    • (2004) Soil Biol. Biochem , vol.36 , pp. 359-369
    • Zavarzina, A.G.1    Leontievsky, A.A.2    Golovleva, L.A.3    Trofimov, S.Y.4
  • 10
    • 0034788827 scopus 로고    scopus 로고
    • Fungal laccase: Properties and activity on lignin
    • Leonowicz, A., Cho, N.-S., Luterek, J. et al., 2001. Fungal laccase: properties and activity on lignin. J. Basic. Micro-biol., 41, 185-227.
    • (2001) J. Basic. Micro-biol , vol.41 , pp. 185-227
    • Leonowicz, A.1    Cho, N.-S.2    Luterek, J.3
  • 12
    • 0000232190 scopus 로고
    • Laccase from sycamore maple (Acer pseudoplatanus) polymerizes monolignols
    • Sterjiades, R., Dean, J.F.D. and Eriksson, K.-E., 1992. Laccase from sycamore maple (Acer pseudoplatanus) polymerizes monolignols. Plant Physiol., 99, 1162-1168.
    • (1992) Plant Physiol , vol.99 , pp. 1162-1168
    • Sterjiades, R.1    Dean, J.F.D.2    Eriksson, K.-E.3
  • 13
    • 0027240897 scopus 로고
    • A laccase associated with lifgnification in Loblolly pine xylem
    • Bao, W., O'Malley, D.M., Whetten, R. and Sederoff, R.R., 1993. A laccase associated with lifgnification in Loblolly pine xylem. Science, 260, 672-674.
    • (1993) Science , vol.260 , pp. 672-674
    • Bao, W.1    O'Malley, D.M.2    Whetten, R.3    Sederoff, R.R.4
  • 14
    • 0033815820 scopus 로고    scopus 로고
    • Oxidase activity in lignifying xylem of taxonomically diverse range of trees: Identification of a conifer laccase
    • Richardson, A., Duncan, J. and McDougall, G.J., 2000. Oxidase activity in lignifying xylem of taxonomically diverse range of trees: identification of a conifer laccase. Tree Physiol., 20, 1039-1047.
    • (2000) Tree Physiol , vol.20 , pp. 1039-1047
    • Richardson, A.1    Duncan, J.2    McDougall, G.J.3
  • 16
    • 0035940514 scopus 로고    scopus 로고
    • Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays
    • De Gregorio, E., Spellman, P.T., Rubin, G.M. and Lemaitre, B., 2001 Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. Proc Nat Acad Sci USA, 98, 12590-12595.
    • (2001) Proc Nat Acad Sci Usa , vol.98 , pp. 12590-12595
    • de Gregorio, E.1    Spellman, P.T.2    Rubin, G.M.3    Lemaitre, B.4
  • 17
    • 0035819288 scopus 로고    scopus 로고
    • Oxidative conjugation of catechols with proteins in insect skeletal systems
    • Kramer, K.J., Kanost, M.R., Hopkins, T.L., Jiang, H., Zhu, Y.C. et al., 2001. Oxidative conjugation of catechols with proteins in insect skeletal systems. Tetrahedron, 57, 385-392.
    • (2001) Tetrahedron , vol.57 , pp. 385-392
    • Kramer, K.J.1    Kanost, M.R.2    Hopkins, T.L.3    Jiang, H.4    Zhu, Y.C.5
  • 18
    • 0742305629 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae, Insect Biochem
    • Dittmer, N.T., Suderman, R.J., Jiang, H., Zhu, Y.C., Gorman, M.J. et al., 2004. Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae, Insect Biochem. Mol. Biol., 34, 29-41.
    • (2004) Mol. Biol , vol.34 , pp. 29-41
    • Dittmer, N.T.1    Suderman, R.J.2    Jiang, H.3    Zhu, Y.C.4    Gorman, M.J.5
  • 19
    • 0037333713 scopus 로고    scopus 로고
    • Laccases and their occurence in prokaryotes
    • Claus, H., 2003. Laccases and their occurence in prokaryotes. Arch. Microbiol., 179, 145-150.
    • (2003) Arch. Microbiol , vol.179 , pp. 145-150
    • Claus, H.1
  • 20
    • 33746142419 scopus 로고    scopus 로고
    • Industrial and bio-technological applications of laccases
    • Couto, S.R. and Herrera, J.L.T., 2006. Industrial and bio-technological applications of laccases. Biotechnology Advanc., 24, 500-513.
    • (2006) Biotechnology Advanc , vol.24 , pp. 500-513
    • Couto, S.R.1    Herrera, J.L.T.2
  • 21
    • 31144463335 scopus 로고    scopus 로고
    • The white-rot fungus Cerrena unicolor strain 137 produces two laccase isoforms with different physico-chemical and catalytic properties
    • Michniewicz, A., Ullrich, R., Ledakowicz, S. and Hofrichter, M., 2006. The white-rot fungus Cerrena unicolor strain 137 produces two laccase isoforms with different physico-chemical and catalytic properties. Appl. Microbiol. Bio-technol., 69, 682-688.
    • (2006) Appl. Microbiol. Bio-technol , vol.69 , pp. 682-688
    • Michniewicz, A.1    Ullrich, R.2    Ledakowicz, S.3    Hofrichter, M.4
  • 22
    • 0642336210 scopus 로고    scopus 로고
    • Comparative study of the extracellular laccases from Cerrena unicolor 059, 0784 and Pleurotus oastreatus 0432
    • (Translated from Prikladnaya Biokhimiya i Mikrobiologiya)
    • Stepanova, E.V., Pegasova, T.V., Gavrilova, V.P., Landesman, E.O. and Koroleva, O.V., 2003. Comparative study of the extracellular laccases from Cerrena unicolor 059, 0784 and Pleurotus oastreatus 0432. Appl. Biochem. Microbiol. (Translated from Prikladnaya Biokhimiya i Mikrobiologiya), 39, 427-434.
    • (2003) Appl. Biochem. Microbiol , vol.39 , pp. 427-434
    • Stepanova, E.V.1    Pegasova, T.V.2    Gavrilova, V.P.3    Landesman, E.O.4    Koroleva, O.V.5
  • 23
    • 0037143262 scopus 로고    scopus 로고
    • Purification and characterization of a laccase from Cerrena unicolor and its reactivity in lignin degradation
    • Kim, Y., Cho, N.S., Eom, T.J. and Shin, W., 2002. Purification and characterization of a laccase from Cerrena unicolor and its reactivity in lignin degradation. Bull. Korean Chem. Soc., 23, 985-989.
    • (2002) Bull. Korean Chem. Soc , vol.23 , pp. 985-989
    • Kim, Y.1    Cho, N.S.2    Eom, T.J.3    Shin, W.4
  • 24
    • 0017879346 scopus 로고
    • Influents of cultural parameters on lignin metabolism by Phanerochaete chrysosporium
    • Kirk, T.K., Schultz, E., Connors, W.J., Lorenz, L.F. and Zeikus, J.G., 1978. Influents of cultural parameters on lignin metabolism by Phanerochaete chrysosporium. Arch. Microbiol., 177, 277-285.
    • (1978) Arch. Microbiol , vol.177 , pp. 277-285
    • Kirk, T.K.1    Schultz, E.2    Connors, W.J.3    Lorenz, L.F.4    Zeikus, J.G.5
  • 25
    • 34250238292 scopus 로고
    • Relationship of nitrogen to the outset and suppression of ligninolytic activity and secondary metabolism in Phanerochaete chrysosporium
    • Fenn, P. and Kirk, T.K., 1981. Relationship of nitrogen to the outset and suppression of ligninolytic activity and secondary metabolism in Phanerochaete chrysosporium. Arch. Microbiol., 130, 59-65.
    • (1981) Arch. Microbiol , vol.130 , pp. 59-65
    • Fenn, P.1    Kirk, T.K.2
  • 26
    • 0032145444 scopus 로고    scopus 로고
    • Purification and characterization of peroxidases from the dye-decolorizing fungus Bjerkandera adusta
    • Heinfling, A., Martinez, A.T., Martinez, M.J., Bergbauer, M. and Szewzyc, U., 1998. Purification and characterization of peroxidases from the dye-decolorizing fungus Bjerkandera adusta. FEMS Microbiol. Lett., 165, 43-50.
    • (1998) Fems Microbiol. Lett , vol.165 , pp. 43-50
    • Heinfling, A.1    Martinez, A.T.2    Martinez, M.J.3    Bergbauer, M.4    Szewzyc, U.5
  • 27
    • 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., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0021180566 scopus 로고
    • Comparative studies of extracellular fungal laccases
    • Bollag, J.-M. and Leonowicz, A., 1984. Comparative studies of extracellular fungal laccases. Appl Env Microbiol., 48, 849-854.
    • (1984) Appl Env Microbiol , vol.48 , pp. 849-854
    • Bollag, J.-M.1    Leonowicz, A.2
  • 31
    • 0001012871 scopus 로고
    • Differently-induced extracellular phenol oxidases from Pleurotus ostreatus
    • Garzillo, A.M.V., Di Paolo, S., Burla, G. and Buonocore, V., 1992. Differently-induced extracellular phenol oxidases from Pleurotus ostreatus. Phytochemistry, 31, 3685-3690.
    • (1992) Phytochemistry , vol.31 , pp. 3685-3690
    • Garzillo, A.M.V.1    Di Paolo, S.2    Burla, G.3    Buonocore, V.4
  • 32
    • 0033451006 scopus 로고    scopus 로고
    • Enhanced production of laccase in Trametes vesicolor by the addition of ethanol
    • Lee, I.-Y., Jung, K.-H., Lee, C.-H. and Park, Y.-H., 1999. Enhanced production of laccase in Trametes vesicolor by the addition of ethanol. Biotechnol. Letters, 21, 965-968.
    • (1999) Biotechnol. Letters , vol.21 , pp. 965-968
    • Lee, I.-Y.1    Jung, K.-H.2    Lee, C.-H.3    Park, Y.-H.4
  • 33
    • 0037005954 scopus 로고    scopus 로고
    • Copper and cadmium increase laccase activity in Pleurotus ostreatus
    • Baldrian, P. and Gabriel, J., 2002. Copper and cadmium increase laccase activity in Pleurotus ostreatus. FEMS Microbiol. Letters, 206, 69-74.
    • (2002) Fems Microbiol. Letters , vol.206 , pp. 69-74
    • Baldrian, P.1    Gabriel, J.2
  • 34
    • 0034976251 scopus 로고    scopus 로고
    • Ligninolytic enzyme production in selected sub-tropical white rot fungi under different culture conditions
    • Tekere, M., Zvauya, R. and Read, J.S., 2001. Ligninolytic enzyme production in selected sub-tropical white rot fungi under different culture conditions. J. Basic. Microbiol., 41, 115-129.
    • (2001) J. Basic. Microbiol , vol.41 , pp. 115-129
    • Tekere, M.1    Zvauya, R.2    Read, J.S.3
  • 35
    • 0030848882 scopus 로고    scopus 로고
    • Regulation of laccase gene transcription in Trametes versicolor
    • Collins, P.J. and Dobson, A.D.W., 1997. Regulation of laccase gene transcription in Trametes versicolor. Appl. Env. Microbiol., 63, 3444-3450.
    • (1997) Appl. Env. Microbiol , vol.63 , pp. 3444-3450
    • Collins, P.J.1    Dobson, A.D.W.2
  • 36
    • 0036068415 scopus 로고    scopus 로고
    • Characterization of major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions
    • Galhaup, C., Goller, S., Peterbauer, C.K., Strauss, J. and Haltrich, D., 2002. Characterization of major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. Microbiology, 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
  • 37
    • 0032472307 scopus 로고    scopus 로고
    • Catalytic behavior and detoxifying ability of a laccase from the fungal strain Cerrena unicolor
    • Gianfreda, L., Sannino, F., Filazzola, M.T. and Leonowicz, A., 1998. Catalytic behavior and detoxifying ability of a laccase from the fungal strain Cerrena unicolor. J. Molec. Catal. B: Enzymatic, 4, 13-23.
    • (1998) J. Molec. Catal. B: Enzymatic , vol.4 , pp. 13-23
    • Gianfreda, L.1    Sannino, F.2    Filazzola, M.T.3    Leonowicz, A.4
  • 39
    • 33746682511 scopus 로고    scopus 로고
    • Thermostability of native and pegylated Myceliophthora thermophila laccase in aqueous and mixed solvents
    • Lopez-Cruz, J.I., Viniegra-Gonzalez, G. and Hernandez-Arana, A., 2006. Thermostability of native and pegylated Myceliophthora thermophila laccase in aqueous and mixed solvents. Bioconjugate Chem., 17, 1093-1098.
    • (2006) Bioconjugate Chem , vol.17 , pp. 1093-1098
    • Lopez-Cruz, J.I.1    Viniegra-Gonzalez, G.2    Hernandez-Arana, A.3
  • 41
    • 0028898977 scopus 로고
    • Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: Comparison with ascorbate oxidase
    • Agostinelli, E., Cervoni, L., Giartosio, A. and Morpurgot, L., 1995. Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: comparison with ascorbate oxidase. Biochem. J., 306, 697-702.
    • (1995) Biochem. J , vol.306 , pp. 697-702
    • Agostinelli, E.1    Cervoni, L.2    Giartosio, A.3    Morpurgot, L.4
  • 42
    • 0027400929 scopus 로고
    • N-linked carbohydrate chains protect laccase III from proteolysis in Coriolus versicolor
    • Yoshitake, A., Katayama, Y., Nakamura, M., Kawai, S. and Morioshi, N., 1993. N-linked carbohydrate chains protect laccase III from proteolysis in Coriolus versicolor. J. Gen. Microbiol., 139, 179-185.
    • (1993) J. Gen. Microbiol , vol.139 , pp. 179-185
    • Yoshitake, A.1    Katayama, Y.2    Nakamura, M.3    Kawai, S.4    Morioshi, N.5
  • 43
    • 0028961640 scopus 로고
    • Production and characterization of laccase from Botrytis cinerea 61-34
    • Slomczynski, D., Nakas, J.P. and Tanenbaum, S.W., 1995. Production and characterization of laccase from Botrytis cinerea 61-34. Appl. Environ. Micribiol., 61, 907-912.
    • (1995) Appl. Environ. Micribiol , vol.61 , pp. 907-912
    • Slomczynski, D.1    Nakas, J.P.2    Tanenbaum, S.W.3
  • 44
    • 31544432060 scopus 로고    scopus 로고
    • Shifting the optimal pH of activity for a laccase from the fungus Trametes versicolor by structure-based mutagenesis
    • Madzak, C., Mimmi, M.C., Caminade, E., Brault, A., Baumberger, S. et al., 2006. Shifting the optimal pH of activity for a laccase from the fungus Trametes versicolor by structure-based mutagenesis. PEDS, 19(2), 77-84.
    • (2006) PEDS , vol.19 , Issue.2 , pp. 77-84
    • Madzak, C.1    Mimmi, M.C.2    Caminade, E.3    Brault, A.4    Baumberger, S.5
  • 45
    • 39549084091 scopus 로고    scopus 로고
    • Conversion of poly-chlorophenols by laccases with 1-hydroxybenzotriazole as a mediator
    • (Translated from Prikladnaya Biokhimiya i Mikrobiologiya)
    • Lisov, A.V., Pozhidaeva, Z.A., Stepanova, E.V., Koroleva, O.V. and Leontievsky, A.A., 2007. Conversion of poly-chlorophenols by laccases with 1-hydroxybenzotriazole as a mediator. Appl. Biochem. Microbiol. (Translated from Prikladnaya Biokhimiya i Mikrobiologiya), 43, 691-694.
    • (2007) Appl. Biochem. Microbiol , vol.43 , pp. 691-694
    • Lisov, A.V.1    Pozhidaeva, Z.A.2    Stepanova, E.V.3    Koroleva, O.V.4    Leontievsky, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.