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Volumn 61, Issue 5-6, 2003, Pages 472-478

Biochemical characterization and antifungal activity of an endo-1,3-β-glucanase of Paenibacillus sp. isolated from garden soil

Author keywords

[No Author keywords available]

Indexed keywords

1,3 BETA GLUCANASE; BACTERIAL ENZYME; CELLULOSE; GLUCAN; XYLAN;

EID: 0038575670     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-003-1249-z     Document Type: Article
Times cited : (87)

References (40)
  • 2
    • 0028970757 scopus 로고
    • Comparative studies of β-1,3-glucanase A1 and B of Bacillus circulans WL-12: Purifications and enzymatic properties
    • Aida K, Okada T, Kasahara N, Nikaidou N, Tanaka H, Watanabe T (1995) Comparative studies of β-1,3-glucanase A1 and B of Bacillus circulans WL-12: purifications and enzymatic properties. J Ferment Bioeng 80:283-286
    • (1995) J Ferment Bioeng , vol.80 , pp. 283-286
    • Aida, K.1    Okada, T.2    Kasahara, N.3    Nikaidou, N.4    Tanaka, H.5    Watanabe, T.6
  • 3
    • 0026557458 scopus 로고
    • Isolation and partial characterization of an 87-kilodalton β-1,3-glucanase from Bacillus circulans IAM1165
    • Aono R, Sato M, Yamamoto M, Horikoshi K (1992) Isolation and partial characterization of an 87-kilodalton β-1,3-glucanase from Bacillus circulans IAM1165. Appl Environ Microbiol 58:520-524
    • (1992) Appl Environ Microbiol , vol.58 , pp. 520-524
    • Aono, R.1    Sato, M.2    Yamamoto, M.3    Horikoshi, K.4
  • 4
    • 0028895388 scopus 로고
    • Isolation of extracellular 28- and 42-kilodalton β-1,3-glucanase and comparison of three β-1,3-glucanase produced by Bacillus circulans IAM1165
    • Aono R, Hammura M, Yamamoto M, Asano T (1995) Isolation of extracellular 28- and 42-kilodalton β-1,3-glucanase and comparison of three β-1,3-glucanase produced by Bacillus circulans IAM1165. Appl Environ Microbiol 61:122-129
    • (1995) Appl Environ Microbiol , vol.61 , pp. 122-129
    • Aono, R.1    Hammura, M.2    Yamamoto, M.3    Asano, T.4
  • 5
    • 0036617995 scopus 로고    scopus 로고
    • Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic β-1,3-glucan-hydrolase BglM of Bacillus circulans IAM1165
    • Asano T, Taki J, Yamamoto M, Aono R (2002) Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic β-1,3-glucan-hydrolase BglM of Bacillus circulans IAM1165. Biosci Biotechnol Biochem 66:1246-1255
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1246-1255
    • Asano, T.1    Taki, J.2    Yamamoto, M.3    Aono, R.4
  • 6
    • 0027860384 scopus 로고
    • Molecular identification of rRNA group 3 bacilli (Ash, Farrow, Wallbanks and Collins) using a PCR probe test. Proposal for the creation of a new genus Paenibacillus
    • Ash C, Priest FG, Collins MD (1993) Molecular identification of rRNA group 3 bacilli (Ash, Farrow, Wallbanks and Collins) using a PCR probe test. Proposal for the creation of a new genus Paenibacillus. Antonie Leeuwenhoek 64:253-260
    • (1993) Antonie Leeuwenhoek , vol.64 , pp. 253-260
    • Ash, C.1    Priest, F.G.2    Collins, M.D.3
  • 7
    • 0020771857 scopus 로고
    • Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas
    • Beguin P (1983) Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas. Anal Biochem 131:333-336
    • (1983) Anal Biochem , vol.131 , pp. 333-336
    • Beguin, P.1
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM (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
  • 9
    • 0025574845 scopus 로고
    • Tissue-specific and pathogen-induced regulation of a Nicotiana plumbaginifolia β-1,3-glucanase gene
    • Castresana C, De Carvalho F, Gheysen G, Habets M, Inze D, Van Montagu M (1990) Tissue-specific and pathogen-induced regulation of a Nicotiana plumbaginifolia β-1,3-glucanase gene. Plant Cell 2:1131-1143
    • (1990) Plant Cell , vol.2 , pp. 1131-1143
    • Castresana, C.1    De Carvalho, F.2    Gheysen, G.3    Habets, M.4    Inze, D.5    Van Montagu, M.6
  • 10
    • 0000738385 scopus 로고
    • Genus Bacillus Cohn 1872
    • Sneath PHA, Mair NS, Sharpe ME, Holt JG (eds). Williams and Wilkins, Baltimore
    • Clans D, Berkeley RCW (1986) Genus Bacillus Cohn 1872. In: Sneath PHA, Mair NS, Sharpe ME, Holt JG (eds) Bergey's manual of systematic bacteriology, vol 2. Williams and Wilkins, Baltimore, pp 1105-1140
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1105-1140
    • Clans, D.1    Berkeley, R.C.W.2
  • 11
    • 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, Benitez 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    Benitez, T.3    Llobell, A.4    Romero, L.C.5
  • 15
    • 0027728296 scopus 로고
    • Barley pathogenesis-related proteins with fungal cell wall lyric activity inhibit the growth of yeasts
    • Grenier J, Potvin C, Asselin A (1993) Barley pathogenesis-related proteins with fungal cell wall lyric activity inhibit the growth of yeasts. Plant Physiol 103:1277-1283
    • (1993) Plant Physiol , vol.103 , pp. 1277-1283
    • Grenier, J.1    Potvin, C.2    Asselin, A.3
  • 16
    • 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 WG, 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.2    Van Der Oost, J.3    De Vos, W.M.4
  • 17
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280:309-316
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 18
    • 0036010816 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of an endo-1,3-β-glucanase from Streptomyces sioyaensis containing a C-terminal family 6 carbohydrate-binding module that binds to 1,3-β-glucan
    • Hong TY, Cheng CW, Huang JW, Meng M (2002) Isolation and biochemical characterization of an endo-1,3-β-glucanase from Streptomyces sioyaensis containing a C-terminal family 6 carbohydrate-binding module that binds to 1,3-β-glucan. Microbiology 148:1151-1159
    • (2002) Microbiology , vol.148 , pp. 1151-1159
    • Hong, T.Y.1    Cheng, C.W.2    Huang, J.W.3    Meng, M.4
  • 19
    • 0029328434 scopus 로고
    • Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco
    • Jach G, Gornhardt B, Mundy J, Logemann J, Pinsdorf E, Leah R, Schell J, Maas C (1995) Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J 8:97-109
    • (1995) Plant J , vol.8 , pp. 97-109
    • Jach, G.1    Gornhardt, B.2    Mundy, J.3    Logemann, J.4    Pinsdorf, E.5    Leah, R.6    Schell, J.7    Maas, C.8
  • 20
    • 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
  • 21
    • 0035128855 scopus 로고    scopus 로고
    • β-1, 3-Glucanase and chitinase transgenes in hybrids show distinctive and independent patterns of posttranscriptional gene silencing
    • 2001
    • Kunz C, Schob H, Leubner-Metzger G, Glazov E, Meins F Jr (2001) β-1, 3-Glucanase and chitinase transgenes in hybrids show distinctive and independent patterns of posttranscriptional gene silencing. Planta 2001 212:243-249
    • (2001) Planta , vol.212 , pp. 243-249
    • Kunz, C.1    Schob, H.2    Leubner-Metzger, G.3    Glazov, E.4    Meins F., Jr.5
  • 22
    • 0001857117 scopus 로고
    • 16S/23S rRNA sequencing
    • Stackebrandt E, Goodfellow M (eds). Wiley, New York
    • Lane DL (1991) 16S/23S rRNA sequencing. In: Stackebrandt E, Goodfellow M (eds) Nucleic acid techniques in bacterial systematics. Wiley, New York, pp 115-175
    • (1991) Nucleic Acid Techniques in Bacterial Systematics , pp. 115-175
    • Lane, D.L.1
  • 23
    • 0018939094 scopus 로고
    • A medium for detecting β-(1,3)-glucanase activity in bacteria
    • Mahasneh AM, Stewart DJ (1980) A medium for detecting β-(1,3)-glucanase activity in bacteria. J Appl Bacteriol 48:457-458
    • (1980) J Appl Bacteriol , vol.48 , pp. 457-458
    • Mahasneh, A.M.1    Stewart, D.J.2
  • 25
    • 0035957330 scopus 로고    scopus 로고
    • Complete genome sequence of Caulobacter crescentus
    • Nierman WC et al (2001) Complete genome sequence of Caulobacter crescentus. Proc Natl Acad Sci USA 98:4136-4141
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4136-4141
    • Nierman, W.C.1
  • 27
    • 0003007762 scopus 로고
    • Fungal cell walls - A review
    • Kuhn OJ, Trinci APJ, Jung MJ, Goosey MW, Copping LG (eds). Springer, Berlin Heidelberg New York
    • Peberdy JF (1990) Fungal cell walls - a review. In: Kuhn OJ, Trinci APJ, Jung MJ, Goosey MW, Copping LG (eds) Biochemistry of cell walls and membranes in fungi. Springer, Berlin Heidelberg New York, pp 5-30
    • (1990) Biochemistry of Cell Walls and Membranes in Fungi , pp. 5-30
    • Peberdy, J.F.1
  • 29
    • 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
  • 32
    • 0001550147 scopus 로고
    • Isolation of a Clostridium thermocellum gene encoding a thermostable β-1,3-glucanase (laminarinase)
    • Schwarz WH, Schimming S, Staudenbauer WL (1988) Isolation of a Clostridium thermocellum gene encoding a thermostable β-1,3-glucanase (laminarinase). Biotechnol Lett 10:225-230
    • (1988) Biotechnol Lett , vol.10 , pp. 225-230
    • Schwarz, W.H.1    Schimming, S.2    Staudenbauer, W.L.3
  • 34
    • 0027547194 scopus 로고
    • Analysis of regulatory, elements involved in stress-induced and organ-specific expression of tobacco acidic and basic β-1,3-glucanase genes
    • Van de Rhee MD, Lemmers R, Bol JF (1993) Analysis of regulatory, elements involved in stress-induced and organ-specific expression of tobacco acidic and basic β-1,3-glucanase genes. Plant Mol Biol 21:451-461
    • (1993) Plant Mol Biol , vol.21 , pp. 451-461
    • Van De Rhee, M.D.1    Lemmers, R.2    Bol, J.F.3
  • 35
    • 0032534001 scopus 로고    scopus 로고
    • Silencing of β-1,3-glucanase genes in tobacco correlates with an increased abundance of RNA degradation intermediates
    • Van Eldik GJ, Litiere K, Jacobs JJ, van Montagu M, Cornelissen M (1998) Silencing of β-1,3-glucanase genes in tobacco correlates with an increased abundance of RNA degradation intermediates. Nucleic Acids Res 26:5176-5181
    • (1998) Nucleic Acids Res , vol.26 , pp. 5176-5181
    • Van Eldik, G.J.1    Litiere, K.2    Jacobs, J.J.3    Van Montagu, M.4    Cornelissen, M.5
  • 36
    • 0026578808 scopus 로고
    • Three N-terminal domains of β-1,3-glucanase A1 are involved in binding to insoluble β-1,3-glucan
    • Watanabe T, Kasahara N, Aida K, Tanaka H (1992) Three N-terminal domains of β-1,3-glucanase A1 are involved in binding to insoluble β-1,3-glucan. J Bacteriol 174:186-190
    • (1992) J Bacteriol , vol.174 , pp. 186-190
    • Watanabe, T.1    Kasahara, N.2    Aida, K.3    Tanaka, H.4
  • 37
    • 77957034698 scopus 로고
    • Methods for measuring cellulase activities
    • Wood TM, Bhat KM (1988) Methods for measuring cellulase activities. Methods Enzymol 160:87-112
    • (1988) Methods Enzymol , vol.160 , pp. 87-112
    • Wood, T.M.1    Bhat, K.M.2
  • 38
    • 0025012650 scopus 로고
    • Structure of the gene encoding β-1,3-glucanase A1 of Bacillus circulans WL-12
    • Yahata N, Watanabe T, Nakamura Y, Yamamoto Y, Kamimiya S, Tanaka H (1990) Structure of the gene encoding β-1,3-glucanase A1 of Bacillus circulans WL-12. Gene 86:113-117
    • (1990) Gene , vol.86 , pp. 113-117
    • Yahata, N.1    Watanabe, T.2    Nakamura, Y.3    Yamamoto, Y.4    Kamimiya, S.5    Tanaka, H.6
  • 39
    • 0031840745 scopus 로고    scopus 로고
    • C-terminal domain of β-1,3-glucanase H in Bacillus circulans IAM1165 has a role in binding to insoluble β-1,3-glucan
    • Yamamoto M, Ezure T, Watanabe T, Tanaka H, Aono R (1998) C-terminal domain of β-1,3-glucanase H in Bacillus circulans IAM1165 has a role in binding to insoluble β-1,3-glucan. FEBS Lett 433:41-43
    • (1998) FEBS Lett , vol.433 , pp. 41-43
    • Yamamoto, M.1    Ezure, T.2    Watanabe, T.3    Tanaka, H.4    Aono, R.5
  • 40
    • 0030943791 scopus 로고    scopus 로고
    • Highly thermostable endo-1,3-β-glucanase (laminarinase) Lama from Thermotoga neapolitana: Nucleotide sequence of the gene and characterization of the recombinant gene product
    • Zverlov VV, Volkov IY, Velikodvorskaya TV, Schwarz WH (1997) Highly thermostable endo-1,3-β-glucanase (laminarinase) Lama from Thermotoga neapolitana: nucleotide sequence of the gene and characterization of the recombinant gene product. Microbiology 143:1701-1708
    • (1997) Microbiology , vol.143 , pp. 1701-1708
    • Zverlov, V.V.1    Volkov, I.Y.2    Velikodvorskaya, T.V.3    Schwarz, W.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.