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Volumn 36, Issue 3, 2007, Pages 232-237

Effect of the chitin binding domain deletion from Bacillus thuringiensis subsp. kurstaki chitinase Chi255 on its stability in Escherichia coli

Author keywords

B. thuringiensis; Chi255; Chitin binding domain; Deletion; Expression in E. coli

Indexed keywords

BACILLUS THURINGIENSIS; CHITIN BINDING DOMAINS; DELETION; EXPRESSION IN E. COLI; PROTEOLYTIC DEGRADATION;

EID: 36248937188     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12033-007-0030-4     Document Type: Article
Times cited : (14)

References (25)
  • 1
    • 0003133857 scopus 로고
    • The ecology of chitin decomposition
    • Gooday, G. W. (1990). The ecology of chitin decomposition. Advances in Microbial Ecology, 11, 378-430.
    • (1990) Advances in Microbial Ecology , vol.11 , pp. 378-430
    • Gooday, G.W.1
  • 2
    • 0033291773 scopus 로고    scopus 로고
    • Classification of chitinases modules
    • Henrissat, B. (1999). Classification of chitinases modules. EXS, 87, 137-156.
    • (1999) EXS , vol.87 , pp. 137-156
    • Henrissat, B.1
  • 3
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., & Bairoch, A. (1993). New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. The Biochemical Journal, 293, 781-788.
    • (1993) The Biochemical Journal , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 4
    • 0030589694 scopus 로고    scopus 로고
    • Study of particular delta-endotoxins produced by three recently isolated strains of Bacillus thuringiensis
    • Jaoua, S., Zouari, N., Tounsi, S., & Ellouz, R. (1996). Study of particular delta-endotoxins produced by three recently isolated strains of Bacillus thuringiensis. FEMS Microbiology Letters, 145, 349-354.
    • (1996) FEMS Microbiology Letters , vol.145 , pp. 349-354
    • Jaoua, S.1    Zouari, N.2    Tounsi, S.3    Ellouz, R.4
  • 6
    • 0031666818 scopus 로고    scopus 로고
    • Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects
    • Sampson, M. N., & Gooday, G. W. (1998). Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects. Microbiology, 144, 2189-2194.
    • (1998) Microbiology , vol.144 , pp. 2189-2194
    • Sampson, M.N.1    Gooday, G.W.2
  • 7
    • 0034521608 scopus 로고    scopus 로고
    • Toxicity of chitinase-producing Bacillus thuringiensis sp. kurstaki HD-1 toward Plutella xylostella
    • Wiwat, C., Thaithanun, S., Pantuwatana, S., & Bhumiratana, A. (2000). Toxicity of chitinase-producing Bacillus thuringiensis sp. kurstaki HD-1 toward Plutella xylostella. Journal of Invertebrate Pathology, 79, 270-277.
    • (2000) Journal of Invertebrate Pathology , vol.79 , pp. 270-277
    • Wiwat, C.1    Thaithanun, S.2    Pantuwatana, S.3    Bhumiratana, A.4
  • 9
    • 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., & Yuan, Z. M. (2002). Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity. Journal of Applied Microbiology, 93, 374-379.
    • (2002) Journal of Applied Microbiology , vol.93 , 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
  • 10
    • 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. Biotechnology Letters, 26, 635-639.
    • (2004) Biotechnology Letters , vol.26 , pp. 635-639
    • Lin, Y.1    Xiong, G.2
  • 11
    • 0002577185 scopus 로고
    • Improvement of the insecticidal activity of Bacillus thuringiensis var. entomocidus on larvae of Spodoptera littoralis (Lepidoptera-Noctuidae) by addition of chitinolytic bacteria, a phagostimulant and a UV-protectant
    • Sneh, B., Schuster, S., & Gross, S. (1983). Improvement of the insecticidal activity of Bacillus thuringiensis var. entomocidus on larvae of Spodoptera littoralis (Lepidoptera-Noctuidae) by addition of chitinolytic bacteria, a phagostimulant and a UV-protectant. Zeitschrift Fur Angewandte Entomologie, 96, 77-83.
    • (1983) Zeitschrift Fur Angewandte Entomologie , vol.96 , pp. 77-83
    • Sneh, B.1    Schuster, S.2    Gross, S.3
  • 13
    • 0034110888 scopus 로고    scopus 로고
    • Characterization of chitinases excreted by Bacillus cereus CH
    • Mabuchi, N., Hashizume, I., & Araki, Y. (2000). Characterization of chitinases excreted by Bacillus cereus CH. Canadian Journal of Microbiology, 46, 370-375.
    • (2000) Canadian Journal of Microbiology , vol.46 , pp. 370-375
    • Mabuchi, N.1    Hashizume, I.2    Araki, Y.3
  • 15
    • 0025314392 scopus 로고
    • Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe, T., Oyanagi, W., Suzuki, K., & Tanaka, H. (1990). Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. Journal of Bacteriology, 172, 4017-4022.
    • (1990) Journal of Bacteriology , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4
  • 16
    • 25844465801 scopus 로고    scopus 로고
    • Molecular characterization of a novel chitinase from Bacillus thuringiensis subsp. kurstaki
    • Driss, F., Kallassy-Awad, M., Zouari, N., & Jaoua, S. (2005). Molecular characterization of a novel chitinase from Bacillus thuringiensis subsp. kurstaki. Journal of Applied Microbiology, 99, 945-953.
    • (2005) Journal of Applied Microbiology , vol.99 , pp. 945-953
    • Driss, F.1    Kallassy-Awad, M.2    Zouari, N.3    Jaoua, S.4
  • 18
    • 0023028051 scopus 로고
    • A genetic approach to analysing membrane protein topology
    • Manoil, C., & Beckwith, J. (1986). A genetic approach to analysing membrane protein topology. Science, 233, 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 19
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller, G. L. (1959). Use of dinitrosalicylic acid reagent for determination of reducing sugars. Analytical Chemistry, 31, 426-428.
    • (1959) Analytical Chemistry , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0030726362 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain
    • Morimoto, K., Karita, S., Kimura, T., Sakka, K., & Ohmiya, K. (1997). Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. Journal of Bacteriology, 179, 7306-7314.
    • (1997) Journal of Bacteriology , vol.179 , pp. 7306-7314
    • Morimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 23
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces serevisiae
    • Kuranda, M. J., & Robbins, P. W. (1991). Chitinase is required for cell separation during growth of Saccharomyces serevisiae. The Journal of Biological Chemistry, 266, 19758-19767.
    • (1991) The Journal of Biological Chemistry , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 24
    • 0028145771 scopus 로고
    • The role of the C-terminal domain and type III domains chitinase A-1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe, T., Ito, Y., Hachimoto, M., Sekine, S., & Tanaka, H. (1994). The role of the C-terminal domain and type III domains chitinase A-1 from Bacillus circulans WL-12 in chitin degradation. Journal of Bacteriology, 176, 4465-4472.
    • (1994) Journal of Bacteriology , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Hachimoto, M.3    Sekine, S.4    Tanaka, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.