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Volumn 21, Issue 7, 2011, Pages 711-718

Characterization of cellobiohydrolase from a newly Isolated strain of Agaricus arvencis

Author keywords

Agaricus arvencis; Catalytic efficiency; Cellobiohydrolase; Enzyme production; Glycoside hydrolase

Indexed keywords

4 NITROPHENYL BETA DEXTRO CELLOBIOSE; CELLULOSE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; DIMER; GLYCOSIDASE; GLYCOSIDE HYDROLASE FAMILY 7; INTERNAL TRANSCRIBED SPACER; RIBOSOME DNA; UNCLASSIFIED DRUG;

EID: 79961014006     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1102.02001     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 34250741703 scopus 로고    scopus 로고
    • Fatty acid and sugar compositions and nutritional value of five wild edible mushrooms
    • Barros, L., P. Baptista, D. M. Correia, S. Casal, B. Oliveira, and I. C. F. R. Ferreira. 2007. Fatty acid and sugar compositions and nutritional value of five wild edible mushrooms. Food Chem. 105: 140-145.
    • (2007) Food Chem. , vol.105 , pp. 140-145
    • Barros, L.1    Baptista, P.2    Correia, D.M.3    Casal, S.4    Oliveira, B.5    Ferreira, I.C.F.R.6
  • 3
    • 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
  • 4
    • 3242685134 scopus 로고    scopus 로고
    • Cellulase complex of the fungus Chrysosporium lucknowense: Isolation and characterization of endoglucanases and cellobiohydrolases
    • Bukhtojarov, F. E., B. B. Ustinov, T. N. Salanovich, A. I. Antonov, A. V. Gusakov, O. N. Okunev, and A. P. Sinitsyn. 2004. Cellulase complex of the fungus Chrysosporium lucknowense: Isolation and characterization of endoglucanases and cellobiohydrolases. Biochemistry 69: 542-551.
    • (2004) Biochemistry , vol.69 , pp. 542-551
    • Bukhtojarov, F.E.1    Ustinov, B.B.2    Salanovich, T.N.3    Antonov, A.I.4    Gusakov, A.V.5    Okunev, O.N.6    Sinitsyn, A.P.7
  • 5
    • 0021426650 scopus 로고
    • An assay for selective determination of exo-1,4-b-glucanases in a mixture of cellulolytic enzymes
    • Deshpande, M. V., K. E. Eriksson, and L. G. Pettersson. 1984. An assay for selective determination of exo-1,4-b-glucanases in a mixture of cellulolytic enzymes. Anal. Biochem. 138: 481-487.
    • (1984) Anal. Biochem. , vol.138 , pp. 481-487
    • Deshpande, M.V.1    Eriksson, K.E.2    Pettersson, L.G.3
  • 6
    • 73949087603 scopus 로고    scopus 로고
    • Simultaneous saccharification and fermentation and partial saccharification and co-fermentation of lignocellulosic biomass for ethanol production
    • Doran-Peterson, J., A. Jangid, S. K. Brandon, E. DeCrescenzo-Henriksen, B. Dien, and L. O. Ingram. 2009. Simultaneous saccharification and fermentation and partial saccharification and co-fermentation of lignocellulosic biomass for ethanol production. Methods Mol. Biol. 581: 263-280.
    • (2009) Methods Mol. Biol. , vol.581 , pp. 263-280
    • Doran-Peterson, J.1    Jangid, A.2    Brandon, S.K.3    de Crescenzo-Henriksen, E.4    Dien, B.5    Ingram, L.O.6
  • 7
    • 44949107516 scopus 로고    scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarity
    • Edwards, I. P., R. A. Upchurch, and R. Z. Donald. 2008. A classification of glycosyl hydrolases based on amino acid sequence similarity. Appl. Environ. Microbiol. 74. 74: 3481-3489.
    • (2008) Appl. Environ. Microbiol. , vol.74 , Issue.74 , pp. 3481-3489
    • Edwards, I.P.1    Upchurch, R.A.2    Donald, R.Z.3
  • 8
    • 9944253283 scopus 로고    scopus 로고
    • Purification, cloning and characterization of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense
    • Gusakov, A. V., A. P. Sinitsyn, T. N. Salanovich, F. E. Bukhtojarov, A. V. Markov, B. B. Ustinov, C. Van Zeijl, P. Punt, and R. Burlingame. 2005. Purification, cloning and characterization of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense. Enzyme Microb. Technol. 36: 57-69.
    • (2005) Enzyme Microb. Technol. , vol.36 , pp. 57-69
    • Gusakov, A.V.1    Sinitsyn, A.P.2    Salanovich, T.N.3    Bukhtojarov, F.E.4    Markov, A.V.5    Ustinov, B.B.6    Van Zeijl, C.7    Punt, P.8    Burlingame, R.9
  • 10
    • 0032936882 scopus 로고    scopus 로고
    • Purification, characterization and gene analysis of exo-cellulase II (Ex-2) from the white rot basidiomycete Irpex lacteus
    • Hamada, N., K. Ishikawa, N. Fuse, R. Kodaira, M. Shimosaka, Y. Amano, T. Kanda, and M. Okazaki. 1999. Purification, characterization and gene analysis of exo-cellulase II (Ex-2) from the white rot basidiomycete Irpex lacteus. J. Biosci. Bioeng. 87: 442-451.
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 442-451
    • Hamada, N.1    Ishikawa, K.2    Fuse, N.3    Kodaira, R.4    Shimosaka, M.5    Amano, Y.6    Kanda, T.7    Okazaki, M.8
  • 11
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarity
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarity. Biochem. J. 280: 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 12
    • 1642521928 scopus 로고    scopus 로고
    • Cloning of a gene encoding thermostable cellobiohydrolase from Thermoascus aurantiacus and its expression in yeast
    • Hong, J., H. Tamaki, K. Yamamoto, and H. Kumagai. 2003. Cloning of a gene encoding thermostable cellobiohydrolase from Thermoascus aurantiacus and its expression in yeast. Appl. Microbiol. Biotechnol. 63: 42-50.
    • (2003) Appl. Microbiol. Biotechnol. , vol.63 , pp. 42-50
    • Hong, J.1    Tamaki, H.2    Yamamoto, K.3    Kumagai, H.4
  • 13
    • 0032766556 scopus 로고    scopus 로고
    • Cloning of the CBHI and CBHII genes involved in cellulose utilization by the straw mushroom Volvariella volvacea
    • Jia, J., P. S. Dyer, and J. F. Buswell. 1999. Cloning of the CBHI and CBHII genes involved in cellulose utilization by the straw mushroom Volvariella volvacea. Mol. Gen. Genet. 261: 985-993.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 985-993
    • Jia, J.1    Dyer, P.S.2    Buswell, J.F.3
  • 14
    • 70350590693 scopus 로고    scopus 로고
    • The genes encoding glycoside hydrolase family 6 and 7 cellulases from the brown-rot fungus Coniphora puteana
    • Kajisa, T., K. Igarahi, and M. Samejima. 2009. The genes encoding glycoside hydrolase family 6 and 7 cellulases from the brown-rot fungus Coniphora puteana. J. Wood Sci. 55: 376-380.
    • (2009) J. Wood Sci. , vol.55 , pp. 376-380
    • Kajisa, T.1    Igarahi, K.2    Samejima, M.3
  • 15
    • 0027526207 scopus 로고
    • Cloning, sequencing, and heterologous expression of a cellulase-encoding cDNA (cbh1) from Penicillium janthinellum
    • Koch, A., C. T. Weigel, and G. Schulz. 1993. Cloning, sequencing, and heterologous expression of a cellulase-encoding cDNA (cbh1) from Penicillium janthinellum. Gene 124: 57-65.
    • (1993) Gene , vol.124 , pp. 57-65
    • Koch, A.1    Weigel, C.T.2    Schulz, G.3
  • 16
    • 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
  • 18
    • 0035910126 scopus 로고    scopus 로고
    • Cloning and characterization of two cellulase genes from Lentinula edodes
    • Lee, C. C., D. W. Wong, and G. H. Robertson. 2001. Cloning and characterization of two cellulase genes from Lentinula edodes. FEMS Microbiol. Lett. 205: 355-360.
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 355-360
    • Lee, C.C.1    Wong, D.W.2    Robertson, G.H.3
  • 19
    • 65549087967 scopus 로고    scopus 로고
    • Purification and characterization of a cellobiohydrolase from the thermophilic fungus Chaetomium thermophilus CT2
    • Li, Y. L., D. C. Li, and F. C. Teng. 2006. Purification and characterization of a cellobiohydrolase from the thermophilic fungus Chaetomium thermophilus CT2. Wei Sheng Wu Xue Bao 46: 143-146.
    • (2006) Wei Sheng Wu Xue Bao , vol.46 , pp. 143-146
    • Li, Y.L.1    Li, D.C.2    Teng, F.C.3
  • 20
    • 34347268084 scopus 로고    scopus 로고
    • Characterization of β-glucosidases from a mesophilic Aureobasidium pullulana and thermophilic Thermoascus aurantiacus
    • Liete, R. S. R., E. Gomes, and R. Da-Silva. 2007. Characterization of β-glucosidases from a mesophilic Aureobasidium pullulana and thermophilic Thermoascus aurantiacus. Process Biochem. 42: 1101-1106.
    • (2007) Process Biochem. , vol.42 , pp. 1101-1106
    • Liete, R.S.R.1    Gomes, E.2    Da-Silva, R.3
  • 21
    • 0029594189 scopus 로고
    • Two cellobiohydrolases of Penicillium occitanis mutant Pol 6: Purification and properties
    • Limam, F., S. E. Chaabouni, R. Ghrir, and N. Marzouki. 1995. Two cellobiohydrolases of Penicillium occitanis mutant Pol 6: Purification and properties. Enzyme Microb. Technol. 17: 340-346.
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 340-346
    • Limam, F.1    Chaabouni, S.E.2    Ghrir, R.3    Marzouki, N.4
  • 22
    • 0032838958 scopus 로고    scopus 로고
    • Purification and biochemical characterization of β-glucosidase from a thermophilic fungus, Thermomyces lanuginosus
    • Lin, J., B. Pillay, and S. Singh. 1999. Purification and biochemical characterization of β-glucosidase from a thermophilic fungus, Thermomyces lanuginosus. Biotechnol. Appl. Biochem. 30: 81-87.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 81-87
    • Lin, J.1    Pillay, B.2    Singh, S.3
  • 23
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 24
    • 34548691900 scopus 로고    scopus 로고
    • Transcriptional regulation of two cellobiohydrolase encoding genes (cel1 and cel2) from the wood-degrading basidiomycete Polyporus arcularius
    • Ohnishi, Y., M. Nagase, T. Ichiyanagi, Y. Kitamoto, and T. Aimi. 2007. Transcriptional regulation of two cellobiohydrolase encoding genes (cel1 and cel2) from the wood-degrading basidiomycete Polyporus arcularius. Appl. Microbiol. Biotechnol. 76: 1069-1078.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 1069-1078
    • Ohnishi, Y.1    Nagase, M.2    Ichiyanagi, T.3    Kitamoto, Y.4    Aimi, T.5
  • 25
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: Screening and selection strategies
    • Percival Zhang, Y. H., M. E. Himmel, and J. R. Mielenz. 2006. Outlook for cellulase improvement: Screening and selection strategies. Biotechnol. Adv. 24: 452-481.
    • (2006) Biotechnol. Adv. , vol.24 , pp. 452-481
    • Percival Zhang, Y.H.1    Himmel, M.E.2    Mielenz, J.R.3
  • 26
    • 0023103376 scopus 로고
    • A capillary racetrack method for isolation of magnetotactic bacteria
    • Wolfe, R. S., R. K. Thauer, and N. Pfennig. 1987. A capillary racetrack method for isolation of magnetotactic bacteria. FEMS Microbiol. Lett. 45: 31-35.
    • (1987) FEMS Microbiol. Lett. , vol.45 , pp. 31-35
    • Wolfe, R.S.1    Thauer, R.K.2    Pfennig, N.3
  • 27
    • 0000420358 scopus 로고
    • Purification and properties of 2 enzymes from Duchomitus squalens which exhibit both cellobiohydrolase and xylanase activity
    • Rouau, X. and E. Odier. 1986. Purification and properties of 2 enzymes from Duchomitus squalens which exhibit both cellobiohydrolase and xylanase activity. Carbohydr. Res. 145: 279-292.
    • (1986) Carbohydr. Res. , vol.145 , pp. 279-292
    • Rouau, X.1    Odier, E.2
  • 28
    • 0027282812 scopus 로고
    • Purification and characterization of two exo-cellobiohydrolases from the brownrot fungus Coniophora puteana (Schum ex Fr) Karst
    • Schmidhalter, D. R. and G. Canevascini. 1993. Purification and characterization of two exo-cellobiohydrolases from the brownrot fungus Coniophora puteana (Schum ex Fr) Karst. Arch. Biochem. Biophys. 300: 551-558.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 551-558
    • Schmidhalter, D.R.1    Canevascini, G.2
  • 29
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cello-biohydrolases
    • Teeri, T. T. 1997. Crystalline cellulose degradation: New insight into the function of cello-biohydrolases. Trends Biotechnol. 15: 160-167.
    • (1997) Trends Biotechnol. , vol.15 , pp. 160-167
    • Teeri, T.T.1
  • 30
    • 0023132478 scopus 로고
    • Homologous domains in Trichoderma reesei cellulolytic enzymes: Gene sequence and expression of cellobiohydrolase II
    • Teeri, T. T., P. Lehtovaara, S. Kauppinen, I. Salovuori, and J. Knowles. 1987. Homologous domains in Trichoderma reesei cellulolytic enzymes: Gene sequence and expression of cellobiohydrolase II. Gene 51: 43-52.
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kauppinen, S.3    Salovuori, I.4    Knowles, J.5
  • 32
    • 0000432452 scopus 로고
    • Amplification and direct sequencing of fungal ribosomal RNA genes for phylogenetics
    • In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (eds.), Academic Press, Inc., New York, NY
    • White, T. J., T. Bruns, S. Lee, and J. Taylor. 1990. Amplification and direct sequencing of fungal ribosomal RNA genes for phylogenetics, pp. 315-322. In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (eds.). PCR Protocols: A Guide to Methods and Applications Academic Press, Inc., New York, NY.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 315-322
    • White, T.J.1    Bruns, T.2    Lee, S.3    Taylor, J.4


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