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Volumn 23, Issue 9, 2007, Pages 1297-1303

Purification and partial characterization of β-1,3-glucanase from Chaetomium thermophilum

Author keywords

Chaetomium thermophilum; Purification; Thermostable 1,3 glucanase

Indexed keywords

CATALYST ACTIVITY; MOLECULAR WEIGHT; PROTEINS; PURIFICATION;

EID: 34547837398     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-007-9366-y     Document Type: Article
Times cited : (12)

References (35)
  • 1
  • 3
    • 0028895388 scopus 로고
    • Isolation of extracellular 28- and 42 kilodalton β-1,3-glucanases and comparison of three β-1,3-glucanases produced by Bacillus circulans IAM1165
    • Aono R, Hammuram M, Yamamoto M, Asano T (1995) Isolation of extracellular 28- and 42 kilodalton β-1,3-glucanases and comparison of three β-1,3-glucanases produced by Bacillus circulans IAM1165. Appl Environ Microbiol 61:122-129
    • (1995) Appl Environ Microbiol , vol.61 , pp. 122-129
    • Aono, R.1    Hammuram, M.2    Yamamoto, M.3    Asano, T.4
  • 4
    • 0032439268 scopus 로고    scopus 로고
    • Characterization of an endo-1,3-(-D-glucanase produced during the interaction between the mycoparasite Stachybotrys elegans and its host Rhizoctonia solani
    • Archambault C, Coloccia P, Kermasha S, Jabaji-Hare S (1998) Characterization of an endo-1,3-(-D-glucanase produced during the interaction between the mycoparasite Stachybotrys elegans and its host Rhizoctonia solani. Can J Microbiol 44:989-997
    • (1998) Can J Microbiol , vol.44 , pp. 989-997
    • Archambault, C.1    Coloccia, P.2    Kermasha, S.3    Jabaji-Hare, S.4
  • 5
    • 0031717013 scopus 로고    scopus 로고
    • Purification and characterization of laccase from Chaetomium thermophilum and its role in humification
    • Benny C, Yona C, Yitzhak H (1998) Purification and characterization of laccase from Chaetomium thermophilum and its role in humification. Appl Environ Microbiol 64:3175-3179
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3175-3179
    • Benny, C.1    Yona, C.2    Yitzhak, H.3
  • 6
    • 0000002475 scopus 로고
    • Determination of glucose with oxidase and peroxidase
    • Bergmeyer HU, Bernt E (1974) Determination of glucose with oxidase and peroxidase. Method Enzym Anal 3:1205-1215
    • (1974) Method Enzym Anal , vol.3 , pp. 1205-1215
    • Bergmeyer, H.U.1    Bernt, E.2
  • 7
    • 25444432792 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable glucoamylase from Chaetomium thermophilum
    • Chen J, Li DC, Zhang YQ, Zhou QX (2005) Purification and characterization of a thermostable glucoamylase from Chaetomium thermophilum. J General Appl Microbiol 51:175-181
    • (2005) J General Appl Microbiol , vol.51 , pp. 175-181
    • Chen, J.1    Li, D.C.2    Zhang, Y.Q.3    Zhou, Q.X.4
  • 8
    • 0033590589 scopus 로고    scopus 로고
    • Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum
    • Cohen-Kupiec R, Broglie KE, Friesem D, Broglie RM, Chet I (1999) Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum. Gene 226:147-154
    • (1999) Gene , vol.226 , pp. 147-154
    • Cohen-Kupiec, R.1    Broglie, K.E.2    Friesem, D.3    Broglie, R.M.4    Chet, I.5
  • 9
    • 0028970716 scopus 로고
    • A novel endo-β-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum
    • De La Cruz J, Pintor-Toro JA, Benítez T, Llobell A, Romero LC (1995) A novel endo-β-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum. J Bacteriol 177:6937-6945
    • (1995) J Bacteriol , vol.177 , pp. 6937-6945
    • De La Cruz, J.1    Pintor-Toro, J.A.2    Benítez, T.3    Llobell, A.4    Romero, L.C.5
  • 10
    • 0031038378 scopus 로고    scopus 로고
    • Purification and characterization of an endo-1,3-β-glucanase from Aspergillus fumigatus
    • Fontaine T, Hartland R, Beauvais A, Diaquin M, Latgé JP (1997) Purification and characterization of an endo-1,3-β-glucanase from Aspergillus fumigatus. Eur J Biochem 243:315-321
    • (1997) Eur J Biochem , vol.243 , pp. 315-321
    • Fontaine, T.1    Hartland, R.2    Beauvais, A.3    Diaquin, M.4    Latgé, J.P.5
  • 11
    • 0001688329 scopus 로고
    • Purification and characterization of two xylanase from Chaetomium thermophile var. coprophile
    • Ganju RK, Vithayathil PJ, Murthy SK (1989) Purification and characterization of two xylanase from Chaetomium thermophile var. coprophile. Can J Microbiol 35:836-842
    • (1989) Can J Microbiol , vol.35 , pp. 836-842
    • Ganju, R.K.1    Vithayathil, P.J.2    Murthy, S.K.3
  • 12
    • 0031437663 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endo-β-1,3- glucanase of the hyperthermophilic archaeon Pyrococcus furiosus
    • Gueguen Y, Voorhorst WGB, Van Der Oost J, De Vos WM (1997) Molecular and biochemical characterization of an endo-β-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 272:31258-31264
    • (1997) J Biol Chem , vol.272 , pp. 31258-31264
    • Gueguen, Y.1    Voorhorst, W.G.B.2    Van Der Oost, J.3    De Vos, W.M.4
  • 13
    • 0021043910 scopus 로고
    • Separation and characterization of six (1-3)-β-glucanases from Saccharomyces cerevisiae
    • Hien NH, Fleet GH (1983) Separation and characterization of six (1-3)-β-glucanases from Saccharomyces cerevisiae. J Bacteriol 156:1204-1213
    • (1983) J Bacteriol , vol.156 , pp. 1204-1213
    • Hien, N.H.1    Fleet, G.H.2
  • 14
    • 0024698885 scopus 로고
    • Purification of (1, 3)-β-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone
    • Hoj PB, Hartman DJ, Morrice NA, Doan DN, Fincher GB (1989) Purification of (1, 3)-β-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone. Plant Mol Biol 13:31-42.
    • (1989) Plant Mol Biol , vol.13 , pp. 31-42
    • Hoj, P.B.1    Hartman, D.J.2    Morrice, N.A.3    Doan, D.N.4    Fincher, G.B.5
  • 15
    • 0027439791 scopus 로고
    • Purification and properties of three (1-3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • Hrmova M, Fincher GB (1993) Purification and properties of three (1-3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare). Biochem J 289:453-461
    • (1993) Biochem J , vol.289 , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 16
    • 0018876847 scopus 로고
    • The extracellular system of (-1,3-glucanases of Alternaria tenuissima and Aspergillus versicolor
    • Jirku V, Kraxnerova B, Krumphanzl V (1980) The extracellular system of (-1,3-glucanases of Alternaria tenuissima and Aspergillus versicolor. Folia Microbiol 25:24-31
    • (1980) Folia Microbiol , vol.25 , pp. 24-31
    • Jirku, V.1    Kraxnerova, B.2    Krumphanzl, V.3
  • 17
    • 0036051173 scopus 로고    scopus 로고
    • Determination of xylanase, β-glucanase, and cellulase activity
    • Konig J, Grasser R, Pikor H, Vogel K (2002) Determination of xylanase, β-glucanase, and cellulase activity. Anal Bioanal Chem 374:80-87
    • (2002) Anal Bioanal Chem , vol.374 , pp. 80-87
    • Konig, J.1    Grasser, R.2    Pikor, H.3    Vogel, K.4
  • 18
    • 0032190308 scopus 로고    scopus 로고
    • The laminarinase from thermophilic eubacterium Rhodothermus marinus - Conformation, stability, and identification of active site carboxylic residues by site-directed mutagenesis
    • Krah M, Misselwitz R, Politz O, Thomsen KK, Welfle H, Borriss R (1998) The laminarinase from thermophilic eubacterium Rhodothermus marinus - conformation, stability, and identification of active site carboxylic residues by site-directed mutagenesis. Eur J Biochem 257:101-111
    • (1998) Eur J Biochem , vol.257 , pp. 101-111
    • Krah, M.1    Misselwitz, R.2    Politz, O.3    Thomsen, K.K.4    Welfle, H.5    Borriss, R.6
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0242541601 scopus 로고    scopus 로고
    • Purification and characterization of an endocellulase from the thermophilic fungus Chaetomium thermophilum CT2
    • Li DC, Lu M, Li YL, Lu J (2003) Purification and characterization of an endocellulase from the thermophilic fungus Chaetomium thermophilum CT2. Enzyme Microb Technol 33:932-938
    • (2003) Enzyme Microb Technol , vol.33 , pp. 932-938
    • Li, D.C.1    Lu, M.2    Li, Y.L.3    Lu, J.4
  • 23
    • 17844398284 scopus 로고    scopus 로고
    • Structure of β-glucan oligomer from laminarin and its effect on human monocytes to inhibit the proliferation of U937 cells
    • Pang Z, Otaka K, Maoka T, Hidaka K, Ishijima S, Oda M, Ohnishi M (2005) Structure of β-glucan oligomer from laminarin and its effect on human monocytes to inhibit the proliferation of U937 cells. Biosci Biotechnol Biochem 69:553-858
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 553-858
    • Pang, Z.1    Otaka, K.2    Maoka, T.3    Hidaka, K.4    Ishijima, S.5    Oda, M.6    Ohnishi, M.7
  • 24
    • 0027572064 scopus 로고
    • Noncellulytic fungal β-glucanase: Their physiology and regulation
    • Pitson SM, Seviour RJ, Mcdougall BM (1993) Noncellulytic fungal β-glucanase: their physiology and regulation. Enzyme Microb Technol 15:178-192
    • (1993) Enzyme Microb Technol , vol.15 , pp. 178-192
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3
  • 25
    • 0019811892 scopus 로고
    • Isolation, properties, function and regulation of endo-(1-3)-β- glucanases in Schizosaccharomyces pombe
    • Reichelt BY, Fleet GH (1981) Isolation, properties, function and regulation of endo-(1-3)-β-glucanases in Schizosaccharomyces pombe. J Bacteriol 147:1085-1094
    • (1981) J Bacteriol , vol.147 , pp. 1085-1094
    • Reichelt, B.Y.1    Fleet, G.H.2
  • 27
    • 0032801449 scopus 로고    scopus 로고
    • The mycoparasite Ampelomyces quisqualis expresses exgA encoding an exo-β-1,3-glucanase in culture and during mycoparasitism
    • Rotem Y, Yarden O, Sztejnberg A (1999) The mycoparasite Ampelomyces quisqualis expresses exgA encoding an exo-β-1,3-glucanase in culture and during mycoparasitism. Phytopathology 89:631-638
    • (1999) Phytopathology , vol.89 , pp. 631-638
    • Rotem, Y.1    Yarden, O.2    Sztejnberg, A.3
  • 28
    • 0021832197 scopus 로고
    • Study of the effect of β-1,3-glucanase from basidiomycete QM 806 on yeast extract production
    • Ryan EM, Ward OP (1985) Study of the effect of β-1,3-glucanase from basidiomycete QM 806 on yeast extract production. Biotechnol Lett 7:409-412
    • (1985) Biotechnol Lett , vol.7 , pp. 409-412
    • Ryan, E.M.1    Ward, O.P.2
  • 29
    • 0028069714 scopus 로고
    • Cloning and targeted gene disruption of EXG1, encoding exo-β-1,3-glucanase, in the phytopathogenic fungus Cochliobolus carbonum
    • Schaeffer HJ, Leykam J, Walton JD (1994) Cloning and targeted gene disruption of EXG1, encoding exo-β-1,3-glucanase, in the phytopathogenic fungus Cochliobolus carbonum. Appl Environ Microbiol 60:594-598
    • (1994) Appl Environ Microbiol , vol.60 , pp. 594-598
    • Schaeffer, H.J.1    Leykam, J.2    Walton, J.D.3
  • 31
    • 0034633831 scopus 로고    scopus 로고
    • Characterization of a β-1,3-glucanase encoded by chlorella virus PBCV-1
    • Sun L, Gurnon JR, Adams BJ, Graves MV, Van Etten JL (2000) Characterization of a β-1,3-glucanase encoded by chlorella virus PBCV-1. Virology 276:27-36
    • (2000) Virology , vol.276 , pp. 27-36
    • Sun, L.1    Gurnon, J.R.2    Adams, B.J.3    Graves, M.V.4    Van Etten, J.L.5
  • 32
    • 0000991087 scopus 로고
    • Purification and characterization of an endo-(1,3)-β-D-glucanase from Trichoderma longibrachiatum
    • Tangarone B, Royer JC, Nakas JP (1989) Purification and characterization of an endo-(1,3)-β-D-glucanase from Trichoderma longibrachiatum. Appl Environ Microbiol 55:177-184
    • (1989) Appl Environ Microbiol , vol.55 , pp. 177-184
    • Tangarone, B.1    Royer, J.C.2    Nakas, J.P.3
  • 33
    • 0000701844 scopus 로고
    • Purification and partial characterization of a (-1,3-glucanase secreted by the mycoparasite Stachybotrys elegans
    • Tweddell RJ, Jabaji-Hare SH, Goetghebeur M, Charest PM, Kermasha S (1995) Purification and partial characterization of a (-1,3-glucanase secreted by the mycoparasite Stachybotrys elegans. Biosci Biotechnol Biochem 59:2223-2227
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 2223-2227
    • Tweddell, R.J.1    Jabaji-Hare, S.H.2    Goetghebeur, M.3    Charest, P.M.4    Kermasha, S.5
  • 34
    • 0029785952 scopus 로고    scopus 로고
    • Highly efficient homologous integration via tandem exo-β-1,3- glucanase genes in the common mushroom, Agaricus bisporus
    • Van De Rhee MD, Mendes O, Werten MW, Huizing HJ, Mooibroek H (1996) Highly efficient homologous integration via tandem exo-β-1,3-glucanase genes in the common mushroom, Agaricus bisporus. Curr Genet 30:166-173
    • (1996) Curr Genet , vol.30 , pp. 166-173
    • Van De Rhee, M.D.1    Mendes, O.2    Werten, M.W.3    Huizing, H.J.4    Mooibroek, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.