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Volumn 43, Issue 6, 2008, Pages 634-641

Cellobiose dehydrogenase production by the mycelial culture of the mushroom Termitomyces clypeatus

Author keywords

Cellobiose dehydrogenase; Edible fungus; Glucose effect; Lactobionic acid; Termitomyces clypeatus; Thermolabile enzyme

Indexed keywords

CELL CULTURE; FUNGI; GLUCOSE; ORGANIC ACIDS; PH;

EID: 42749088544     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.01.025     Document Type: Article
Times cited : (24)

References (36)
  • 1
  • 2
    • 0035252395 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase-an extracellular fungal flavocytochrome
    • Cameron M.D., and Aust S.D. Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme Microb Technol 28 (2001) 129-138
    • (2001) Enzyme Microb Technol , vol.28 , pp. 129-138
    • Cameron, M.D.1    Aust, S.D.2
  • 3
    • 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 Peptide Sci 7 (2006) 255-280
    • (2006) Curr Protein Peptide 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
  • 4
    • 0035931413 scopus 로고    scopus 로고
    • Continuous enzymatic regeneration of redox mediators used in biotransformation reactions employing flavoproteins
    • Baminger U., Ludwig R., Galhaup C., Leitner C., Kulbe K.D., and Haltrich D. Continuous enzymatic regeneration of redox mediators used in biotransformation reactions employing flavoproteins. J Mol Catal B Enzyme 11 (2001) 541-550
    • (2001) J Mol Catal B Enzyme , vol.11 , pp. 541-550
    • Baminger, U.1    Ludwig, R.2    Galhaup, C.3    Leitner, C.4    Kulbe, K.D.5    Haltrich, D.6
  • 5
    • 3042627355 scopus 로고    scopus 로고
    • Continuous enzymatic regeneration of electron acceptors used by flavoenzymes: cellobiose dehydrogenase-catalyzed production of lactobionic acid as an example
    • Ludwig R., Ozga M., Zamocky M., Peterbauer C., Kulbe K.D., and Haltrich D. Continuous enzymatic regeneration of electron acceptors used by flavoenzymes: cellobiose dehydrogenase-catalyzed production of lactobionic acid as an example. Biocatal Biotransform 22 (2004) 97-104
    • (2004) Biocatal Biotransform , vol.22 , pp. 97-104
    • Ludwig, R.1    Ozga, M.2    Zamocky, M.3    Peterbauer, C.4    Kulbe, K.D.5    Haltrich, D.6
  • 6
    • 0027222127 scopus 로고
    • Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium
    • Bao W., Usha S.N., and Renganathan V. Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium. Arch Biochem Biophys 300 2 (1993) 705-713
    • (1993) Arch Biochem Biophys , vol.300 , Issue.2 , pp. 705-713
    • Bao, W.1    Usha, S.N.2    Renganathan, V.3
  • 7
    • 0025420075 scopus 로고
    • β-Glucosidase production by the mycelial culture of mushroom Termitomyces clypeatus
    • Sengupta S., and Sengupta S. β-Glucosidase production by the mycelial culture of mushroom Termitomyces clypeatus. Enzyme Microb Technol 12 4 (1990) 309-311
    • (1990) Enzyme Microb Technol , vol.12 , Issue.4 , pp. 309-311
    • Sengupta, S.1    Sengupta, S.2
  • 8
    • 51249161640 scopus 로고
    • Regulation of endo-1,4-β-glucanase secretion from Termitomyces clypeatus by carbon catabolic product(s)
    • Mukherjee M., Khowala S., Ghosh A.K., and Sengupta S. Regulation of endo-1,4-β-glucanase secretion from Termitomyces clypeatus by carbon catabolic product(s). Folia Microbiol 40 (1995) 475-480
    • (1995) Folia Microbiol , vol.40 , pp. 475-480
    • Mukherjee, M.1    Khowala, S.2    Ghosh, A.K.3    Sengupta, S.4
  • 9
    • 0030565601 scopus 로고    scopus 로고
    • Synthesis of glycolipids: dialkyl N-[N-(4-lactonamidobutyl) succinamoyl]-l-glutamates
    • Zhang Z., Fukunaga K., Sugimura Y., Nakao K., and Shimizu T. Synthesis of glycolipids: dialkyl N-[N-(4-lactonamidobutyl) succinamoyl]-l-glutamates. Carbohydr Res 290 (1996) 225-232
    • (1996) Carbohydr Res , vol.290 , pp. 225-232
    • Zhang, Z.1    Fukunaga, K.2    Sugimura, Y.3    Nakao, K.4    Shimizu, T.5
  • 10
    • 0025760499 scopus 로고
    • Biomass estimation in solid state fermentation. Part I. Manual biochemical methods
    • Desgranges C., Vergoignan C., Georges M., and Durand A. Biomass estimation in solid state fermentation. Part I. Manual biochemical methods. Appl Microbiol Biotechnol 35 (1991) 200-205
    • (1991) Appl Microbiol Biotechnol , vol.35 , pp. 200-205
    • Desgranges, C.1    Vergoignan, C.2    Georges, M.3    Durand, A.4
  • 11
    • 0031839473 scopus 로고    scopus 로고
    • Chitin as an indicator of the biomass of two wood-decay fungi in relation to temperature, incubation time, and media composition
    • Nilsson K., and Bjurman J. Chitin as an indicator of the biomass of two wood-decay fungi in relation to temperature, incubation time, and media composition. Can J Microbiol 44 (1998) 575-581
    • (1998) Can J Microbiol , vol.44 , pp. 575-581
    • Nilsson, K.1    Bjurman, J.2
  • 12
    • 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., and Haltrich D. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl Environ Microbiol 67 4 (2001) 1766-1774
    • (2001) Appl Environ Microbiol , vol.67 , Issue.4 , pp. 1766-1774
    • Baminger, U.1    Subramaniam, S.S.2    Renganathan, V.3    Haltrich, D.4
  • 13
    • 28444457376 scopus 로고    scopus 로고
    • Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26 (-) and comparison with basidiomycetous cellobiose dehydrogenase
    • Karapetyan K.N., Fedorova T.V., Vasil'chenko L.G., Ludwig R., Haltrich D., and Rabinovich M.L. Properties of neutral cellobiose dehydrogenase from the ascomycete Chaetomium sp. INBI 2-26 (-) and comparison with basidiomycetous cellobiose dehydrogenase. J Biotechnol 121 (2006) 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
  • 14
    • 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 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 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., and Sigoillot J.C. Lignocellulolytic and hemicellulolytic system of Pycnoporus cinnabarinus: isolation and characterization of a cellobiose dehydrogenase and a new xylanase. Enzyme Microb Technol 31 (2002) 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
  • 16
    • 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
  • 17
    • 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., and Rabinovich M.L. Isolation and characterization of a cellobiose dehydrogenase formed by a nonsporulating mycelial fungus INBI 2-26 (-). Appl Biochem Microbiol 39 (2003) 642-651
    • (2003) Appl Biochem Microbiol , vol.39 , pp. 642-651
    • Karapetyan, K.N.1    Yachkova, S.N.2    Vasil'chenko, L.G.3    Borzykh, M.N.4    Rabinovich, M.L.5
  • 18
    • 0000795403 scopus 로고
    • A direct enzymatic lactose assay using cellobiose- (lactose-)dehydrogenase from Sporotrichum thermophile
    • Canevascini G., Etienne K., and Meier H. A direct enzymatic lactose assay using cellobiose- (lactose-)dehydrogenase from Sporotrichum thermophile. Z Lebensm Unters Forsch 175 (1982) 125-129
    • (1982) Z Lebensm Unters Forsch , vol.175 , pp. 125-129
    • Canevascini, G.1    Etienne, K.2    Meier, H.3
  • 19
    • 77956832035 scopus 로고
    • Chemical extraction methods of microbial cells
    • Sutherland I.W., and Wilkinson J.F. Chemical extraction methods of microbial cells. Methods Microbiol 5B (1971) 345-383
    • (1971) Methods Microbiol , vol.5 B , pp. 345-383
    • Sutherland, I.W.1    Wilkinson, J.F.2
  • 20
    • 0005658772 scopus 로고
    • Chromatography on paper
    • Whistler R.L., and Wolfrom M.L. (Eds), Academic Press, New York, London
    • Hough L., and Jones J.K.N. Chromatography on paper. In: Whistler R.L., and Wolfrom M.L. (Eds). Methods in carbohydrate chemistry I (1962), Academic Press, New York, London 21-31
    • (1962) Methods in carbohydrate chemistry , vol.I , pp. 21-31
    • Hough, L.1    Jones, J.K.N.2
  • 21
    • 0030770510 scopus 로고    scopus 로고
    • Enhanced production of cellobiose dehydrogenase in cultures of Phanerochaete chrysosporium supplemented with bovine calf serum
    • Habu N., Igarashi K., Samejima M., Pettersson B., and Eriksson K.E.L. Enhanced production of cellobiose dehydrogenase in cultures of Phanerochaete chrysosporium supplemented with bovine calf serum. Biotechnol Appl Biochem 26 (1997) 97-102
    • (1997) Biotechnol Appl Biochem , vol.26 , pp. 97-102
    • Habu, N.1    Igarashi, K.2    Samejima, M.3    Pettersson, B.4    Eriksson, K.E.L.5
  • 22
    • 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., and Gao P. Optimization of cellobiose dehydrogenase production by Schizophyllum commune and effect of the enzyme on kraft pulp bleaching by ligninases. Process Biochem 34 (1999) 957-961
    • (1999) Process Biochem , vol.34 , pp. 957-961
    • Fang, J.1    Huang, F.2    Gao, P.3
  • 23
    • 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., and Gao P.J. Cellobiose dehydrogenase from Schizophyllum commune: purification and study of some catalytic, inactivation and cellulose-binding properties. Arch Biochem Biophys 353 1 (1998) 37-46
    • (1998) Arch Biochem Biophys , vol.353 , Issue.1 , pp. 37-46
    • Fang, J.1    Liu, W.2    Gao, P.J.3
  • 24
    • 0029928876 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium
    • Li B., Nagalla S.R., and Renganathan V. Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium. Appl Environ Microbiol 62 4 (1996) 1329-1335
    • (1996) Appl Environ Microbiol , vol.62 , Issue.4 , pp. 1329-1335
    • Li, B.1    Nagalla, S.R.2    Renganathan, V.3
  • 25
    • 0033562157 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile
    • Subramaniam S.S., Nagalla S.R., and Renganathan V. Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile. Arch Biochem Biophys 365 2 (1999) 223-230
    • (1999) Arch Biochem Biophys , vol.365 , Issue.2 , pp. 223-230
    • Subramaniam, S.S.1    Nagalla, S.R.2    Renganathan, V.3
  • 26
    • 0037126648 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding cellobiose dehydrogenase from the wood-rotting fungus Grifola frondosa
    • Yoshida M., Ohira T., Igarashi K., Nagasawa H., and Samejima M. Molecular cloning and characterization of a cDNA encoding cellobiose dehydrogenase from the wood-rotting fungus Grifola frondosa. FEMS Microbiol Lett 217 (2002) 225-230
    • (2002) FEMS Microbiol Lett , vol.217 , pp. 225-230
    • Yoshida, M.1    Ohira, T.2    Igarashi, K.3    Nagasawa, H.4    Samejima, M.5
  • 27
    • 34250211800 scopus 로고    scopus 로고
    • Laccase production by the white-rot fungus Termitomyces clypeatus
    • Bose S., Mazumder S., and Mukherjee M. Laccase production by the white-rot fungus Termitomyces clypeatus. J Basic Microbiol 47 (2007) 127-131
    • (2007) J Basic Microbiol , vol.47 , pp. 127-131
    • Bose, S.1    Mazumder, S.2    Mukherjee, M.3
  • 28
    • 0026032346 scopus 로고
    • Cellobiose oxidase from Phanerochaete chrysosporium can be cleaved by papain into two domains
    • Henriksson G., Pettersson G., Johansson G., Ruiz A., and Uzcategui E. Cellobiose oxidase from Phanerochaete chrysosporium can be cleaved by papain into two domains. Eur J Biochem 196 (1991) 101-106
    • (1991) Eur J Biochem , vol.196 , pp. 101-106
    • Henriksson, G.1    Pettersson, G.2    Johansson, G.3    Ruiz, A.4    Uzcategui, E.5
  • 29
    • 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., and Archibald F.S. Purification and characterization of cellobiose dehydrogenases from the white rot fungus Trametes versicolor. Appl Environ Microbiol 62 12 (1996) 4417-4427
    • (1996) Appl Environ Microbiol , vol.62 , Issue.12 , pp. 4417-4427
    • Roy, B.P.1    Dumonceaux, T.2    Koukoulas, A.A.3    Archibald, F.S.4
  • 30
    • 2342432133 scopus 로고    scopus 로고
    • Characterization 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. Characterization of cellobiose dehydrogenases from the white-rot fungi Trametes pubescens and Trametes villosa. Appl Microbiol Biotechnol 64 (2004) 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
  • 31
    • 33746449143 scopus 로고    scopus 로고
    • Purification and characterization of cellobiose dehydrogenase from white-rot basidiomycete Trametes hirsuta
    • Nakagame S., Furujyo A., and Sugiura J. Purification and characterization of cellobiose dehydrogenase from white-rot basidiomycete Trametes hirsuta. Biosci Biotechnol Biochem 70 7 (2006) 1629-1635
    • (2006) Biosci Biotechnol Biochem , vol.70 , Issue.7 , pp. 1629-1635
    • Nakagame, S.1    Furujyo, A.2    Sugiura, J.3
  • 32
    • 0032519528 scopus 로고    scopus 로고
    • Characterization of a cellobiose dehydrogenase from Humicola insolens
    • Schou C., Christensen M.H., and Schülein M. Characterization of a cellobiose dehydrogenase from Humicola insolens. Biochem J 330 (1998) 565-571
    • (1998) Biochem J , vol.330 , pp. 565-571
    • Schou, C.1    Christensen, M.H.2    Schülein, M.3
  • 33
    • 0030895389 scopus 로고    scopus 로고
    • The behaviour of Phanerochaete chrysosporium cellobiose dehydrogenase on absorption to crystalline and amorphous celluloses
    • Samejima M., Ohkubo T., Igarashi K., Isogai A., Kuga S., Sugiyama J., et al. The behaviour of Phanerochaete chrysosporium cellobiose dehydrogenase on absorption to crystalline and amorphous celluloses. Biotechnol Appl Biochem 25 (1997) 135-141
    • (1997) Biotechnol Appl Biochem , vol.25 , pp. 135-141
    • Samejima, M.1    Ohkubo, T.2    Igarashi, K.3    Isogai, A.4    Kuga, S.5    Sugiyama, J.6
  • 34
    • 0343865359 scopus 로고
    • Cellobiose dehydrogenase from Phanerochaete chrysosporium: substrate specificity for cellulose oxidation and cellulose hydrolysis enhancement
    • Vienna, Austria 11-15 June
    • Subramaniam S.S., Bao W., and Renganathan V. Cellobiose dehydrogenase from Phanerochaete chrysosporium: substrate specificity for cellulose oxidation and cellulose hydrolysis enhancement. Proceedings of the 6th International Conference on Biotechnol Pulp and paper Industry. Vienna, Austria 11-15 June (1995) 192
    • (1995) Proceedings of the 6th International Conference on Biotechnol Pulp and paper Industry , pp. 192
    • Subramaniam, S.S.1    Bao, W.2    Renganathan, V.3
  • 35
    • 0021813669 scopus 로고
    • Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum
    • Morpeth F.F. Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum. Biochem J 228 (1985) 557-564
    • (1985) Biochem J , vol.228 , pp. 557-564
    • Morpeth, F.F.1
  • 36
    • 0028169897 scopus 로고
    • 1H NMR evidence for conversion of β-d-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium
    • 1H NMR evidence for conversion of β-d-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium. FEBS Lett 351 (1994) 128-132
    • (1994) FEBS Lett , vol.351 , pp. 128-132
    • Higham, C.W.1    Gordon-Smith, D.2    Dempsey, C.E.3    Wood, P.M.4


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