메뉴 건너뛰기




Volumn 48, Issue 1, 2010, Pages 53-62

Purification and biochemical properties of a glucose-stimulated β-D-glucosidase produced by Humicola grisea var. thermoidea grown on sugarcane bagasse

Author keywords

Agricultural residues; Cellobiase; Glucose stimulated D glucosidase; H. grisea; Sugarcane bagasse; Thermophilic fungi

Indexed keywords

BAGASSE; BETA GLUCOSIDASE; CELLULASE; CELLULOSE; FUNGAL PROTEIN; GLUCOSE;

EID: 77949292657     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-009-0159-x     Document Type: Article
Times cited : (60)

References (62)
  • 1
    • 4344599124 scopus 로고    scopus 로고
    • Effect of carbon source on the biochemical properties of β-xylosidases produced by Aspergillus versicolor
    • Andrade, S. V., M. L. T. M. Polizeli, H. F. Terenzi, and J. A. Jorge. 2004. Effect of carbon source on the biochemical properties of β-xylosidases produced by Aspergillus versicolor. Proc. Biochem. 39, 1931-1938.
    • (2004) Proc. Biochem. , vol.39 , pp. 1931-1938
    • Andrade, S.V.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 2
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • Beguin, P. and J. P. Aubert. 1994. The biological degradation of cellulose. FEMS Microbiol. Rev. 13, 25-58.
    • (1994) FEMS Microbiol. Rev. , vol.13 , pp. 25-58
    • Beguin, P.1    Aubert, J.P.2
  • 3
    • 0000002475 scopus 로고
    • D-glucose determination with glucose oxidase and peroxidase
    • H. U. Bergmeyer (Ed.), New York, N.Y., USA: Verlag Chimie-Academic Press
    • Bergmeyer, H. U. and E. Bernt. 1974. D-glucose determination with glucose oxidase and peroxidase, pp. 1205-1215. In H. U. Bergmeyer (ed.), Methods of Enzymatic Analysis, vol. 3. Verlag Chimie-Academic Press, New York, N. Y., USA.
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1205-1215
    • Bergmeyer, H.U.1    Bernt, E.2
  • 4
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degrading enzymes and their potential industrial applications
    • Bhat, M. and T. S. Bhat. 1997. Cellulose degrading enzymes and their potential industrial applications. Biotechnol. Adv. 15, 583-620.
    • (1997) Biotechnol. Adv. , vol.15 , pp. 583-620
    • Bhat, M.1    Bhat, T.S.2
  • 5
    • 0036448608 scopus 로고    scopus 로고
    • Microbial β-glucosidases: Cloning, properties, and applications
    • Bhatia, Y., S. Mishra, and V. S. Bisaria. 2002. Microbial β-glucosidases: cloning, properties, and applications. Crit. Rev. Biotechnol. 22, 375-407.
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 6
    • 50049110704 scopus 로고    scopus 로고
    • Purification and biochemical characterization of extracellular β-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis
    • Bhiri, F., S. E. Chaabouni, F. Limam, R. Ghrir, and N. Marzouki. 2008. Purification and biochemical characterization of extracellular β-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis. Appl. Biochem. Biotechnol. 149, 169-182.
    • (2008) Appl. Biochem. Biotechnol. , vol.149 , pp. 169-182
    • Bhiri, F.1    Chaabouni, S.E.2    Limam, F.3    Ghrir, R.4    Marzouki, N.5
  • 7
    • 77949308963 scopus 로고
    • Thermophilic fungi: an account of their biology, activities, and classification, In W. H. Freeman (ed.), San Francisco, California, USA
    • Cooney, D. G. and R. Emerson. 1964. Humicola insolens and Humicola grisea var. thermoidea. Thermophilic fungi: an account of their biology, activities, and classification, pp. 73-79. In W. H. Freeman (ed.), San Francisco, California, USA.
    • (1964) Humicola insolens and Humicola grisea var. thermoidea , pp. 73-79
    • Cooney, D.G.1    Emerson, R.2
  • 8
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • Davis, B. J. 1964. Disc electrophoresis. II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121, 404-427.
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 9
    • 0035091719 scopus 로고    scopus 로고
    • β-glucosidase multiplicity from Aspergillus tubingiensis CBS 643.92: Purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition and acid tolerance
    • Decker, C. H., J. Visser, and P. Schreier. 2001. β-glucosidase multiplicity from Aspergillus tubingiensis CBS 643. 92: purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition and acid tolerance. Appl. Microbiol. Biotechnol. 55, 157-163.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 157-163
    • Decker, C.H.1    Visser, J.2    Schreier, P.3
  • 10
    • 0028138630 scopus 로고
    • The glycosylation of phosphoglumutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae
    • Dey, N. B., P. Bounelis, T. A. Fritz, D. M. Bedewell, and R. B. Marchase. 1994. The glycosylation of phosphoglumutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 269, 27143-27148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27143-27148
    • Dey, N.B.1    Bounelis, P.2    Fritz, T.A.3    Bedewell, D.M.4    Marchase, R.B.5
  • 11
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M., K. A. Gilles, J. K. Hamilton, P. A. Rebers, and F. Smith. 1956. Colorimetric method for determination of sugars and related substances. Anal. Chem. 28, 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 12
    • 0029921130 scopus 로고    scopus 로고
    • Bioconversion of forest products industry waste cellulosics to fuel ethanol: A review
    • Duff, S. J. B. and W. D. Murray. 1996. Bioconversion of forest products industry waste cellulosics to fuel ethanol: A review. Biores. Technol. 55, 1-33.
    • (1996) Biores. Technol. , vol.55 , pp. 1-33
    • Duff, S.J.B.1    Murray, W.D.2
  • 13
    • 0035295879 scopus 로고    scopus 로고
    • Factors affecting cellulose production by Trichoderma koningii
    • El-Hawary, F. I. and Y. S. Mostafa. 2001. Factors affecting cellulose production by Trichoderma koningii. Acta Aliment. 30, 3-13.
    • (2001) Acta Aliment. , vol.30 , pp. 3-13
    • El-Hawary, F.I.1    Mostafa, Y.S.2
  • 14
    • 0035457369 scopus 로고    scopus 로고
    • Cellulase production and conversion of rice straw to lactic acid by simultaneous saccharification and fermentation
    • El-Hawary, F. I., Y. S. Mostafa, and E. Laszlo. 2001. Cellulase production and conversion of rice straw to lactic acid by simultaneous saccharification and fermentation. Acta Aliment. 30, 281-295.
    • (2001) Acta Aliment. , vol.30 , pp. 281-295
    • El-Hawary, F.I.1    Mostafa, Y.S.2    Laszlo, E.3
  • 15
    • 0036385526 scopus 로고    scopus 로고
    • A review of the production of ethanol from softwood
    • Galbe, M. and G. Zacchi. 2002. A review of the production of ethanol from softwood. Appl. Microbiol. Biotechnol. 59, 618-628.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 618-628
    • Galbe, M.1    Zacchi, G.2
  • 16
    • 45449111746 scopus 로고    scopus 로고
    • Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus M11 under solid-state cultivation on corn stover
    • Gao, J., H. Weng, D. Zhu, M. Yuan, F. Guan, and Y. Xi. 2008. Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus M11 under solid-state cultivation on corn stover. Biores. Technol. 99, 7623-7629.
    • (2008) Biores. Technol. , vol.99 , pp. 7623-7629
    • Gao, J.1    Weng, H.2    Zhu, D.3    Yuan, M.4    Guan, F.5    Xi, Y.6
  • 18
    • 0030893813 scopus 로고    scopus 로고
    • Characterization of cellulose complex of Streptomyces albaduncus
    • Harchand, R. K. and S. Singh. 1997. Characterization of cellulose complex of Streptomyces albaduncus. J. Basic Microbiol. 37, 93-103.
    • (1997) J. Basic Microbiol. , vol.37 , pp. 93-103
    • Harchand, R.K.1    Singh, S.2
  • 19
    • 0032528621 scopus 로고    scopus 로고
    • Modified glycosylation of cellobiohydrolase I from a high cellulase producing mutant strain of Trichoderma reesei
    • Harrison, M. J., A. S. Nouwens, D. R. Jardine, N. E. Zachara, A. A. Gooley, and H. Nevalainen. 1998. Modified glycosylation of cellobiohydrolase I from a high cellulase producing mutant strain of Trichoderma reesei. Eur. J. Biochem. 256, 119-127.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 119-127
    • Harrison, M.J.1    Nouwens, A.S.2    Jardine, D.R.3    Zachara, N.E.4    Gooley, A.A.5    Nevalainen, H.6
  • 20
    • 0008010753 scopus 로고
    • Cellulases of Humicola insolens and Humicola grisea
    • Hayashida, S., K. Ohta, and K. Mo. 1988. Cellulases of Humicola insolens and Humicola grisea. Methods Enzymol. 160, 323-332.
    • (1988) Methods Enzymol. , vol.160 , pp. 323-332
    • Hayashida, S.1    Ohta, K.2    Mo, K.3
  • 21
    • 0035836058 scopus 로고    scopus 로고
    • Characterization of cellobiohydrolase I (Cel7A) glycoforms from extracts of Trichoderma reesei using capillary isoelectric focusing and electrospray mass spectrometry
    • Hui, J. P. M., P. Lanthier, T. C. White, S. G. McHugh, M. Yaguchi, R. Roy, and P. Tribault. 2001. Characterization of cellobiohydrolase I (Cel7A) glycoforms from extracts of Trichoderma reesei using capillary isoelectric focusing and electrospray mass spectrometry. J. Chrom. B 752, 349-368.
    • (2001) J. Chrom. B , vol.752 , pp. 349-368
    • Hui, J.P.M.1    Lanthier, P.2    White, T.C.3    McHugh, S.G.4    Yaguchi, M.5    Roy, R.6    Tribault, P.7
  • 22
    • 34247098005 scopus 로고    scopus 로고
    • Purification and biochemical characterization of an extracellular beta-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.: Fr.) Rehm
    • Karnchanatat, A., A. Petsom, P. Sangvanich, J. Piaphukiew, A. J. Whalley, C. D. Reynolds, and P. Sihanonth. 2007. Purification and biochemical characterization of an extracellular beta-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.: Fr.) Rehm. FEMS Microbiol. Lett. 270, 162-170.
    • (2007) FEMS Microbiol. Lett. , vol.270 , pp. 162-170
    • Karnchanatat, A.1    Petsom, A.2    Sangvanich, P.3    Piaphukiew, J.4    Whalley, A.J.5    Reynolds, C.D.6    Sihanonth, P.7
  • 23
    • 34247606449 scopus 로고    scopus 로고
    • Purification and characterization of β-glucosidase from Melanocarpus sp. MTCC 3922
    • Kaur, J., B. S. Chadha, B. A. Kumar, S. K. Ghatora, and H. S. Saini. 2007. Purification and characterization of β-glucosidase from Melanocarpus sp. MTCC 3922. Electronic J. Biotechnol. 10, 260-270.
    • (2007) Electronic J. Biotechnol , vol.10 , pp. 260-270
    • Kaur, J.1    Chadha, B.S.2    Kumar, B.A.3    Ghatora, S.K.4    Saini, H.S.5
  • 24
    • 33645225564 scopus 로고    scopus 로고
    • Regulation of cellulose production in two thermophilic fungi Melanocarpus sp. MTCC 3922 and Scytalidium thermophilum MTCC 4520. Enzyme Microb
    • Kaur, J., B. S. Chadha, and H. S. Saini. 2006. Regulation of cellulose production in two thermophilic fungi Melanocarpus sp. MTCC 3922 and Scytalidium thermophilum MTCC 4520. Enzyme Microb. Technol. 38, 931-936.
    • (2006) Technol , vol.38 , pp. 931-936
    • Kaur, J.1    Chadha, B.S.2    Saini, H.S.3
  • 25
    • 0027050823 scopus 로고
    • Stability, quaternary structure, and folding of internal, external, and coreglycosylated invertase from yeast
    • Kern, G., N. Schülke, F. X. Schmid, and R. Jaenicke. 1992. Stability, quaternary structure, and folding of internal, external, and coreglycosylated invertase from yeast. Protein Sci. 1, 120-131.
    • (1992) Protein Sci. , vol.1 , pp. 120-131
    • Kern, G.1    Schülke, N.2    Schmid, F.X.3    Jaenicke, R.4
  • 26
    • 0031468584 scopus 로고    scopus 로고
    • Cellobiohydrolase I from Trichoderma reesei: Identification of an active-site nucelophile and additional information on sequence including the glycosylation pattern for the core protein
    • Klarskov, K., K. Piens, J. Stahlberg, P. B. Hoj, J. M. van Beeumen, and M. Claeyssens. 1997. Cellobiohydrolase I from Trichoderma reesei: Identification of an active-site nucelophile and additional information on sequence including the glycosylation pattern for the core protein. Carbohydr. Res. 304, 143-154.
    • (1997) Carbohydr. Res. , vol.304 , pp. 143-154
    • Klarskov, K.1    Piens, K.2    Stahlberg, J.3    Hoj, P.B.4    van Beeumen, J.M.5    Claeyssens, M.6
  • 27
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lingocellulosic biomass: Biochemical and molecular perspectives
    • Kumar, R., S. Singh, and O. V. Singh. 2008. Bioconversion of lingocellulosic biomass: biochemical and molecular perspectives. J. Ind. Microbiol. Biotechnol. 35, 377-391.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 28
    • 52949122139 scopus 로고    scopus 로고
    • Production and characteristics comparison of crude β-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes
    • Leite, R. S. R., H. F. Alves-Prado, H. Cabral, F. C. Pagnocca, E. Gomes, and R. Da-Silva. 2008. Production and characteristics comparison of crude β-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes. Enzyme Microb. Technol. 43, 391-395.
    • (2008) Enzyme Microb. Technol. , vol.43 , pp. 391-395
    • Leite, R.S.R.1    Alves-Prado, H.F.2    Cabral, H.3    Pagnocca, F.C.4    Gomes, E.5    Da-Silva, R.6
  • 30
    • 0035242417 scopus 로고    scopus 로고
    • The effects of the sitedirected removal of N-glycosylation from cationic peanut peroxidase on its function
    • Lige, B., S. Ma, and R. B. van Huystee. 2001. The effects of the sitedirected removal of N-glycosylation from cationic peanut peroxidase on its function. Arch. Biochem. Biophys. 386, 17-24.
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 17-24
    • Lige, B.1    Ma, S.2    van Huystee, R.B.3
  • 31
    • 0032838958 scopus 로고    scopus 로고
    • Purification and biochemical characteristics of β-D-glucosidase from a thermophilic fungus Thermomyces lanuginosus-SSBP
    • Lin, J., B. Pillay, and S. Singh. 1999. Purification and biochemical characteristics of β-D-glucosidase from a thermophilic fungus Thermomyces lanuginosus-SSBP. Biotechnol. Appl. Biochem. 30, 81-87.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 81-87
    • Lin, J.1    Pillay, B.2    Singh, S.3
  • 34
    • 3142741699 scopus 로고
    • Localization of carbohydrases at the surface of fungus spores by acid treatment
    • Mandels, G. R. 1953. Localization of carbohydrases at the surface of fungus spores by acid treatment. Exp. Cell Res. 5, 48-55.
    • (1953) Exp. Cell Res. , vol.5 , pp. 48-55
    • Mandels, G.R.1
  • 35
    • 0030957795 scopus 로고    scopus 로고
    • Structural characterization of Nlinked oligosaccharides from cellobiohydrolase secreted by filamentous fungi Trichoderma reesei Rut-C-30
    • Maras, M., A. DeBruyn, J. Schraml, P. Herdewijn, M. Claeyssens, W. Fiers, and R. Contreras. 1997. Structural characterization of Nlinked oligosaccharides from cellobiohydrolase secreted by filamentous fungi Trichoderma reesei Rut-C-30. Eur. J. Biochem. 245, 617-625.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 617-625
    • Maras, M.1    Debruyn, A.2    Schraml, J.3    Herdewijn, P.4    Claeyssens, M.5    Fiers, W.6    Contreras, R.7
  • 37
    • 0027995966 scopus 로고
    • Different effects of Nglycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-β-glucananases secreted from yeast
    • Meldgaard, M. and I. Svendsen. 1994. Different effects of Nglycosylation on the thermostability of highly homologous bacterial (1, 3-1, 4)-β-glucananases secreted from yeast. Microbiology 140, 159-166.
    • (1994) Microbiology , vol.140 , pp. 159-166
    • Meldgaard, M.1    Svendsen, I.2
  • 38
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 31, 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 39
    • 33646190494 scopus 로고    scopus 로고
    • Purification and characterization of an intracellular enzyme with β-glucosidase and β-galactosidase activity from the thermophilic fungus Talaromyces thermophilus CBS 236.58
    • Nakkharat, P. and D. Haltrich. 2006. Purification and characterization of an intracellular enzyme with β-glucosidase and β-galactosidase activity from the thermophilic fungus Talaromyces thermophilus CBS 236. 58. J. Biotechnol. 123, 304-313.
    • (2006) J. Biotechnol. , vol.123 , pp. 304-313
    • Nakkharat, P.1    Haltrich, D.2
  • 40
    • 0031980657 scopus 로고    scopus 로고
    • Technical communication: Survey and analysis of commercial cellulose preparations suitable for biomass conversion to ethanol
    • Nieves, R. A., C. I. Ehrman, W. S. Adney, R. T. Elander, and M. E. Himmel. 1998. Technical communication: Survey and analysis of commercial cellulose preparations suitable for biomass conversion to ethanol. World J. Microbiol. Biotechnol. 14, 301-304.
    • (1998) World J. Microbiol. Biotechnol. , vol.14 , pp. 301-304
    • Nieves, R.A.1    Ehrman, C.I.2    Adney, W.S.3    Elander, R.T.4    Himmel, M.E.5
  • 41
    • 0005812912 scopus 로고
    • Isolation of Streptomyces sp. producing glucose-tolerant β-glucosidases and properties of the enzymes
    • Osaki, H. and K. Yamada. 1991. Isolation of Streptomyces sp. producing glucose-tolerant β-glucosidases and properties of the enzymes. Agric. Biol. Chem. 55, 979-987.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 979-987
    • Osaki, H.1    Yamada, K.2
  • 42
    • 0035156434 scopus 로고    scopus 로고
    • Biochemical characterization and mechanisms of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus
    • Parry, N. J., D. E. Beever, E. Owen, I. Vandenberghe, J. van Beeumen, and M. K. Bhat. 2001. Biochemical characterization and mechanisms of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus. Biochem. J. 353, 117-127.
    • (2001) Biochem. J. , vol.353 , pp. 117-127
    • Parry, N.J.1    Beever, D.E.2    Owen, E.3    Vandenberghe, I.4    van Beeumen, J.5    Bhat, M.K.6
  • 43
    • 0031016918 scopus 로고    scopus 로고
    • A highly thermostable β-glucosidase activity from the thermophilic fungus Humicola grisea var. thermoidea: Purification and biochemical characterization
    • Peralta, R. M., M. K. Kadowaki, H. F. Terenzi, and J. A. Jorge. 1997. A highly thermostable β-glucosidase activity from the thermophilic fungus Humicola grisea var. thermoidea: purification and biochemical characterization. FEMS Microbiol. Lett. 146, 291-295.
    • (1997) FEMS Microbiol. Lett. , vol.146 , pp. 291-295
    • Peralta, R.M.1    Kadowaki, M.K.2    Terenzi, H.F.3    Jorge, J.A.4
  • 44
    • 0025137168 scopus 로고
    • β-Glycosidase activities of Humicola grisea: Biochemical and kinetic characterization of a multifunctional enzyme
    • Peralta, R. M., H. F. Terenzi, and J. A. Jorge. 1990. β-Glycosidase activities of Humicola grisea: biochemical and kinetic characterization of a multifunctional enzyme. Biochim. Biophys. Acta. 1033, 243-249.
    • (1990) Biochim. Biophys. Acta. , vol.1033 , pp. 243-249
    • Peralta, R.M.1    Terenzi, H.F.2    Jorge, J.A.3
  • 45
    • 0029100735 scopus 로고
    • Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)
    • Perez-Pons, J. A., X. Rebordosa, and E. Querol. 1995. Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238). Biochim. Biophys. Acta. 1251, 145-153.
    • (1995) Biochim. Biophys. Acta. , vol.1251 , pp. 145-153
    • Perez-Pons, J.A.1    Rebordosa, X.2    Querol, E.3
  • 46
    • 17544362056 scopus 로고    scopus 로고
    • Effect of carbon source on the β-glucosidase system of the thermophilic fungus Humicola grisea
    • Polizeli, M. L. T. M., J. A. Jorge, and H. F. Terenzi. 1996. Effect of carbon source on the β-glucosidase system of the thermophilic fungus Humicola grisea. World J. Microbiol. Biotechnol. 12, 297-299.
    • (1996) World J. Microbiol. Biotechnol. , vol.12 , pp. 297-299
    • Polizeli, M.L.T.M.1    Jorge, J.A.2    Terenzi, H.F.3
  • 47
    • 0024153519 scopus 로고
    • Purification and characterization of a beta-glucosidase and endocellulase from Humicola insolens
    • Rao, U. S. and S. K. Murthy. 1988. Purification and characterization of a beta-glucosidase and endocellulase from Humicola insolens. Indian J. Biochem. Biophys. 25, 687-694.
    • (1988) Indian J. Biochem. Biophys. , vol.25 , pp. 687-694
    • Rao, U.S.1    Murthy, S.K.2
  • 48
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae
    • Riou, C., J. M. Salmon, M. J. Vallier, Z. Günata, and P. Bare. 1998. Purification, characterization and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae. Appl. Environ. Microbiol. 64, 3607-3614.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.M.2    Vallier, M.J.3    Günata, Z.4    Bare, P.5
  • 49
    • 0030063336 scopus 로고    scopus 로고
    • Glucose tolerant and thermophilic β-glucosidases from yeasts
    • Saha, B. C. and R. J. Bothast. 1996a. Glucose tolerant and thermophilic β-glucosidases from yeasts. Biotechnol. Lett. 18, 155-158.
    • (1996) Biotechnol. Lett. , vol.18 , pp. 155-158
    • Saha, B.C.1    Bothast, R.J.2
  • 50
    • 0029786225 scopus 로고    scopus 로고
    • Production, purification and characterization of a highly glucose-tolerant novel β-glucosidase from Candida peltata
    • Saha, B. C. and R. J. Bothast. 1996b. Production, purification and characterization of a highly glucose-tolerant novel β-glucosidase from Candida peltata. Appl. Environ. Microbiol. 62, 3165-3170.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3165-3170
    • Saha, B.C.1    Bothast, R.J.2
  • 52
    • 42049095517 scopus 로고    scopus 로고
    • Identification of glucose tolerant acid active β-glucosidases from thermophilic and thermotolerant fungi
    • Sonia, K. G., B. S. Chadha, A. K. Badhan, H. S. Saini, and M. K. Bhat. 2008. Identification of glucose tolerant acid active β-glucosidases from thermophilic and thermotolerant fungi. World J. Microbiol. Biotechnol. 24, 599-604.
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , pp. 599-604
    • Sonia, K.G.1    Chadha, B.S.2    Badhan, A.K.3    Saini, H.S.4    Bhat, M.K.5
  • 53
    • 4444371517 scopus 로고    scopus 로고
    • Factors influencing glycosylation of Trichoderma reesei cellulases. II: N-glycosylation of Cel7A core protein isolated from different strains
    • Stals, I., K. Sandra, B. Devreese, J. van Beeumen, and M. Claeyssens. 2004a. Factors influencing glycosylation of Trichoderma reesei cellulases. II: N-glycosylation of Cel7A core protein isolated from different strains. Glycobiology 14, 725-737.
    • (2004) Glycobiology , vol.14 , pp. 725-737
    • Stals, I.1    Sandra, K.2    Devreese, B.3    van Beeumen, J.4    Claeyssens, M.5
  • 54
    • 1942486976 scopus 로고    scopus 로고
    • Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretorial changes of the O- and N-glycosylation pattern of Cel7A
    • Stals, I., K. Sandra, S. Geysens, R. Contreras, J. van Beeumen, and M. Claeyssens. 2004b. Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretorial changes of the O- and N-glycosylation pattern of Cel7A. Glycobiology 14, 713-724.
    • (2004) Glycobiology , vol.14 , pp. 713-724
    • Stals, I.1    Sandra, K.2    Geysens, S.3    Contreras, R.4    van Beeumen, J.5    Claeyssens, M.6
  • 55
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. 1993. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 56
    • 0036005993 scopus 로고    scopus 로고
    • Extracellular β-D-glucosidase from Chaetomium thermophilum var. coprophilum: Production, purification and some biochemical properties
    • Venturi, L. L., M. L. T. M. Polizeli, H. F. Terenzi, R. P. M. Furriel, and J. A. Jorge. 2002. Extracellular β-D-glucosidase from Chaetomium thermophilum var. coprophilum: production, purification and some biochemical properties. J. Basic Microbiol. 42, 55-66.
    • (2002) J. Basic Microbiol. , vol.42 , pp. 55-66
    • Venturi, L.L.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Furriel, R.P.M.4    Jorge, J.A.5
  • 57
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. and M. Osborn. 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 58
    • 0026443120 scopus 로고
    • Cloning, characterization, nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli
    • Wright, R. M., M. D. Yablonsky, Z. P. Shalita, A. K. Goyal, and D. E. Eveleigh. 1992. Cloning, characterization, nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable β-glucosidase expressed in Escherichia coli. Appl. Environ. Microbiol. 58, 3455-3465.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3455-3465
    • Wright, R.M.1    Yablonsky, M.D.2    Shalita, Z.P.3    Goyal, A.K.4    Eveleigh, D.E.5
  • 59
    • 38949170567 scopus 로고    scopus 로고
    • Characterization of a thermostable extracellular β-glucosidase with activities of exoglucanase and transglycosylation from Paecilomyces thermophila
    • Yang, S., Z. Jiang, Q. Yan, and H. Zhu. 2008. Characterization of a thermostable extracellular β-glucosidase with activities of exoglucanase and transglycosylation from Paecilomyces thermophila. J. Agric. Food Chem. 56, 602-608.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 602-608
    • Yang, S.1    Jiang, Z.2    Yan, Q.3    Zhu, H.4
  • 60
    • 43249094258 scopus 로고    scopus 로고
    • Purification and characterization of thermostable β-glucosidase from the brown-rot basidiomycete Fomitopsis palustris grown on microcrystalline cellulose
    • Yoon, J. J., K. Y. Kim, and C. J. Cha. 2008. Purification and characterization of thermostable β-glucosidase from the brown-rot basidiomycete Fomitopsis palustris grown on microcrystalline cellulose. J. Microbiol. 46, 51-55.
    • (2008) J. Microbiol. , vol.46 , pp. 51-55
    • Yoon, J.J.1    Kim, K.Y.2    Cha, C.J.3
  • 61
    • 7644238142 scopus 로고    scopus 로고
    • β-Glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose
    • Zanoelo, F. F., M. L. T. M. Polizeli, H. F. Terenzi, and J. A. Jorge. 2004. β-Glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose. FEMS Microbiol. Lett. 240, 137-143.
    • (2004) FEMS Microbiol. Lett. , vol.240 , pp. 137-143
    • Zanoelo, F.F.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 62
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: Screening and selection strategies
    • Zhang, Y. H. P., 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
    • Zhang, Y.H.P.1    Himmel, M.E.2    Mielenz, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.