메뉴 건너뛰기




Volumn 44, Issue 6-7, 2009, Pages 426-433

Fermentation optimization and characterization of the laccase from Pleurotus ostreatus strain 10969

Author keywords

Laccase; Pleurotus ostreatus; Response surface methodology

Indexed keywords

BIO ENERGIES; BIO-MASS ENERGIES; CONCOMITANT REDUCTIONS; ENZYME PRODUCTIONS; EXTRACELLULAR; FERMENTATION MEDIAS; GROWTH PARAMETERS; HIGH YIELDS; INDUSTRIAL PROCESS; LACCASE; LACCASE ACTIVITIES; LACCASE PRODUCTIONS; MERCAPTOETHANOL; OPTIMIZED CONDITIONS; OPTIMUM CONCENTRATIONS; OPTIMUM PH; PLEUROTUS OSTREATUS; RESPONSE SURFACE METHODOLOGY;

EID: 64449085022     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.02.008     Document Type: Article
Times cited : (103)

References (39)
  • 2
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston C.F. The structure and function of fungal laccases. Microbiology (Reading) 140 (1994) 19-26
    • (1994) Microbiology (Reading) , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 3
    • 0033537844 scopus 로고    scopus 로고
    • Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
    • Camarero S., Sarkar S., Ruiz-Duenas F.J., Martinez M.J., and Martinez A.T. Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J Biol Chem 274 (1999) 10324-10330
    • (1999) J Biol Chem , vol.274 , pp. 10324-10330
    • Camarero, S.1    Sarkar, S.2    Ruiz-Duenas, F.J.3    Martinez, M.J.4    Martinez, A.T.5
  • 4
    • 0023478845 scopus 로고
    • Enzymatic"combustion": the microbial degradation of lignin
    • Kirk T.K., and Farrell R.L. Enzymatic"combustion": the microbial degradation of lignin. Annu Rev Microbiol 41 (1987) 465-501
    • (1987) Annu Rev Microbiol , vol.41 , pp. 465-501
    • Kirk, T.K.1    Farrell, R.L.2
  • 5
    • 0026662089 scopus 로고
    • Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii
    • Guillen F., Martinez A.T., and Martinez M.J. Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii. Eur J Biochem 209 (1992) 603-611
    • (1992) Eur J Biochem , vol.209 , pp. 603-611
    • Guillen, F.1    Martinez, A.T.2    Martinez, M.J.3
  • 6
    • 0023264566 scopus 로고
    • 2 production by Phanerochaete chrysosporium
    • 2 production by Phanerochaete chrysosporium. J Bacteriol 169 (1987) 2195-2201
    • (1987) J Bacteriol , vol.169 , pp. 2195-2201
    • Kersten, P.J.1    Kirk, T.K.2
  • 7
    • 0032840163 scopus 로고    scopus 로고
    • Laccase-catalyzed decolorization of synthetic dyes
    • Wong Y., and Yu J. Laccase-catalyzed decolorization of synthetic dyes. Water Res 33 (1999) 3512-3520
    • (1999) Water Res , vol.33 , pp. 3512-3520
    • Wong, Y.1    Yu, J.2
  • 8
    • 84987057619 scopus 로고
    • On the chemistry of lignin biodegradation
    • Schoemaker H.E. On the chemistry of lignin biodegradation. Recl Trav Chim Pays-Bas 109 (1990) 255-272
    • (1990) Recl Trav Chim Pays-Bas , vol.109 , pp. 255-272
    • Schoemaker, H.E.1
  • 9
    • 0027195338 scopus 로고
    • The Aspergillus nidulans yA gene is regulated by abaA
    • Aramayo R., and Timberlake W.E. The Aspergillus nidulans yA gene is regulated by abaA. EMBO J 12 (1993) 2039
    • (1993) EMBO J , vol.12 , pp. 2039
    • Aramayo, R.1    Timberlake, W.E.2
  • 10
    • 0025353560 scopus 로고
    • Sequence and molecular structure of the Aspergillus nidulans yA (laccase I) gene
    • Aramayo R., and Timberlake W.E. Sequence and molecular structure of the Aspergillus nidulans yA (laccase I) gene. Nucleic Acids Res 18 (1990) 3415
    • (1990) Nucleic Acids Res , vol.18 , pp. 3415
    • Aramayo, R.1    Timberlake, W.E.2
  • 11
    • 0001722912 scopus 로고
    • Repression of laccase formation in Botrytis cinerea and its possible relation to phytopathogenicity
    • Nun B., Lev A.T., Harel E., and Mayer A.M. Repression of laccase formation in Botrytis cinerea and its possible relation to phytopathogenicity. Phytochemistry 27 (1988) 2505-2509
    • (1988) Phytochemistry , vol.27 , pp. 2505-2509
    • Nun, B.1    Lev, A.T.2    Harel, E.3    Mayer, A.M.4
  • 12
    • 33748091360 scopus 로고    scopus 로고
    • Laccase induction in fungi and laccase/N-OH mediator systems applied in paper mill effluent
    • Minussi R.C., Pastore G.M., and Durán N. Laccase induction in fungi and laccase/N-OH mediator systems applied in paper mill effluent. Bioresour Technol 98 (2007) 158-164
    • (2007) Bioresour Technol , vol.98 , pp. 158-164
    • Minussi, R.C.1    Pastore, G.M.2    Durán, N.3
  • 14
    • 33645027271 scopus 로고    scopus 로고
    • Fungal laccases-occurrence and properties
    • Baldrian P. Fungal laccases-occurrence and properties. FEMS Microbiol Rev 30 (2006) 215-242
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 215-242
    • Baldrian, P.1
  • 16
    • 0042705205 scopus 로고    scopus 로고
    • Lacasse: A useful enzyme for industrial applications
    • Kruus K., and Laccase:. A useful enzyme for industrial applications. Kemia Kemi 27 (2000) 184-187
    • (2000) Kemia Kemi , vol.27 , pp. 184-187
    • Kruus, K.1
  • 17
  • 18
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: blue enzymes for green chemistry
    • Riva S. Laccases: blue enzymes for green chemistry. Trends Biotechnol 24 (2006) 219-226
    • (2006) Trends Biotechnol , vol.24 , pp. 219-226
    • Riva, S.1
  • 19
    • 33746142419 scopus 로고    scopus 로고
    • Industrial and biotechnological applications of laccases: a review
    • Rodríguez Couto S., and Toca Herrera J.L. Industrial and biotechnological applications of laccases: a review. Biotechnol Adv 24 (2006) 500-513
    • (2006) Biotechnol Adv , vol.24 , pp. 500-513
    • Rodríguez Couto, S.1    Toca Herrera, J.L.2
  • 20
    • 0142185232 scopus 로고    scopus 로고
    • Potential use of oxidative enzymes for the detoxification of organic pollutants
    • Torres E., Bustos-Jaimes I., and Borgne Le S. Potential use of oxidative enzymes for the detoxification of organic pollutants. Appl Catal B: Environ 46 (2003) 1-15
    • (2003) Appl Catal B: Environ , vol.46 , pp. 1-15
    • Torres, E.1    Bustos-Jaimes, I.2    Borgne Le, S.3
  • 21
    • 4043151312 scopus 로고    scopus 로고
    • A high sensitivity amperometric biosensor using a monomolecular layer of laccase as biorecognition element
    • Vianello F., Cambria A., Ragusa S., Cambria M.T., Zennaro L., and Rigo A. A high sensitivity amperometric biosensor using a monomolecular layer of laccase as biorecognition element. Biosens. Bioelectron 20 (2004) 315-321
    • (2004) Biosens. Bioelectron , vol.20 , pp. 315-321
    • Vianello, F.1    Cambria, A.2    Ragusa, S.3    Cambria, M.T.4    Zennaro, L.5    Rigo, A.6
  • 22
    • 29044440810 scopus 로고    scopus 로고
    • Applications of oxidoreductases: recent progress
    • Xu F. Applications of oxidoreductases: recent progress. Ind. Biotechnol 1 (2005) 38-50
    • (2005) Ind. Biotechnol , vol.1 , pp. 38-50
    • Xu, F.1
  • 23
    • 43249112307 scopus 로고    scopus 로고
    • Molecular characteristics of two laccase from the basidiomycete fungus Polyporus brumalis
    • Ryu S.H., Lee A.Y., and Kim M. Molecular characteristics of two laccase from the basidiomycete fungus Polyporus brumalis. J Microbiol 46 (2008) 62-69
    • (2008) J Microbiol , vol.46 , pp. 62-69
    • Ryu, S.H.1    Lee, A.Y.2    Kim, M.3
  • 25
    • 64449085382 scopus 로고    scopus 로고
    • Chinese Agricultural Technology Press, Beijing
    • Lin Z.X., and Lin H. Juncao technology (2003), Chinese Agricultural Technology Press, Beijing
    • (2003) Juncao technology
    • Lin, Z.X.1    Lin, H.2
  • 26
    • 34548269068 scopus 로고    scopus 로고
    • The chemical structure and application of lignin
    • Tao Y.Z., and Guan Y.T. The chemical structure and application of lignin. J Cell Sci Technol 11 001 (2003) 42-55
    • (2003) J Cell Sci Technol , vol.11 , Issue.1 , pp. 42-55
    • Tao, Y.Z.1    Guan, Y.T.2
  • 27
    • 0036644167 scopus 로고    scopus 로고
    • Fed-batch fermentation of Ganoderma lucidum for hyperproduction of polysaccharide and ganoderic acid
    • Tang Y.J., and Zhong J.J. Fed-batch fermentation of Ganoderma lucidum for hyperproduction of polysaccharide and ganoderic acid. Enzyme Microb Technol 31 (2002) 20-28
    • (2002) Enzyme Microb Technol , vol.31 , pp. 20-28
    • Tang, Y.J.1    Zhong, J.J.2
  • 28
    • 0036158901 scopus 로고    scopus 로고
    • Submerged fermentation of higher fungus Ganoderma lucidum for production of valuable bioactive metabolites-ganoderic acid and polysaccharide
    • Fang Q.H., and Zhong J.J. Submerged fermentation of higher fungus Ganoderma lucidum for production of valuable bioactive metabolites-ganoderic acid and polysaccharide. Biochem Eng J 10 (2002) 61-65
    • (2002) Biochem Eng J , vol.10 , pp. 61-65
    • Fang, Q.H.1    Zhong, J.J.2
  • 29
    • 0034487330 scopus 로고    scopus 로고
    • Use of Box-Behnken design of experiments in the production of manganese peroxidase by Phanerochaete chrysosporium (MTCC 767) and decolorization of crystal violet
    • Annadurai G., Rajesh Babu S., Nagarajan G., and Ragu K. Use of Box-Behnken design of experiments in the production of manganese peroxidase by Phanerochaete chrysosporium (MTCC 767) and decolorization of crystal violet. Bioprocess Biosyst Eng 23 (2000) 715-719
    • (2000) Bioprocess Biosyst Eng , vol.23 , pp. 715-719
    • Annadurai, G.1    Rajesh Babu, S.2    Nagarajan, G.3    Ragu, K.4
  • 30
    • 3042849149 scopus 로고    scopus 로고
    • Optimization of culture conditions and properties of lipase from Penicillium camembertii Thom PG-3
    • Tan T.W., Zhang M., Xu J.L., and Zhang J.J. Optimization of culture conditions and properties of lipase from Penicillium camembertii Thom PG-3. Process Biochem 39 (2004) 1495-1502
    • (2004) Process Biochem , vol.39 , pp. 1495-1502
    • Tan, T.W.1    Zhang, M.2    Xu, J.L.3    Zhang, J.J.4
  • 31
    • 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 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 33749186486 scopus 로고    scopus 로고
    • Purification and characterization of laccase produced by a white rot fungus Pleurotus sajor-caju under submerged culture condition and its potential in decolorization of azo dyes
    • Murugesan K., Arulmani M., Nam I.H., Kim Y.M., Chang Y.S., and Kalaichelvan P.T. Purification and characterization of laccase produced by a white rot fungus Pleurotus sajor-caju under submerged culture condition and its potential in decolorization of azo dyes. Appl Microbiol Biotechnol 72 (2006) 939-946
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 939-946
    • Murugesan, K.1    Arulmani, M.2    Nam, I.H.3    Kim, Y.M.4    Chang, Y.S.5    Kalaichelvan, P.T.6
  • 34
    • 0142043932 scopus 로고    scopus 로고
    • Isolation of a thermostable laccase with DMAB and MBTH oxidative coupling activity from a mesophilic white rot fungus
    • Jordaan J., and Leukes W.D. Isolation of a thermostable laccase with DMAB and MBTH oxidative coupling activity from a mesophilic white rot fungus. Enzyme Microb Technol 33 (2003) 212-219
    • (2003) Enzyme Microb Technol , vol.33 , pp. 212-219
    • Jordaan, J.1    Leukes, W.D.2
  • 35
    • 0036947687 scopus 로고    scopus 로고
    • Molecular cloning of a laccase isozyme gene from Pleurotus sajor-caju and expression in the heterologous Pichia pastoris host
    • Soden D.M., O'Callaghan J., and Dobson A.D. Molecular cloning of a laccase isozyme gene from Pleurotus sajor-caju and expression in the heterologous Pichia pastoris host. Microbiology 148 (2002) 4003-4014
    • (2002) Microbiology , vol.148 , pp. 4003-4014
    • Soden, D.M.1    O'Callaghan, J.2    Dobson, A.D.3
  • 36
    • 0141447532 scopus 로고    scopus 로고
    • Purification, characterization and sequence analysis of a laccase from the ascomycete Mauginiella sp.
    • Palonen H., Saloheimo M., Viikari L., and Kruus K. Purification, characterization and sequence analysis of a laccase from the ascomycete Mauginiella sp. Enzyme Microb Technol 33 (2003) 854-862
    • (2003) Enzyme Microb Technol , vol.33 , pp. 854-862
    • Palonen, H.1    Saloheimo, M.2    Viikari, L.3    Kruus, K.4
  • 37
    • 34247609835 scopus 로고    scopus 로고
    • Purification and characterization of laccase from Pycnoporus sanguineus and decolorization of an anthraquinone dye by the enzyme
    • Lu L., Zhao M., Zhang B.B., Yu S.Y., Bian X.J., Wang W., et al. Purification and characterization of laccase from Pycnoporus sanguineus and decolorization of an anthraquinone dye by the enzyme. Appl Microbiol Biotechnol 74 (2007) 1232-1239
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 1232-1239
    • Lu, L.1    Zhao, M.2    Zhang, B.B.3    Yu, S.Y.4    Bian, X.J.5    Wang, W.6
  • 38
    • 0042825653 scopus 로고    scopus 로고
    • Purification and characterization of the main laccase produced by the white-rot fungus Pleurotus pulmonarius on wheat bran solid state medium
    • Marques De Souza C.G., and Peralta R.M. Purification and characterization of the main laccase produced by the white-rot fungus Pleurotus pulmonarius on wheat bran solid state medium. J Basic Microbiol 43 (2007) 278-286
    • (2007) J Basic Microbiol , vol.43 , pp. 278-286
    • Marques De Souza, C.G.1    Peralta, R.M.2
  • 39
    • 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. The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase. Appl Environ Microbiol 62 (1996) 1151-1158
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1151-1158
    • Eggert, C.1    Temp, U.2    Eriksson, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.