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Volumn 64, Issue 3, 2004, Pages 346-352

Natural and recombinant fungal laccases for paper pulp bleaching

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL ENZYME; LACCASE; RECOMBINANT ENZYME;

EID: 2442428319     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-003-1468-3     Document Type: Article
Times cited : (101)

References (29)
  • 1
    • 0030838432 scopus 로고    scopus 로고
    • Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae
    • Berka RM, Schneider P, Golightly EJ, Brown SH, Madden M, Brown KM, Halkier T, Mondorf K, Xu F (1997) Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Appl Environ Microbiol 63:3151-3157
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3151-3157
    • Berka, R.M.1    Schneider, P.2    Golightly, E.J.3    Brown, S.H.4    Madden, M.5    Brown, K.M.6    Halkier, T.7    Mondorf, K.8    Xu, F.9
  • 2
    • 0028291911 scopus 로고
    • Fractionation of subcellular membranes of the secretory pathway from the peroxidase-producing white rot fungus Phanerochaete chrysosporium
    • Bonnarme P, Moukha S, Moreau P, Record E, Lesage L, Cassagne C, Asther M (1994) Fractionation of subcellular membranes of the secretory pathway from the peroxidase-producing white rot fungus Phanerochaete chrysosporium. FEMS Microbiol Lett 120:155-162
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 155-162
    • Bonnarme, P.1    Moukha, S.2    Moreau, P.3    Record, E.4    Lesage, L.5    Cassagne, C.6    Asther, M.7
  • 3
    • 3042846929 scopus 로고    scopus 로고
    • Electrochemical analysis of the interactions of laccase mediators with lignin model compounds
    • Bourbonnais R, Leech D, Paice MG (1998) Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim Biophys Acta 1379:381-390
    • (1998) Biochim Biophys Acta , vol.1379 , pp. 381-390
    • Bourbonnais, R.1    Leech, D.2    Paice, M.G.3
  • 4
    • 4243542277 scopus 로고    scopus 로고
    • History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lygnozym-process)
    • Call HP, Mücke I (1997) History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lygnozym-process). J Biotechnol 53:163-202
    • (1997) J Biotechnol , vol.53 , pp. 163-202
    • Call, H.P.1    Mücke, I.2
  • 7
    • 0029947617 scopus 로고    scopus 로고
    • The lignolytic system of the white rot fungus Pycnoporus cinnabarinus: Purification and characterization of the laccase
    • Eggert C, Temp U, Eriksson KE (1996) The lignolytic 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.3
  • 8
    • 0037127592 scopus 로고    scopus 로고
    • Comparing the catalytic efficiency of some mediators of laccase
    • Fabbrini M, Galli C, Gentili P (2002) Comparing the catalytic efficiency of some mediators of laccase. J Mol Catal B Enzym 16:231-240
    • (2002) J Mol Catal B Enzym , vol.16 , pp. 231-240
    • Fabbrini, M.1    Galli, C.2    Gentili, P.3
  • 9
    • 0000326191 scopus 로고    scopus 로고
    • Laccases: A useful group of oxidoreductive enzymes
    • Gianfreda L, Xu F, Bollag JM (1999) Laccases: a useful group of oxidoreductive enzymes. Bioremediation J 3:1-25
    • (1999) Bioremediation J , vol.3 , pp. 1-25
    • Gianfreda, L.1    Xu, F.2    Bollag, J.M.3
  • 12
    • 0033971693 scopus 로고    scopus 로고
    • Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems
    • Johannes C, Majcherczyk A (2000) Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems. Appl Environ Microbiol 66:524-528
    • (2000) Appl Environ Microbiol , vol.66 , pp. 524-528
    • Johannes, C.1    Majcherczyk, A.2
  • 13
    • 0036296326 scopus 로고    scopus 로고
    • Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: Insights into the structural relationship with the cupredoxins and the multi copper proteins
    • Kanbi LD, Antonyuk S, Hough MA, Hall JF, Dodd FE, Hasnain SS (2002) Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins. J Mol Biol 320:263-275
    • (2002) J Mol Biol , vol.320 , pp. 263-275
    • Kanbi, L.D.1    Antonyuk, S.2    Hough, M.A.3    Hall, J.F.4    Dodd, F.E.5    Hasnain, S.S.6
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, UK (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
  • 15
    • 84957298651 scopus 로고
    • Thioacidolysis of poplar lignins: Identification of monomeric syringyl products and characterization of guaiacyl-syringyl lignin fractions
    • Lapierre C, Monties B, Rolando C (1986) Thioacidolysis of poplar lignins: identification of monomeric syringyl products and characterization of guaiacyl-syringyl lignin fractions. Holzforschung 40:113-118
    • (1986) Holzforschung , vol.40 , pp. 113-118
    • Lapierre, C.1    Monties, B.2    Rolando, C.3
  • 16
    • 0033050135 scopus 로고    scopus 로고
    • Comparison of fungal laccases and redox mediators in oxidation of a non phenolic lignin model compound
    • Li K, Xu F, Eriksson KEL (1999) Comparison of fungal laccases and redox mediators in oxidation of a non phenolic lignin model compound. Appl Environ Microbiol 65:2654-2660
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2654-2660
    • Li, K.1    Xu, F.2    Eriksson, K.E.L.3
  • 18
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: New functions for an old enzyme
    • Mayer AM, Staples RC (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
  • 19
    • 0033846798 scopus 로고    scopus 로고
    • Isolation of a new laccase isoform from the white-rot fungi Pycnoporus cinnabarinus strain ss3
    • Otterbein L, Record E, Chereau D, Herpoël I, Asther M, Moukha S (2000) Isolation of a new laccase isoform from the white-rot fungi Pycnoporus cinnabarinus strain ss3. Can J Microbiol 46:759-763
    • (2000) Can J Microbiol , vol.46 , pp. 759-763
    • Otterbein, L.1    Record, E.2    Chereau, D.3    Herpoël, I.4    Asther, M.5    Moukha, S.6
  • 20
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers
    • Piontek K, Antorini M, Choinowski T (2002) Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers. J Biol Chem 40:37663-37669
    • (2002) J Biol Chem , vol.40 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 21
    • 0027016529 scopus 로고
    • Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers
    • Punt PJ, Hondel CAAJJ van den (1992) Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers. Methods Enzymol 216:447-457
    • (1992) Methods Enzymol , vol.216 , pp. 447-457
    • Punt, P.J.1    Van Den Hondel, C.A.A.J.J.2
  • 22
    • 0036164150 scopus 로고    scopus 로고
    • Expression of the Pycnoporus cinnabarinus laccase gene in Aspergillus niger and characterization of the recombinant enzyme
    • Record E, Punt PJ, Chamkha M, Labat M, Hondel CAAJJ van den, Asther M (2002) Expression of the Pycnoporus cinnabarinus laccase gene in Aspergillus niger and characterization of the recombinant enzyme. Eur J Biochem 269:602-609
    • (2002) Eur J Biochem , vol.269 , pp. 602-609
    • Record, E.1    Punt, P.J.2    Chamkha, M.3    Labat, M.4    Van Den Hondel, C.A.A.J.J.5    Asther, M.6
  • 23
    • 0001886633 scopus 로고
    • Laccase
    • Lontie R (ed). CRC Press, Boca Raton
    • Reinhammar B (1984) Laccase. In: Lontie R (ed) Copper proteins and copper enzymes, vol 3. CRC Press, Boca Raton, pp 1-35
    • (1984) Copper Proteins and Copper Enzymes , vol.3 , pp. 1-35
    • Reinhammar, B.1
  • 26
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston CF (1994) The structure and function of fungal laccases. Microbiology 140:19-25
    • (1994) Microbiology , vol.140 , pp. 19-25
    • Thurston, C.F.1
  • 27
    • 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. Biochim Biophys Acta 1292:303-311
    • (1996) Biochim Biophys Acta , 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
  • 29
    • 34848826800 scopus 로고
    • Chemistry of lacquer (urichi)
    • Yoshida H (1883) Chemistry of lacquer (urichi). J Chem Soc 43:472-486
    • (1883) J Chem Soc , vol.43 , pp. 472-486
    • Yoshida, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.