메뉴 건너뛰기




Volumn 26, Issue 12, 2010, Pages 2171-2178

Molecular characterization of an endochitinase from Bacillus thuringiensis subsp. konkukian

Author keywords

Antifungal; B. thuringiensis; Characterization; Chitinase; Crystalline chitin degradation

Indexed keywords

ANTI-FUNGAL; ASPERGILLUS NIGER; BACILLUS THURINGIENSIS; BACILLUS THURINGIENSIS SEROVAR; BROAD SPECTRUM; CARBOHYDRATE BINDING MODULES; CHITINASE GENES; CHITINASES; CO-EXPRESSION; COLLOIDAL CHITIN; CROP PLANTS; CRYSTALLINE CHITIN DEGRADATION; ENDOCHITINASE; FUNGAL SPORES; FUSARIUM OXYSPORUMS; HYPHAL GROWTH; INCUBATION PERIODS; INSECTICIDAL PROTEIN; ISO-ELECTRIC POINTS; MODULAR STRUCTURES; MOLECULAR CHARACTERIZATION; N-TERMINALS; OPEN READING FRAME; PATHOGENIC FUNGI; PURIFIED ENZYME; RECOMBINANT ENZYMES; THURINGIENSIS;

EID: 79955524724     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-010-0401-z     Document Type: Article
Times cited : (9)

References (37)
  • 1
    • 0028820391 scopus 로고
    • How does Bacillus thuringiensis produce so much insecticidal crystal protein?
    • Agaisse H, Lereclus D (1995) How does Bacillus thuringiensis produce so much insecticidal crystal protein? J Bacteriol 177: 6027-6032.
    • (1995) J Bacteriol , vol.177 , pp. 6027-6032
    • Agaisse, H.1    Lereclus, D.2
  • 2
    • 46849118084 scopus 로고    scopus 로고
    • Wide-range antifungal antagonism of Paenibacillus ehimensis IB-X-b and its dependence on chitinase and beta-1, 3-glucanase production
    • Aktuganov G, Melentjev A, Galimzianova N, Khalikova E, Korpela T, Susi P (2008) Wide-range antifungal antagonism of Paenibacillus ehimensis IB-X-b and its dependence on chitinase and beta-1, 3-glucanase production. Can J Microbiol 54(7): 577-587.
    • (2008) Can J Microbiol , vol.54 , Issue.7 , pp. 577-587
    • Aktuganov, G.1    Melentjev, A.2    Galimzianova, N.3    Khalikova, E.4    Korpela, T.5    Susi, P.6
  • 4
    • 52049099457 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endochitinase (ChiA-HD73) from Bacillus thuringiensis subsp. kurstaki HD-73
    • Barboza-Corona JE, Reyes-Rios DM, Salcedo-Hernandez R, Bideshi DK (2008) Molecular and biochemical characterization of an endochitinase (ChiA-HD73) from Bacillus thuringiensis subsp. kurstaki HD-73. Mol Biotechnol 39(1): 29-37.
    • (2008) Mol Biotechnol , vol.39 , Issue.1 , pp. 29-37
    • Barboza-Corona, J.E.1    Reyes-Rios, D.M.2    Salcedo-Hernandez, R.3    Bideshi, D.K.4
  • 5
    • 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
  • 6
    • 0028989744 scopus 로고
    • Chitinolytic Enterobacter agglomerans antagonistic to fungal plant pathogens
    • Chernin L, Ismailov Z, Haran S, Chet I (1995) Chitinolytic Enterobacter agglomerans antagonistic to fungal plant pathogens. Appl Environ Microbiol 61(5): 1720-1726.
    • (1995) Appl Environ Microbiol , vol.61 , Issue.5 , pp. 1720-1726
    • Chernin, L.1    Ismailov, Z.2    Haran, S.3    Chet, I.4
  • 7
    • 0031038259 scopus 로고    scopus 로고
    • Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans
    • Chernin LS, De la Fuente L, Sobolev V, Haran S, Vorgias CE, Oppenheim AB, Chet I (1997) Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans. Appl Environ Microbiol 63(3): 834-839.
    • (1997) Appl Environ Microbiol , vol.63 , Issue.3 , pp. 834-839
    • Chernin, L.S.1    de la Fuente, L.2    Sobolev, V.3    Haran, S.4    Vorgias, C.E.5    Oppenheim, A.B.6    Chet, I.7
  • 8
    • 33749524596 scopus 로고    scopus 로고
    • Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi
    • de la Vega LM, Barboza-Corona JE, Aguilar-Uscanga MG, Ramirez-Lepe M (2006) Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi. Can J Microbiol 52(7): 651-657.
    • (2006) Can J Microbiol , vol.52 , Issue.7 , pp. 651-657
    • de la Vega, L.M.1    Barboza-Corona, J.E.2    Aguilar-Uscanga, M.G.3    Ramirez-Lepe, M.4
  • 9
    • 43349089434 scopus 로고    scopus 로고
    • Improving the insecticidal activity by expression of a recombinant cry1Ac gene with chitinase-encoding gene in acrystalliferous Bacillus thuringiensis
    • Ding X, Luo Z, Xia L, Gao B, Sun Y, Zhang Y (2008) Improving the insecticidal activity by expression of a recombinant cry1Ac gene with chitinase-encoding gene in acrystalliferous Bacillus thuringiensis. Curr Microbiol 56(5): 442-446.
    • (2008) Curr Microbiol , vol.56 , Issue.5 , pp. 442-446
    • Ding, X.1    Luo, Z.2    Xia, L.3    Gao, B.4    Sun, Y.5    Zhang, Y.6
  • 10
    • 36248937188 scopus 로고    scopus 로고
    • Effect of the chitin binding domain deletion from Bacillus thuringiensis subsp. kurstaki chitinase Chi255 on its stability in Escherichia coli
    • Driss F, Baanannou A, Rouis S, Masmoudi I, Zouari N, Jaoua S (2007) Effect of the chitin binding domain deletion from Bacillus thuringiensis subsp. kurstaki chitinase Chi255 on its stability in Escherichia coli. Mol Biotechnol 36(3): 232-237.
    • (2007) Mol Biotechnol , vol.36 , Issue.3 , pp. 232-237
    • Driss, F.1    Baanannou, A.2    Rouis, S.3    Masmoudi, I.4    Zouari, N.5    Jaoua, S.6
  • 11
    • 68549085320 scopus 로고    scopus 로고
    • Bacillus thuringiensis Bel protein enhances the toxicity of Cry1Ac protein to Helicoverpa armigera larvae by degrading insect intestinal mucin
    • Fang S, Wang L, Guo W, Zhang X, Peng D, Luo C, Yu Z, Sun M (2009) Bacillus thuringiensis Bel protein enhances the toxicity of Cry1Ac protein to Helicoverpa armigera larvae by degrading insect intestinal mucin. Appl Environ Microbiol 75(16): 5237-5243.
    • (2009) Appl Environ Microbiol , vol.75 , Issue.16 , pp. 5237-5243
    • Fang, S.1    Wang, L.2    Guo, W.3    Zhang, X.4    Peng, D.5    Luo, C.6    Yu, Z.7    Sun, M.8
  • 12
    • 0035206324 scopus 로고    scopus 로고
    • Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48
    • Frankowski J, Lorito M, Scala F, Schmid R, Berg G, Bahl H (2001) Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48. Arch Microbiol 176(6): 421-426.
    • (2001) Arch Microbiol , vol.176 , Issue.6 , pp. 421-426
    • Frankowski, J.1    Lorito, M.2    Scala, F.3    Schmid, R.4    Berg, G.5    Bahl, H.6
  • 13
    • 0022638244 scopus 로고
    • Cloning of a Serratia marcescens gene encoding chitinase
    • Fuchs RL, McPherson SA, Drahos DJ (1986) Cloning of a Serratia marcescens gene encoding chitinase. Appl Environ Microbiol 51(3): 504-509.
    • (1986) Appl Environ Microbiol , vol.51 , Issue.3 , pp. 504-509
    • Fuchs, R.L.1    McPherson, S.A.2    Drahos, D.J.3
  • 14
    • 33845265284 scopus 로고    scopus 로고
    • Antifungal properties of Haem Peroxidase from Acorus calamus
    • Ghosh M (2006) Antifungal properties of Haem Peroxidase from Acorus calamus. Annals Bot 98(6): 1145-1153.
    • (2006) Annals Bot , vol.98 , Issue.6 , pp. 1145-1153
    • Ghosh, M.1
  • 15
    • 2542475295 scopus 로고    scopus 로고
    • Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay
    • Hardt M, Laine RA (2004) Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay. Arch Biochem Biophys 426(2): 286-297.
    • (2004) Arch Biochem Biophys , vol.426 , Issue.2 , pp. 286-297
    • Hardt, M.1    Laine, R.A.2
  • 16
    • 0033974048 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Asp280 suggests substrate-assisted catalysis of chitinase A1 from Bacillus circulans WL-12
    • Hashimoto M, Honda Y, Nikaidou N, Fukamizo T, Watanabe T (2000) Site-directed mutagenesis of Asp280 suggests substrate-assisted catalysis of chitinase A1 from Bacillus circulans WL-12. J Biosci Bioeng 89(1): 100-102.
    • (2000) J Biosci Bioeng , vol.89 , Issue.1 , pp. 100-102
    • Hashimoto, M.1    Honda, Y.2    Nikaidou, N.3    Fukamizo, T.4    Watanabe, T.5
  • 17
    • 63949088397 scopus 로고    scopus 로고
    • Efficient constitutive expression of chitinase in the mother cell of Bacillus thuringiensis and its potential to enhance the toxicity of Cry1Ac protoxin
    • Hu SB, Liu P, Ding XZ, Yan L, Sun YJ, Zhang YM, Li WP, Xia LQ (2009) Efficient constitutive expression of chitinase in the mother cell of Bacillus thuringiensis and its potential to enhance the toxicity of Cry1Ac protoxin. Appl Microbiol Biotechnol 82: 1157-1167.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 1157-1167
    • Hu, S.B.1    Liu, P.2    Ding, X.Z.3    Yan, L.4    Sun, Y.J.5    Zhang, Y.M.6    Li, W.P.7    Xia, L.Q.8
  • 18
    • 0036195363 scopus 로고    scopus 로고
    • Characterization of a chitinase gene from Stenotrophomonas maltophilia strain 34S1 and its involvement in biological control
    • Kobayashi DY, Reedy RM, Bick J, Oudemans PV (2002) Characterization of a chitinase gene from Stenotrophomonas maltophilia strain 34S1 and its involvement in biological control. Appl Environ Microbiol 68(3): 1047-1054.
    • (2002) Appl Environ Microbiol , vol.68 , Issue.3 , pp. 1047-1054
    • Kobayashi, D.Y.1    Reedy, R.M.2    Bick, J.3    Oudemans, P.V.4
  • 19
    • 33847051259 scopus 로고    scopus 로고
    • Screening of genes involved in chitinase production in Aeromonas caviae CB101 via transposon mutagenesis
    • Li Q, Xiao X, Wang F (2007) Screening of genes involved in chitinase production in Aeromonas caviae CB101 via transposon mutagenesis. J Appl Microbiol 102(3): 640-649.
    • (2007) J Appl Microbiol , vol.102 , Issue.3 , pp. 640-649
    • Li, Q.1    Xiao, X.2    Wang, F.3
  • 20
    • 3342961755 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of the chitinase gene from Bacillus thuringiensis serovar alesti
    • Lin Y, Xiong G (2004) Molecular cloning and sequence analysis of the chitinase gene from Bacillus thuringiensis serovar alesti. Biotechnol Lett 26(8): 635-639.
    • (2004) Biotechnol Lett , vol.26 , Issue.8 , pp. 635-639
    • Lin, Y.1    Xiong, G.2
  • 21
    • 48349113600 scopus 로고    scopus 로고
    • Cloning and characterization of a novel chitinase gene (chi46) from Chaetomium globosum and identification of its biological activity
    • Liu ZH, Yang Q, Hu S, Zhang JD, Ma J (2008) Cloning and characterization of a novel chitinase gene (chi46) from Chaetomium globosum and identification of its biological activity. Appl Microbiol Biotechnol 80(2): 241-252.
    • (2008) Appl Microbiol Biotechnol , vol.80 , Issue.2 , pp. 241-252
    • Liu, Z.H.1    Yang, Q.2    Hu, S.3    Zhang, J.D.4    Ma, J.5
  • 22
  • 23
    • 77649237271 scopus 로고    scopus 로고
    • Aeromonas caviae CB101 contains four chitinases encoded by a single gene chi1
    • Mehmood MA, Yingbao G, Zhuang Q, Wang F, Xiao X, Wang F (2010) Aeromonas caviae CB101 contains four chitinases encoded by a single gene chi1. Mol Biotechnol 44: 213-220.
    • (2010) Mol Biotechnol , vol.44 , pp. 213-220
    • Mehmood, M.A.1    Yingbao, G.2    Zhuang, Q.3    Wang, F.4    Xiao, X.5    Wang, F.6
  • 24
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for detection of reducing sugar
    • Miller G (1959) Use of dinitrosalicylic acid reagent for detection of reducing sugar. Anal Chem 31: 426-428.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.1
  • 25
    • 33746063201 scopus 로고    scopus 로고
    • Characterization and biocontrol ability of fusion chitinase in Escherichia coli carrying chitinase cDNA from Trichothecium roseum
    • Pan H, Wei Y, Xin F, Zhou M, Zhang S (2006) Characterization and biocontrol ability of fusion chitinase in Escherichia coli carrying chitinase cDNA from Trichothecium roseum. Z Naturforsch [C] 61(5-6): 397-404.
    • (2006) Z Naturforsch [C] , vol.61 , Issue.5-6 , pp. 397-404
    • Pan, H.1    Wei, Y.2    Xin, F.3    Zhou, M.4    Zhang, S.5
  • 27
    • 17144436519 scopus 로고    scopus 로고
    • Antifungal activity of Bacillus thuringiensis chitinase and its potential for the biocontrol of phytopathogenic fungi in soybean seeds
    • Reyes-Ramírez A, Escudero-Abarca BI, Aguilar-Uscanga G, Hayward-Jones PM, Barboza-Corona JE (2004) Antifungal activity of Bacillus thuringiensis chitinase and its potential for the biocontrol of phytopathogenic fungi in soybean seeds. J Food Sci 69: 131-134.
    • (2004) J Food Sci , vol.69 , pp. 131-134
    • Reyes-Ramírez, A.1    Escudero-Abarca, B.I.2    Aguilar-Uscanga, G.3    Hayward-Jones, P.M.4    Barboza-Corona, J.E.5
  • 28
    • 0031666818 scopus 로고    scopus 로고
    • Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects
    • Sampson MN, Gooday GW (1998) Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects. Microbiology 144(8): 2189-2194.
    • (1998) Microbiology , vol.144 , Issue.8 , pp. 2189-2194
    • Sampson, M.N.1    Gooday, G.W.2
  • 29
    • 77957071226 scopus 로고
    • Preparation of crustacean chitin
    • Shimahara K, Takiguchi Y (1988) Preparation of crustacean chitin. Methods Enzymol 161: 417-423.
    • (1988) Methods Enzymol , vol.161 , pp. 417-423
    • Shimahara, K.1    Takiguchi, Y.2
  • 30
    • 0036562588 scopus 로고    scopus 로고
    • Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation
    • Suzuki K, Sugawara N, Suzuki M, Uchiyama T, Katouno F, Nikaidou N, Watanabe T (2002) Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation. Biosci Biotechnol Biochem 66(5): 1075-1083.
    • (2002) Biosci Biotechnol Biochem , vol.66 , Issue.5 , pp. 1075-1083
    • Suzuki, K.1    Sugawara, N.2    Suzuki, M.3    Uchiyama, T.4    Katouno, F.5    Nikaidou, N.6    Watanabe, T.7
  • 32
    • 0345411954 scopus 로고    scopus 로고
    • The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis
    • Wang F, Li Q, Zhou Y, Li MG, Xiao X (2003) The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis. Proteins 53(4): 908-916.
    • (2003) Proteins , vol.53 , Issue.4 , pp. 908-916
    • Wang, F.1    Li, Q.2    Zhou, Y.3    Li, M.G.4    Xiao, X.5
  • 33
    • 0025171327 scopus 로고
    • Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin
    • Watanabe T, Suzuki K, Oyanagi W, Ohnishi K, Tanaka H (1990) Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J Biol Chem 265(26): 15659-15665.
    • (1990) J Biol Chem , vol.265 , Issue.26 , pp. 15659-15665
    • Watanabe, T.1    Suzuki, K.2    Oyanagi, W.3    Ohnishi, K.4    Tanaka, H.5
  • 35
    • 0034521608 scopus 로고    scopus 로고
    • Toxicity of chitinase-producing Bacillus thuringiensis ssp. kurstaki HD-1 (G) toward Plutella xylostella
    • Wiwat C, Thaithanun S, Pantuwatana S, Bhumiratana A (2000) Toxicity of chitinase-producing Bacillus thuringiensis ssp. kurstaki HD-1 (G) toward Plutella xylostella. J Invertebr Pathol 76(4): 270-277.
    • (2000) J Invertebr Pathol , vol.76 , Issue.4 , pp. 270-277
    • Wiwat, C.1    Thaithanun, S.2    Pantuwatana, S.3    Bhumiratana, A.4
  • 36
    • 70350421963 scopus 로고    scopus 로고
    • Chitinases from the plant disease biocontrol agent, Stenotrophomonas maltophilia C3
    • Zhang Z, Yuen GY, Sarath G, Penheiter AR (2000) Chitinases from the plant disease biocontrol agent, Stenotrophomonas maltophilia C3. Biol Control 91(2): 205-211.
    • (2000) Biol Control , vol.91 , Issue.2 , pp. 205-211
    • Zhang, Z.1    Yuen, G.Y.2    Sarath, G.3    Penheiter, A.R.4
  • 37
    • 31444442114 scopus 로고    scopus 로고
    • Cloning of the Bacillus thuringiensis serovar sotto chitinase (Schi) gene and characterization of its protein
    • Zhong WF, Fang JC, Cai PZ, Yan WZ, Wu J, Guo HF (2005) Cloning of the Bacillus thuringiensis serovar sotto chitinase (Schi) gene and characterization of its protein. Genet Mol Biol 28(4): 821-826.
    • (2005) Genet Mol Biol , vol.28 , Issue.4 , pp. 821-826
    • Zhong, W.F.1    Fang, J.C.2    Cai, P.Z.3    Yan, W.Z.4    Wu, J.5    Guo, H.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.