메뉴 건너뛰기




Volumn 83, Issue 1, 2010, Pages 74-81

A method of purification, identification and characterization of β-glucosidase from Trichoderma koningii AS3.2774

Author keywords

glucosidase; Electroelution; Native gradient polyacrylamide gel electrophoresis; Trichoderma koningii

Indexed keywords

BETA GLUCOSIDASE; CELLULASE;

EID: 77956414224     PISSN: 01677012     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mimet.2010.07.019     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 33750987679 scopus 로고    scopus 로고
    • Characterization of a novel β-glucosidase from a Stachybotrys strain
    • Amouri B., Gargouri A. Characterization of a novel β-glucosidase from a Stachybotrys strain. Biochem. Eng. J. 2006, 32:191-197.
    • (2006) Biochem. Eng. J. , vol.32 , pp. 191-197
    • Amouri, B.1    Gargouri, A.2
  • 2
    • 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. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0013667384 scopus 로고
    • Purification and properties of an extracellular β-glucosidase from the cellulolytic thermophile Clostridium stercorarium
    • Bronnenmeier K., Staudenbauer W.L. Purification and properties of an extracellular β-glucosidase from the cellulolytic thermophile Clostridium stercorarium. Appl. Microbiol. Biotechnol. 1988, 28:380-386.
    • (1988) Appl. Microbiol. Biotechnol. , vol.28 , pp. 380-386
    • Bronnenmeier, K.1    Staudenbauer, W.L.2
  • 4
    • 0032007604 scopus 로고    scopus 로고
    • β-Glucosidase components of the cellulolytic system of the edible straw mushroom, Volvariella volvacea
    • Cai Y.J., Buswell J.A., Chang S.T. β-Glucosidase components of the cellulolytic system of the edible straw mushroom, Volvariella volvacea. Enzyme Microb. Technol. 1998, 22:122-129.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 122-129
    • Cai, Y.J.1    Buswell, J.A.2    Chang, S.T.3
  • 5
    • 0027535162 scopus 로고
    • Purification and some properties of β-glucosidase from the ectomycorrhizal fungus Pisolithus tinctorius strain SMF
    • Cao W., Crawford D.L. Purification and some properties of β-glucosidase from the ectomycorrhizal fungus Pisolithus tinctorius strain SMF. Can. J. Microbiol. 1993, 1:125-129.
    • (1993) Can. J. Microbiol. , vol.1 , pp. 125-129
    • Cao, W.1    Crawford, D.L.2
  • 6
    • 0018082362 scopus 로고
    • Production, purification and partial characterization of 1,4-β-glucosidase enzymes from Sporotrichum pulverulentum
    • Deshpande V., Eriksson K.E., Pettersson B. Production, purification and partial characterization of 1,4-β-glucosidase enzymes from Sporotrichum pulverulentum. Eur. J. Biochem. 1978, 90:191-198.
    • (1978) Eur. J. Biochem. , vol.90 , pp. 191-198
    • Deshpande, V.1    Eriksson, K.E.2    Pettersson, B.3
  • 7
    • 84943470296 scopus 로고
    • Measurement of cellulase activities
    • Ghose T.K. Measurement of cellulase activities. Pure Appl. Chem. 1987, 59:257-268.
    • (1987) Pure Appl. Chem. , vol.59 , pp. 257-268
    • Ghose, T.K.1
  • 8
    • 0017394722 scopus 로고
    • Cellobiase from Trichoderma viride: purification, properties, kinetics, and mechanism
    • Gong C.S., Ladisch M.R., Tsao G.T. Cellobiase from Trichoderma viride: purification, properties, kinetics, and mechanism. Biotechnol. Bioeng. 1977, 19:959-981.
    • (1977) Biotechnol. Bioeng. , vol.19 , pp. 959-981
    • Gong, C.S.1    Ladisch, M.R.2    Tsao, G.T.3
  • 9
    • 0036105886 scopus 로고    scopus 로고
    • Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable β-glycosidases
    • Hanssona T., Adlercreutza P. Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable β-glycosidases. Biocatal. Biotransform. 2002, 20:167-178.
    • (2002) Biocatal. Biotransform. , vol.20 , pp. 167-178
    • Hanssona, T.1    Adlercreutza, P.2
  • 10
    • 33747590965 scopus 로고    scopus 로고
    • Technical innovations for the automated identification of gel-separated proteins by MALDI-TOF mass spectrometry
    • Jahn O., Hesse D., Reinelt M., Kratzin H.D. Technical innovations for the automated identification of gel-separated proteins by MALDI-TOF mass spectrometry. Anal. Bioanal. Chem. 2006, 386:92-103.
    • (2006) Anal. Bioanal. Chem. , vol.386 , pp. 92-103
    • Jahn, O.1    Hesse, D.2    Reinelt, M.3    Kratzin, H.D.4
  • 11
    • 67349195285 scopus 로고    scopus 로고
    • Purification and characterization of a β-1,4-glucosidase from a newly isolated strain of Fomitopsis pinicola
    • Joo A.R., Jeya M., Lee K.M., Sim W.I., Kim J.S., Kim I.W., et al. Purification and characterization of a β-1,4-glucosidase from a newly isolated strain of Fomitopsis pinicola. Appl. Microbiol. Biotechnol. 2009, 83:285-294.
    • (2009) Appl. Microbiol. Biotechnol. , vol.83 , pp. 285-294
    • Joo, A.R.1    Jeya, M.2    Lee, K.M.3    Sim, W.I.4    Kim, J.S.5    Kim, I.W.6
  • 12
    • 0030829823 scopus 로고    scopus 로고
    • Analysis of the chloroplast protein complexes by blue-native polyacrylamide gel electrophoresis (BN-PAGE)
    • Kügler M., Jänsch L., Kruft V., Schmitz U.K., Braun H.P. Analysis of the chloroplast protein complexes by blue-native polyacrylamide gel electrophoresis (BN-PAGE). Photosynth. Res. 1997, 53:35-44.
    • (1997) Photosynth. Res. , vol.53 , pp. 35-44
    • Kügler, M.1    Jänsch, L.2    Kruft, V.3    Schmitz, U.K.4    Braun, H.P.5
  • 13
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen S.W., Luesink E.J., Stams A.J., Zehnder A.J. Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 1993, 213:305-312.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.1    Luesink, E.J.2    Stams, A.J.3    Zehnder, A.J.4
  • 14
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0032838958 scopus 로고    scopus 로고
    • Purification and biochemical characteristics of beta-d-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP
    • Lin J., Pillay B., Singh S. Purification and biochemical characteristics of beta-d-glucosidase from a thermophilic fungus, Thermomyces lanuginosus-SSBP. Biotechnol. Appl. Biochem. 1999, 30:81-87.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 81-87
    • Lin, J.1    Pillay, B.2    Singh, S.3
  • 16
    • 70349320162 scopus 로고    scopus 로고
    • Induction of cellulase gene transcription by a novel oligosaccharide: molasses alcohol stillage substance
    • Ling M., Chen G., Lin Y., Liang Z. Induction of cellulase gene transcription by a novel oligosaccharide: molasses alcohol stillage substance. World J. Microbiol. Biotechnol. 2009, 25:1485-1489.
    • (2009) World J. Microbiol. Biotechnol. , vol.25 , pp. 1485-1489
    • Ling, M.1    Chen, G.2    Lin, Y.3    Liang, Z.4
  • 17
    • 0000992883 scopus 로고
    • Sophorose as an inducer of cellulase in Trichoderma reesei
    • Mandels M., Parrish F.W., Reese E.T. Sophorose as an inducer of cellulase in Trichoderma reesei. J. Bacteriol. 1962, 83:400-408.
    • (1962) J. Bacteriol. , vol.83 , pp. 400-408
    • Mandels, M.1    Parrish, F.W.2    Reese, E.T.3
  • 19
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250:4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.1
  • 20
    • 0011478079 scopus 로고
    • Preparative purification of Trichoderma reesei native and "core" cellobiohydrolase I by electrophoresis and chromatofocusing
    • Offord D., Lee N., Woodward J. Preparative purification of Trichoderma reesei native and "core" cellobiohydrolase I by electrophoresis and chromatofocusing. Appl. Biochem. Biotechnol. 1991, 28-29:377-386.
    • (1991) Appl. Biochem. Biotechnol. , pp. 377-386
    • Offord, D.1    Lee, N.2    Woodward, J.3
  • 21
    • 0031305765 scopus 로고    scopus 로고
    • Purification and characterization of a β-glucosidase from Aspergillus niger
    • Rashid M.H., Siddiqui K.S. Purification and characterization of a β-glucosidase from Aspergillus niger. Folia Microbiol. 1997, 42:544-550.
    • (1997) Folia Microbiol. , vol.42 , pp. 544-550
    • Rashid, M.H.1    Siddiqui, K.S.2
  • 23
    • 51249168694 scopus 로고
    • Electrophoretic isolation of membrane proteins from acrylamide gels
    • Schägger H. Electrophoretic isolation of membrane proteins from acrylamide gels. Appl. Biochem. Biotechnol. 1994, 48:185-203.
    • (1994) Appl. Biochem. Biotechnol. , vol.48 , pp. 185-203
    • Schägger, H.1
  • 24
    • 0028848239 scopus 로고
    • Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes
    • Schagger H. Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes. Methods Enzymol. 1995, 260:190-202.
    • (1995) Methods Enzymol. , vol.260 , pp. 190-202
    • Schagger, H.1
  • 25
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger H., Cramer W.A., von Jagow G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 1994, 217:220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 26
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 1987, 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 27
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H., von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199:223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 28
    • 4043138347 scopus 로고    scopus 로고
    • Purifying proteins for proteomics: a laboratory manual
    • Cold Spring Harbor Laboratory Press, New York, R.J. Simpson (Ed.)
    • Simpson R.J. Purifying proteins for proteomics: a laboratory manual. Chromatographic Methods for Preparing Proteins for Proteomics 2004, 39-80. Cold Spring Harbor Laboratory Press, New York. R.J. Simpson (Ed.).
    • (2004) Chromatographic Methods for Preparing Proteins for Proteomics , pp. 39-80
    • Simpson, R.J.1
  • 30
    • 0041926672 scopus 로고    scopus 로고
    • Purification, characterization, cDNA cloning and nucleotide sequencing of a cellulase from the yellow-spotted longicorn beetle, Psacothea hilaris
    • Sugimura M., Watanabe H., Lo N., Saito H. Purification, characterization, cDNA cloning and nucleotide sequencing of a cellulase from the yellow-spotted longicorn beetle, Psacothea hilaris. Eur. J. Biochem. 2003, 270:3455-3460.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3455-3460
    • Sugimura, M.1    Watanabe, H.2    Lo, N.3    Saito, H.4
  • 31
    • 0343003867 scopus 로고    scopus 로고
    • Function, structure and regulation of cyanobacterial and chloroplast ATP synthase
    • Walraven H.S., Bakels R.H.A. Function, structure and regulation of cyanobacterial and chloroplast ATP synthase. Physiol. Plantarum. 1996, 96:526-532.
    • (1996) Physiol. Plantarum. , vol.96 , pp. 526-532
    • Walraven, H.S.1    Bakels, R.H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.