메뉴 건너뛰기




Volumn 47, Issue 3, 2009, Pages 270-276

Effect of glycosylation on the biochemical properties of β-xylosidases from Aspergillus versicolor

Author keywords

xylosidase; Deglycosylation; Glycoprotein; Glycosylation; Xylobiase

Indexed keywords

ASPERGILLUS; ASPERGILLUS VERSICOLOR;

EID: 68349119239     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-008-0286-9     Document Type: Article
Times cited : (20)

References (30)
  • 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
    • 0026450509 scopus 로고
    • Purification and characterization of β-xylosidase activities from the yeast Arxula adeninivorans
    • Bütner, R. and R. Bode. 1992. Purification and characterization of β-xylosidase activities from the yeast Arxula adeninivorans. J. Basic Microbiol. 32, 159-166.
    • (1992) J. Basic Microbiol. , vol.32 , pp. 159-166
    • Bütner, R.1    Bode, R.2
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0025782660 scopus 로고
    • Purification and characterization of β-xylosidase from Aureobasidium pullulans
    • Dobberstein, J. and C.C. Emeis. 1991. Purification and characterization of β-xylosidase from Aureobasidium pullulans. Appl. Microbiol. Biotechnol. 35, 210-215.
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 210-215
    • Dobberstein, J.1    Emeis, C.C.2
  • 8
    • 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
  • 9
    • 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
  • 10
    • 0027050823 scopus 로고
    • Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeast
    • Kern, G., N. Schülke, F.X. Schmid, and R. Jaenicke. 1992. Stability, quaternary structure, and folding of internal, external, and core-glycosylated 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
  • 11
    • 0031468584 scopus 로고    scopus 로고
    • Cellobiohydrolase I from Trichoederma reesei: Identification of an active-site nucelophile and additional information on sequence including the glycosylation pattern for the core protein
    • Klarskov, K., K.K. Piens, J. Stahlberg, P.B. Hoj, J.M. van Beeumen, and M. Claeyssens. 1997. Cellobiohydrolase I from Trichoederma 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.K.2    Stahlberg, J.3    Hoj, P.B.4    van Beeumen, J.M.5    Claeyssens, M.6
  • 12
    • 0028984122 scopus 로고
    • Regulation of β-ylosidase formation by xylose in Trichoderma reesei
    • Kristufek, D., S. Zellinger, and C.P. Kubicek. 1995. Regulation of β-ylosidase formation by xylose in Trichoderma reesei. Appl. Microbiol. Biotechnol. 42, 713-717.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 713-717
    • Kristufek, D.1    Zellinger, S.2    Kubicek, C.P.3
  • 13
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnolological aspects of xylanase
    • Kulkarni, N., A. Shendye, and M. Rao. 1999. Molecular and biotechnolological aspects of xylanase. FEMS Microbiol. Rev. 23, 411-456.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0035242417 scopus 로고    scopus 로고
    • The effects of the site-directed 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 site-directed 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
  • 17
    • 3142741699 scopus 로고
    • Localization of carbohydrases at surface of fungus spores by acid treatment
    • Mandels, G.R. 1953. Localization of carbohydrases at 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
  • 18
    • 0030957795 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides from cellobiohydrolase secreted by filamentous fungi Trichoderma reesei Rut-C-30
    • Maras, M., A. De Bruyn, J. Schraml, P. Herdewijn, M. Claeyssens, W. Fiers, and R. Contreras. 1997. Structural characterization of N-linked 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    De Bruyn, A.2    Schraml, J.3    Herdewijn, P.4    Claeyssens, M.5    Fiers, W.6    Contreras, R.7
  • 19
    • 0027995966 scopus 로고
    • Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-β-glucanases secreted from yeast
    • Meldgaard, M. and I. Svendsen. 1994. Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-β-glucanases secreted from yeast. Microbiology 140, 159-166.
    • (1994) Microbiology , vol.140 , pp. 159-166
    • Meldgaard, M.1    Svendsen, I.2
  • 21
    • 45949126832 scopus 로고
    • Evaluation of different microbial xylanolytic systems
    • Poutanen, K., P. Ratto, and L. Viikari. 1987. Evaluation of different microbial xylanolytic systems. J. Biotechnol. 6, 49-60.
    • (1987) J. Biotechnol. , vol.6 , pp. 49-60
    • Poutanen, K.1    Ratto, P.2    Viikari, L.3
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0025233340 scopus 로고
    • Formation of deglycosylated α-L-fucosidase by endo-β-N-acetylglucosaminidase in Fusarium oxysporum
    • Tsuji T., K. Yamamoto, and T. Tochikura. 1990. Formation of deglycosylated α-L-fucosidase by endo-β-N-acetylglucosaminidase in Fusarium oxysporum. Appl. Environ. Microbiol. 56, 928-933.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 928-933
    • Tsuji, T.1    Yamamoto, K.2    Tochikura, T.3
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora (medium N)
    • Vogel, H.J.A. 1956. A convenient growth medium for Neurospora (medium N). Microbial Genet. Bull. 37, 387-394.
    • (1956) Microbial Genet. Bull. , vol.37 , pp. 387-394
    • Vogel, H.J.A.1
  • 28
    • 0024087074 scopus 로고    scopus 로고
    • Multiplicity of β-1,4-xylanases in microorganisms: Functions and applications
    • Wong, K.K.Y., L.U.L. Tan, and J.N. Saddler. 1998. Multiplicity of β-1,4-xylanases in microorganisms: functions and applications. Microbiol. Rev. 52, 305-317.
    • (1998) Microbiol. Rev. , vol.52 , pp. 305-317
    • Wong, K.K.Y.1    Tan, L.U.L.2    Saddler, J.N.3
  • 29
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., T. Boulikas, V.P. Wray, and R. Hancock. 1981. Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118, 197-203.
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 30
    • 3142674377 scopus 로고    scopus 로고
    • Purification and biochemical properties of a thermostable xylose-tolerant β-D-xylosidase from Scytalidium thermophilum
    • Zanoelo, F.F., M.L.T.M. Polizeli, H.F. Terenzi, and J.A. Jorge. 2004. Purification and biochemical properties of a thermostable xylose-tolerant β-D-xylosidase from Scytalidium thermophilum. J. Ind. Microbiol. Biotechnol. 31, 170-176.
    • (2004) J. Ind. Microbiol. Biotechnol. , vol.31 , pp. 170-176
    • Zanoelo, F.F.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.