메뉴 건너뛰기




Volumn 46, Issue 3-4, 2010, Pages 252-256

Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential

Author keywords

Antagonism; Bacillus thuringiensis; Characterization; ChiA; Dimmer; Synergism

Indexed keywords

ANTAGONISM; BACILLUS THURINGIENSIS; CHITINASES; CRYSTAL PROTEINS; GLYCOL CHITIN; HELICOVERPA ARMIGERA; INHIBITORY CONCENTRATION; LETHAL CONCENTRATION; OPTIMAL ACTIVITY; OPTIMUM PH; PARTIAL CHARACTERIZATION; PROTEIN BANDS; RENATURATION; SDS-PAGE; SEPHADEX; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; SPODOPTERA EXIGUA; SPORE GERMINATION; SURFACE CONTAMINATIONS;

EID: 74049139078     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.10.007     Document Type: Article
Times cited : (82)

References (33)
  • 1
    • 0346399742 scopus 로고    scopus 로고
    • Chitin metabolism in insects: structure, function and regulation of chitin syntheses and chitinases
    • Merzendorfer H., and Zimoch L. Chitin metabolism in insects: structure, function and regulation of chitin syntheses and chitinases. J Exp Biol 206 24 (2003) 4393-4412
    • (2003) J Exp Biol , vol.206 , Issue.24 , pp. 4393-4412
    • Merzendorfer, H.1    Zimoch, L.2
  • 2
    • 34848826214 scopus 로고    scopus 로고
    • Bacillus pumilus SG2 isolated from saline conditions produces and secretes two chitinases
    • Ahmadian G., Degrassi G., Venturi V., Zeigler D.R., Soudi M., and Zanguinejad P. Bacillus pumilus SG2 isolated from saline conditions produces and secretes two chitinases. J Appl Microbiol 103 4 (2007) 1081-1089
    • (2007) J Appl Microbiol , vol.103 , Issue.4 , pp. 1081-1089
    • Ahmadian, G.1    Degrassi, G.2    Venturi, V.3    Zeigler, D.R.4    Soudi, M.5    Zanguinejad, P.6
  • 3
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda M.J., and Robbins P.W. Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol Chem 266 29 (1991) 19758-19767
    • (1991) J Biol Chem , vol.266 , Issue.29 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 5
    • 25844465801 scopus 로고    scopus 로고
    • Molecular characterization of a novel chitinase from Bacillus thuringiensis subsp. Kurstaki
    • Driss F., Kallassy-Awad M., Zouari N., and Jaoua S. Molecular characterization of a novel chitinase from Bacillus thuringiensis subsp. Kurstaki. J Appl Microbiol 99 4 (2005) 945-953
    • (2005) J Appl Microbiol , vol.99 , Issue.4 , pp. 945-953
    • Driss, F.1    Kallassy-Awad, M.2    Zouari, N.3    Jaoua, S.4
  • 6
    • 21244486744 scopus 로고    scopus 로고
    • Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9
    • Huang C.J., Wang T.K., Chung S.C., and Chen C.Y. Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9. J Biochem Mol Biol 38 1 (2005) 82-88
    • (2005) J Biochem Mol Biol , vol.38 , Issue.1 , pp. 82-88
    • Huang, C.J.1    Wang, T.K.2    Chung, S.C.3    Chen, C.Y.4
  • 7
    • 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 L.M., Barboza-Corona J.E., Aguilar-Uscanga M.G., and Ramírez-Lepe M. Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi. Can J Microbiol 52 7 (2006) 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    Ramírez-Lepe, M.4
  • 8
    • 37549061086 scopus 로고    scopus 로고
    • Antifungal activity of chitinases from Trichoderma aureoviride DY-59 and Rhizopus microsporus VS-9
    • Nguyen N.V., Kim Y.J., Oh K.T., Jung W.J., and Park R.D. Antifungal activity of chitinases from Trichoderma aureoviride DY-59 and Rhizopus microsporus VS-9. Curr Microbiol 56 1 (2008) 28-32
    • (2008) Curr Microbiol , vol.56 , Issue.1 , pp. 28-32
    • Nguyen, N.V.1    Kim, Y.J.2    Oh, K.T.3    Jung, W.J.4    Park, R.D.5
  • 9
    • 4043092288 scopus 로고    scopus 로고
    • Improving the insecticidal activity of Bacillus thuringiensis subsp. aizawai against Spodoptera exigua by chromosomal expression of a chitinase gene
    • Thamthiankul S., Moar W.J., Miller M.E., and Panbangred W. Improving the insecticidal activity of Bacillus thuringiensis subsp. aizawai against Spodoptera exigua by chromosomal expression of a chitinase gene. Appl Microbiol Biotechnol 65 2 (2004) 183-192
    • (2004) Appl Microbiol Biotechnol , vol.65 , Issue.2 , pp. 183-192
    • Thamthiankul, S.1    Moar, W.J.2    Miller, M.E.3    Panbangred, W.4
  • 10
    • 0036902507 scopus 로고    scopus 로고
    • Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity
    • Liu M., Cai Q.X., Liu H.Z., Zhang B.H., Yan J.P., and Yuan Z.M. Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity. J Appl Microbiol 93 3 (2002) 374-379
    • (2002) J Appl Microbiol , vol.93 , Issue.3 , pp. 374-379
    • Liu, M.1    Cai, Q.X.2    Liu, H.Z.3    Zhang, B.H.4    Yan, J.P.5    Yuan, Z.M.6
  • 11
    • 38449111889 scopus 로고    scopus 로고
    • Improving the insecticidal activity against resistant Culex quinquefasciatus by expression of chitinase gene chiAC in Bacillus sphaericus
    • Cai Y.J., Yan J.P., Hu X.M., Han B., and Yuan Z.M. Improving the insecticidal activity against resistant Culex quinquefasciatus by expression of chitinase gene chiAC in Bacillus sphaericus. Appl Environ Microbiol 73 23 (2007) 7744-7746
    • (2007) Appl Environ Microbiol , vol.73 , Issue.23 , pp. 7744-7746
    • Cai, Y.J.1    Yan, J.P.2    Hu, X.M.3    Han, B.4    Yuan, Z.M.5
  • 12
    • 2942570088 scopus 로고    scopus 로고
    • Expression of chitinase-encoding genes in Bacillus thuringiensis and toxicity of engineered B. thuringiensis subsp aizawai toward Lymantria dispar larvae
    • Lertcanawanichakul M., Wiwat C., Bhumiratana A., and Dean D.H. Expression of chitinase-encoding genes in Bacillus thuringiensis and toxicity of engineered B. thuringiensis subsp aizawai toward Lymantria dispar larvae. Curr Microbiol 48 3 (2004) 175-181
    • (2004) Curr Microbiol , vol.48 , Issue.3 , pp. 175-181
    • Lertcanawanichakul, M.1    Wiwat, C.2    Bhumiratana, A.3    Dean, D.H.4
  • 13
    • 0035544534 scopus 로고    scopus 로고
    • Coexpression of chitinase and the cry11Aa1 toxin genes in Bacillus thuringiensis serovar israelensis
    • Sirichotpakorn N., Rongnoparut P., Choosang K., and Panbangred W. Coexpression of chitinase and the cry11Aa1 toxin genes in Bacillus thuringiensis serovar israelensis. J Invertebr Pathol 78 3 (2001) 160-169
    • (2001) J Invertebr Pathol , vol.78 , Issue.3 , pp. 160-169
    • Sirichotpakorn, N.1    Rongnoparut, P.2    Choosang, K.3    Panbangred, W.4
  • 14
    • 0031666818 scopus 로고    scopus 로고
    • Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects
    • Sampson M.N., and Gooday G.W. Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects. Microbiology 144 8 (1998) 2189-2194
    • (1998) Microbiology , vol.144 , Issue.8 , pp. 2189-2194
    • Sampson, M.N.1    Gooday, G.W.2
  • 15
    • 65849455047 scopus 로고    scopus 로고
    • Cloning, expression and sequence analysis of chiA, chiB in Bacillus thuringiensis subsp colmeri 15A3
    • Chen Y.L., Lu W., Chen Y.H., Xiao L., and Cai J. Cloning, expression and sequence analysis of chiA, chiB in Bacillus thuringiensis subsp colmeri 15A3. Acta Microbiol Sin 47 5 (2007) 843-848
    • (2007) Acta Microbiol Sin , vol.47 , Issue.5 , pp. 843-848
    • Chen, Y.L.1    Lu, W.2    Chen, Y.H.3    Xiao, L.4    Cai, J.5
  • 16
    • 66549107215 scopus 로고    scopus 로고
    • Chitinase B from Bacillus thuringiensis and its antagonism and insecticidal enhancing potential
    • Liu D., Chen Y.H., Cai J., Xiao L., and Liu C. Chitinase B from Bacillus thuringiensis and its antagonism and insecticidal enhancing potential. Acta Microbiol Sin 49 2 (2009) 180-185
    • (2009) Acta Microbiol Sin , vol.49 , Issue.2 , pp. 180-185
    • Liu, D.1    Chen, Y.H.2    Cai, J.3    Xiao, L.4    Liu, C.5
  • 17
    • 0042171469 scopus 로고    scopus 로고
    • A constitutively expressed 36 kDa exochitinase from Bacillus thuringiensis HD-1
    • Arora N., Ahmad T., Rajagopal R., and Bhatnagar R.K. A constitutively expressed 36 kDa exochitinase from Bacillus thuringiensis HD-1. Biochem Biophys Res Commun 307 3 (2003) 620-625
    • (2003) Biochem Biophys Res Commun , vol.307 , Issue.3 , pp. 620-625
    • Arora, N.1    Ahmad, T.2    Rajagopal, R.3    Bhatnagar, R.K.4
  • 19
    • 0034893011 scopus 로고    scopus 로고
    • Molecular cloning and structural analysis of the gene encoding Bacillus cereus exochitinase Chi36
    • Wang S.Y., Wu S.J., Thottappilly G., Locy R.D., and Singh N.K. Molecular cloning and structural analysis of the gene encoding Bacillus cereus exochitinase Chi36. J Biosci Bioeng 92 1 (2001) 59-66
    • (2001) J Biosci Bioeng , vol.92 , Issue.1 , pp. 59-66
    • Wang, S.Y.1    Wu, S.J.2    Thottappilly, G.3    Locy, R.D.4    Singh, N.K.5
  • 20
    • 0030770243 scopus 로고    scopus 로고
    • Chitinolytic activity of an endophytic strain of Bacillus cereus
    • Pleban S., Chernin L., and Chet I. Chitinolytic activity of an endophytic strain of Bacillus cereus. Lett Appl Microbiol 25 4 (1997) 284-288
    • (1997) Lett Appl Microbiol , vol.25 , Issue.4 , pp. 284-288
    • Pleban, S.1    Chernin, L.2    Chet, I.3
  • 21
    • 0034761842 scopus 로고    scopus 로고
    • Cloning and sequencing of two genes encoding chitinases A and B from Bacillus cereus CH
    • Mabuchi N., and Araki Y. Cloning and sequencing of two genes encoding chitinases A and B from Bacillus cereus CH. Can J Microbiol 47 10 (2001) 370-375
    • (2001) Can J Microbiol , vol.47 , Issue.10 , pp. 370-375
    • Mabuchi, N.1    Araki, Y.2
  • 22
  • 23
    • 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 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0024662890 scopus 로고
    • Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens
    • Joshi S., Kozlowski M., Richens S., and Comberbach D.M. Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens. Enzyme Microb Technol 11 5 (1989) 289-296
    • (1989) Enzyme Microb Technol , vol.11 , Issue.5 , pp. 289-296
    • Joshi, S.1    Kozlowski, M.2    Richens, S.3    Comberbach, D.M.4
  • 25
    • 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 277 5259 (1970) 680-685
    • (1970) Nature , vol.277 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel J., and Asselin A. Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal Biochem 178 2 (1989) 362-366
    • (1989) Anal Biochem , vol.178 , Issue.2 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 27
    • 0025015465 scopus 로고
    • Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacterriolytic enzymes by polyacrylamide gel electrophoresis
    • Sugai M., Akiyama T., Komatsuzawa H., Miyake Y., and Suginaka H. Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacterriolytic enzymes by polyacrylamide gel electrophoresis. J Bacteriol 172 11 (1990) 6494-6498
    • (1990) J Bacteriol , vol.172 , Issue.11 , pp. 6494-6498
    • Sugai, M.1    Akiyama, T.2    Komatsuzawa, H.3    Miyake, Y.4    Suginaka, H.5
  • 28
    • 74049157010 scopus 로고    scopus 로고
    • Bioassays guided isolation and inhibitory activity against Magnaporthe grisea of the compounds from fruits of Eucalyptus globulus Labill
    • Tan M.L., Zhou L.G., Wang Y., Hao X.J., and Zhang Z.K. Bioassays guided isolation and inhibitory activity against Magnaporthe grisea of the compounds from fruits of Eucalyptus globulus Labill. Acta Pharmacol Sin 37 5 (2007) 535-540
    • (2007) Acta Pharmacol Sin , vol.37 , Issue.5 , pp. 535-540
    • Tan, M.L.1    Zhou, L.G.2    Wang, Y.3    Hao, X.J.4    Zhang, Z.K.5
  • 29
    • 0029019571 scopus 로고
    • Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis
    • Rocha E.R., and Smith C.J. Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis. J Bacteriol 177 11 (1995) 3111-3119
    • (1995) J Bacteriol , vol.177 , Issue.11 , pp. 3111-3119
    • Rocha, E.R.1    Smith, C.J.2
  • 30
    • 0030047892 scopus 로고    scopus 로고
    • Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum
    • Fraaije M.W., Roubroeks H.P., Hagen W.R., and Van Berkel W.J. Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum. Eur J Biochem 235 1-2 (1996) 192-198
    • (1996) Eur J Biochem , vol.235 , Issue.1-2 , pp. 192-198
    • Fraaije, M.W.1    Roubroeks, H.P.2    Hagen, W.R.3    Van Berkel, W.J.4
  • 31
    • 0036067313 scopus 로고    scopus 로고
    • Structural and genetic analysis of the BldB protein of Streptomyces coelicolor
    • Eccleston M., Ali R.A., Seyler R., Westpheling J., and Nodwell J. Structural and genetic analysis of the BldB protein of Streptomyces coelicolor. J Bacteriol 184 15 (2002) 4270-4276
    • (2002) J Bacteriol , vol.184 , Issue.15 , pp. 4270-4276
    • Eccleston, M.1    Ali, R.A.2    Seyler, R.3    Westpheling, J.4    Nodwell, J.5
  • 32
    • 0036562552 scopus 로고    scopus 로고
    • Functional analysis of the Chitin-binding domain of a family 19 Chitinase from Streptomyces griseus HUT6037: substrate-binding affinity and cis-dominant increase of antifungal function
    • Itoh Y., Kawase T., Nikaidou N., Mitsutomi M., Watanabe T., and Itoh Y. Functional analysis of the Chitin-binding domain of a family 19 Chitinase from Streptomyces griseus HUT6037: substrate-binding affinity and cis-dominant increase of antifungal function. Biosci Biotechnol Biochem 66 5 (2002) 1084-1092
    • (2002) Biosci Biotechnol Biochem , vol.66 , Issue.5 , pp. 1084-1092
    • Itoh, Y.1    Kawase, T.2    Nikaidou, N.3    Mitsutomi, M.4    Watanabe, T.5    Itoh, Y.6
  • 33
    • 33749827454 scopus 로고    scopus 로고
    • Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C
    • Itoh Y., Watanabe J., Fukada H., Mizuno R., Kezuka Y., Nonaka T., et al. Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C. Appl Microbiol Biotechnol 72 6 (2006) 1176-1184
    • (2006) Appl Microbiol Biotechnol , vol.72 , Issue.6 , pp. 1176-1184
    • Itoh, Y.1    Watanabe, J.2    Fukada, H.3    Mizuno, R.4    Kezuka, Y.5    Nonaka, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.