메뉴 건너뛰기




Volumn 42, Issue 5, 2007, Pages 773-790

Bacillus thuringiensis proteases: Production and role in growth, sporulation and synergism

Author keywords

Bacillus thuringiensis; Insecticidal crystal protein; Proteases; Sporulation; Wastewater; Wastewater sludge

Indexed keywords

CELLS; GROWTH KINETICS; INDICATORS (CHEMICAL); INSECT CONTROL; SEWAGE SLUDGE; TOXIC MATERIALS; WASTEWATER;

EID: 34047254300     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2007.01.015     Document Type: Article
Times cited : (34)

References (135)
  • 1
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Hofte H., and Whiteley H.R. Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol Rev 53 (1989) 242-255
    • (1989) Microbiol Rev , vol.53 , pp. 242-255
    • Hofte, H.1    Whiteley, H.R.2
  • 3
    • 0032008260 scopus 로고    scopus 로고
    • Endogenous protease activated 66-kDa toxin from Bacillus thuringiensis subsp. kurstaki active against Spodoptera littoralis
    • Kumar N.S., and Venkateswerlu G. Endogenous protease activated 66-kDa toxin from Bacillus thuringiensis subsp. kurstaki active against Spodoptera littoralis. FEMS Microbiol Lett 159 (1998) 113-120
    • (1998) FEMS Microbiol Lett , vol.159 , pp. 113-120
    • Kumar, N.S.1    Venkateswerlu, G.2
  • 4
    • 0036884443 scopus 로고    scopus 로고
    • Intracellular proteases of Bacillus thuringiensis subsp. kurstaki and a protease-deficient mutant Btk-q
    • Reddy Y.C., and Venkateswerlu G. Intracellular proteases of Bacillus thuringiensis subsp. kurstaki and a protease-deficient mutant Btk-q. Curr Microbiol 45 (2002) 405-409
    • (2002) Curr Microbiol , vol.45 , pp. 405-409
    • Reddy, Y.C.1    Venkateswerlu, G.2
  • 5
    • 0002439624 scopus 로고
    • Microbial proteinases and biotechnology
    • Fogarty C.T., and Kelly K. (Eds), Elsevier, London
    • Outtrup H., and Boyce C.O.L. Microbial proteinases and biotechnology. In: Fogarty C.T., and Kelly K. (Eds). Microbial enzymes and biotechnology (1990), Elsevier, London 227-254
    • (1990) Microbial enzymes and biotechnology , pp. 227-254
    • Outtrup, H.1    Boyce, C.O.L.2
  • 7
    • 0037213311 scopus 로고    scopus 로고
    • An overview on fermentation, downstream processing and properties of microbial alkaline proteases
    • Gupta R., Beg Q.K., Khan S., and Chauhan B. An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl Microbiol Biotechnol 60 (2002) 381-395
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 381-395
    • Gupta, R.1    Beg, Q.K.2    Khan, S.3    Chauhan, B.4
  • 8
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: molecular approaches and industrial applications
    • Gupta R., Beg Q.K., and Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol 59 (2002) 15-32
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, P.3
  • 9
    • 84945927214 scopus 로고
    • Purification and characterization of a thermostable serine protease from Bacillus thuringiensis
    • Kunitate A., Okamoto M., and Ohmori I. Purification and characterization of a thermostable serine protease from Bacillus thuringiensis. Agric Biol Chem 53 (1989) 3251-3256
    • (1989) Agric Biol Chem , vol.53 , pp. 3251-3256
    • Kunitate, A.1    Okamoto, M.2    Ohmori, I.3
  • 10
    • 0027562745 scopus 로고
    • In vitro and in vivo proteolysis of the Bacillus thuringiensis subsp. israelensis CryIVD protein by Culex quinquefasciatus larval midgut proteases
    • Dai S.M., and Gill S.S. In vitro and in vivo proteolysis of the Bacillus thuringiensis subsp. israelensis CryIVD protein by Culex quinquefasciatus larval midgut proteases. Insect Biochem Mol Biol 23 (1993) 273-283
    • (1993) Insect Biochem Mol Biol , vol.23 , pp. 273-283
    • Dai, S.M.1    Gill, S.S.2
  • 11
    • 0030920927 scopus 로고    scopus 로고
    • Cloning of the nprA gene for neutral protease A of Bacillus thuringiensis and effect of in vivo deletion of nprA on insecticidal crystal protein
    • Donovan W.P., Tan Y., and Slaney A.C. Cloning of the nprA gene for neutral protease A of Bacillus thuringiensis and effect of in vivo deletion of nprA on insecticidal crystal protein. Appl Environ Microbiol 63 (1997) 2311-2317
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2311-2317
    • Donovan, W.P.1    Tan, Y.2    Slaney, A.C.3
  • 12
    • 0344541099 scopus 로고    scopus 로고
    • Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki
    • Kumar N.S., and Venkateswerlu G. Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki. Biochem Mol Biol Intl 42 (1997) 901-908
    • (1997) Biochem Mol Biol Intl , vol.42 , pp. 901-908
    • Kumar, N.S.1    Venkateswerlu, G.2
  • 13
    • 0013661269 scopus 로고    scopus 로고
    • Intracellular proteases in sporulated Bacillus thuringiensis subsp. kurstaki and their role in protoxin activation
    • Kumar N.S., and Venkateswerlu G. Intracellular proteases in sporulated Bacillus thuringiensis subsp. kurstaki and their role in protoxin activation. FEMS Microbiol Lett 166 (1998) 377-382
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 377-382
    • Kumar, N.S.1    Venkateswerlu, G.2
  • 14
    • 72949151819 scopus 로고
    • Proteolytic enzymes
    • Hartley B.S. Proteolytic enzymes. Annu Rev Biochem 29 (1960) 45-72
    • (1960) Annu Rev Biochem , vol.29 , pp. 45-72
    • Hartley, B.S.1
  • 15
    • 0022386469 scopus 로고
    • Protease activation of the entomocidal protoxin of Bacillus thuringiensis subsp. kurstaki.
    • Andrews Jr. R.E., Bibilos M.M., and Bulla Jr. L.A. Protease activation of the entomocidal protoxin of Bacillus thuringiensis subsp. kurstaki. Appl Environ Microbiol (1985) 737-742
    • (1985) Appl Environ Microbiol , pp. 737-742
    • Andrews Jr., R.E.1    Bibilos, M.M.2    Bulla Jr., L.A.3
  • 16
    • 0024320570 scopus 로고
    • Proteolytic processing of a coleopteran- specific delta-endotoxin produced by Bacillus thuringiensis var. tenebrionis
    • Carroll J., Li J., and Ellar D.J. Proteolytic processing of a coleopteran- specific delta-endotoxin produced by Bacillus thuringiensis var. tenebrionis. Biochem J 261 (1989) 99-105
    • (1989) Biochem J , vol.261 , pp. 99-105
    • Carroll, J.1    Li, J.2    Ellar, D.J.3
  • 17
    • 0031149715 scopus 로고    scopus 로고
    • Production of alkaline protease by Bacillus thuringiensis H14 in aqueous two-phase systems
    • Hotha S., and Banik R.M. Production of alkaline protease by Bacillus thuringiensis H14 in aqueous two-phase systems. J Chem Tech Biotechnol 69 (1997) 5-10
    • (1997) J Chem Tech Biotechnol , vol.69 , pp. 5-10
    • Hotha, S.1    Banik, R.M.2
  • 18
    • 0034144083 scopus 로고    scopus 로고
    • Bacillus thuringiensis crystal delta-endotoxin: role of proteases in the conversion of protoxin to toxin
    • Rukimini V., Reddy C.Y., and Venkateswerlu G. Bacillus thuringiensis crystal delta-endotoxin: role of proteases in the conversion of protoxin to toxin. Biochimie 82 (2000) 109-116
    • (2000) Biochimie , vol.82 , pp. 109-116
    • Rukimini, V.1    Reddy, C.Y.2    Venkateswerlu, G.3
  • 19
    • 0034876697 scopus 로고    scopus 로고
    • Gene knockout demonstrates that vip3A contributes to the pathogenesis of Bacillus thuringiensis toward Agrotis ipsilon and Spodoptera exigua
    • Donovan W.P., Donovan J.C., and Engleman J.T. Gene knockout demonstrates that vip3A contributes to the pathogenesis of Bacillus thuringiensis toward Agrotis ipsilon and Spodoptera exigua. J Inv Pathol 78 (2001) 45-51
    • (2001) J Inv Pathol , vol.78 , pp. 45-51
    • Donovan, W.P.1    Donovan, J.C.2    Engleman, J.T.3
  • 20
    • 0036208001 scopus 로고    scopus 로고
    • De-repression and subsequent induction of protease synthesis by Bacillus mojavensis under fed-batch operations
    • Beg Q.K., Saxena R.K., and Gupta R. De-repression and subsequent induction of protease synthesis by Bacillus mojavensis under fed-batch operations. Process Biochem 37 (2002) 1103-1109
    • (2002) Process Biochem , vol.37 , pp. 1103-1109
    • Beg, Q.K.1    Saxena, R.K.2    Gupta, R.3
  • 21
    • 0030466509 scopus 로고    scopus 로고
    • Effect of medium composition on the production by a new Bacillus subtilis isolate of protease with promising unhairing activity
    • Varela H., Ferrari M.D., Belobradjic L., Weyrauch R., and Loperena M.L. Effect of medium composition on the production by a new Bacillus subtilis isolate of protease with promising unhairing activity. World J Microbiol Biotechnol 12 (1996) 643-645
    • (1996) World J Microbiol Biotechnol , vol.12 , pp. 643-645
    • Varela, H.1    Ferrari, M.D.2    Belobradjic, L.3    Weyrauch, R.4    Loperena, M.L.5
  • 22
    • 0033044069 scopus 로고    scopus 로고
    • Effect of dissolved oxygen tension and pH on the production of extracellular protease from a new isolate of Bacillus subtilis K2, for use in leather processing
    • Hameed A., Keshavarz T., and Evans C.S. Effect of dissolved oxygen tension and pH on the production of extracellular protease from a new isolate of Bacillus subtilis K2, for use in leather processing. J Chem Technol Biotechnol 74 (1999) 5-8
    • (1999) J Chem Technol Biotechnol , vol.74 , pp. 5-8
    • Hameed, A.1    Keshavarz, T.2    Evans, C.S.3
  • 23
    • 0036545890 scopus 로고    scopus 로고
    • Optimization of alkaline protease production from Bacillus sp. using response surface methodology
    • Puri S., Beg Q.K., and Gupta R. Optimization of alkaline protease production from Bacillus sp. using response surface methodology. Curr Microbiol 44 (2002) 286-290
    • (2002) Curr Microbiol , vol.44 , pp. 286-290
    • Puri, S.1    Beg, Q.K.2    Gupta, R.3
  • 24
    • 0009871589 scopus 로고
    • Immobilization of Bacillus firmus cells in cellulose triacetate fibers and films and their use for proteinase biosynthesis
    • Landau N.S., Egorov N.S., Gornova I.B., Krasovskaya S.B., and Virnik A.D. Immobilization of Bacillus firmus cells in cellulose triacetate fibers and films and their use for proteinase biosynthesis. Microbiology (USSR) 64 (1995) 530-536
    • (1995) Microbiology (USSR) , vol.64 , pp. 530-536
    • Landau, N.S.1    Egorov, N.S.2    Gornova, I.B.3    Krasovskaya, S.B.4    Virnik, A.D.5
  • 25
    • 0009865701 scopus 로고    scopus 로고
    • Proteinase production by free and immobilized cells of Bacillus firmus 44b
    • Landau N.S., Gornova I.B., Gulikova O.M., and Egorov N.S. Proteinase production by free and immobilized cells of Bacillus firmus 44b. Microbiology (USSR) 66 (1997) 310-315
    • (1997) Microbiology (USSR) , vol.66 , pp. 310-315
    • Landau, N.S.1    Gornova, I.B.2    Gulikova, O.M.3    Egorov, N.S.4
  • 26
    • 0025118164 scopus 로고
    • Production of alkaline protease by Bacillus licheniformis in an aqueous two-phase system
    • Lee Y.H., and Chang H.N. Production of alkaline protease by Bacillus licheniformis in an aqueous two-phase system. J Ferment Bioeng 69 (1990) 89-92
    • (1990) J Ferment Bioeng , vol.69 , pp. 89-92
    • Lee, Y.H.1    Chang, H.N.2
  • 27
    • 0002477183 scopus 로고
    • Production of a thermostable alkaline protease by a new Pseudomonas sp. by solid substrate fermentation
    • Chakraborty R., and Srinivasan M. Production of a thermostable alkaline protease by a new Pseudomonas sp. by solid substrate fermentation. J Microb Biotechnol 8 (1993) 7-16
    • (1993) J Microb Biotechnol , vol.8 , pp. 7-16
    • Chakraborty, R.1    Srinivasan, M.2
  • 28
    • 0029111339 scopus 로고
    • Production of protease by Bacillus amyloliquefaciens in solid-state fermentation and its application in the unhairing of hides and skins
    • George S., Raju V., Krishnan M.R.V., Subramanian T.V., and Jayaraman K. Production of protease by Bacillus amyloliquefaciens in solid-state fermentation and its application in the unhairing of hides and skins. Process Biochem 30 (1995) 457-462
    • (1995) Process Biochem , vol.30 , pp. 457-462
    • George, S.1    Raju, V.2    Krishnan, M.R.V.3    Subramanian, T.V.4    Jayaraman, K.5
  • 29
    • 0035745539 scopus 로고    scopus 로고
    • Enhanced production and characterization of a highly thermostable alkaline protease from Bacillus sp. P-2
    • Kaur S., Vohra R.M., Kapoor M., Beg Q.K., and Hoondal G.S. Enhanced production and characterization of a highly thermostable alkaline protease from Bacillus sp. P-2. World J Microbiol Biotechnol 17 (2001) 125-129
    • (2001) World J Microbiol Biotechnol , vol.17 , pp. 125-129
    • Kaur, S.1    Vohra, R.M.2    Kapoor, M.3    Beg, Q.K.4    Hoondal, G.S.5
  • 33
    • 0034681010 scopus 로고    scopus 로고
    • Deletion of aprA and nprA genes for alkaline protease A and neutral protease A from Bacillus thuringiensis: effect on insecticidal crystal proteins
    • Tan Y., and Donovan W.P. Deletion of aprA and nprA genes for alkaline protease A and neutral protease A from Bacillus thuringiensis: effect on insecticidal crystal proteins. J Biotechnol 84 (2000) 67-72
    • (2000) J Biotechnol , vol.84 , pp. 67-72
    • Tan, Y.1    Donovan, W.P.2
  • 34
    • 0036203159 scopus 로고    scopus 로고
    • Sporulation and δ -endotoxin synthesis by Bacillus thuringiensis
    • Aronson A. Sporulation and δ -endotoxin synthesis by Bacillus thuringiensis. Cell Mol Life Sci 59 (2002) 417-425
    • (2002) Cell Mol Life Sci , vol.59 , pp. 417-425
    • Aronson, A.1
  • 35
    • 0033180054 scopus 로고    scopus 로고
    • Production and characterization of metalloproteases synthesized concomitantly with δ-endotoxin by Bacillus thuringiensis subsp. kurstaki strain grown on gruel-based media
    • Zouari N., and Jaoua S. Production and characterization of metalloproteases synthesized concomitantly with δ-endotoxin by Bacillus thuringiensis subsp. kurstaki strain grown on gruel-based media. Enzyme Microb Technol 25 (1999) 364-371
    • (1999) Enzyme Microb Technol , vol.25 , pp. 364-371
    • Zouari, N.1    Jaoua, S.2
  • 36
    • 0023839274 scopus 로고
    • Production of protease by Bacillus subtilis using simultaneous control of glucose and ammonium concentrations
    • Kole M.M., Draper I., and Gerson D.F. Production of protease by Bacillus subtilis using simultaneous control of glucose and ammonium concentrations. J Chem Technol Biotechnol 41 (1988) 197-206
    • (1988) J Chem Technol Biotechnol , vol.41 , pp. 197-206
    • Kole, M.M.1    Draper, I.2    Gerson, D.F.3
  • 37
    • 0000795704 scopus 로고
    • Crystalline soybean trypsin inhibitor
    • Kunitz M. Crystalline soybean trypsin inhibitor. J Gen Physiol 30 (1947) 291-310
    • (1947) J Gen Physiol , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 38
    • 0037009174 scopus 로고    scopus 로고
    • Production of delta-endotoxins by Bacillus thuringiensis strains exhibiting various insecticidal activities towards Lepidoptera and diptera in gruel and fish meal media
    • Zouari N., Ali S.B.S., and Jaoua S. Production of delta-endotoxins by Bacillus thuringiensis strains exhibiting various insecticidal activities towards Lepidoptera and diptera in gruel and fish meal media. Enzyme Microb Technol 31 (2002) 411-418
    • (2002) Enzyme Microb Technol , vol.31 , pp. 411-418
    • Zouari, N.1    Ali, S.B.S.2    Jaoua, S.3
  • 39
    • 0016217656 scopus 로고
    • Pleiotropic mutations affecting sporulation conditions and the synthesis of extracellular enzymes in Bacillus subtilis 168
    • Kunst F., Pascal M., Lepesant-Kejzlarova J., Lepesant J.-A., Billault A., and Dedonder R. Pleiotropic mutations affecting sporulation conditions and the synthesis of extracellular enzymes in Bacillus subtilis 168. Biochimie 56 (1974) 1481-1489
    • (1974) Biochimie , vol.56 , pp. 1481-1489
    • Kunst, F.1    Pascal, M.2    Lepesant-Kejzlarova, J.3    Lepesant, J.-A.4    Billault, A.5    Dedonder, R.6
  • 40
    • 0025164975 scopus 로고
    • Signal transduction pathway controlling synthesis of a class of degradative enzymes in Bacillus subtilis: expression of the regulatory genes and analysis of mutations in degS and degU
    • Msadek T., Kunst F., Henner D., Klier A., Rapoport G., and Dedonder R. Signal transduction pathway controlling synthesis of a class of degradative enzymes in Bacillus subtilis: expression of the regulatory genes and analysis of mutations in degS and degU. J Bacteriol (1990) 824-834
    • (1990) J Bacteriol , pp. 824-834
    • Msadek, T.1    Kunst, F.2    Henner, D.3    Klier, A.4    Rapoport, G.5    Dedonder, R.6
  • 41
    • 33847297485 scopus 로고    scopus 로고
    • Improvement of Bacillus thuringiensis delta-endotoxin production by overcome of carbon catabolite repression through adequate control of aeration
    • Ghribi D., Zouari N., Trabelsi H., and Jaoua S. Improvement of Bacillus thuringiensis delta-endotoxin production by overcome of carbon catabolite repression through adequate control of aeration. Enzyme Microb Technol 40 4 (2007) 612-622
    • (2007) Enzyme Microb Technol , vol.40 , Issue.4 , pp. 612-622
    • Ghribi, D.1    Zouari, N.2    Trabelsi, H.3    Jaoua, S.4
  • 42
    • 33344457744 scopus 로고    scopus 로고
    • Molecular screening of Bacillus thuringiensis strains from wastewater sludge for biopesticide production
    • Mohammedi S., Subramanian B., Song Y., Tyagi R.D., and Valéro J.R. Molecular screening of Bacillus thuringiensis strains from wastewater sludge for biopesticide production. Process Biochem 41 4 (2006) 829-835
    • (2006) Process Biochem , vol.41 , Issue.4 , pp. 829-835
    • Mohammedi, S.1    Subramanian, B.2    Song, Y.3    Tyagi, R.D.4    Valéro, J.R.5
  • 43
    • 34047247194 scopus 로고    scopus 로고
    • Simultaneous production of biopesticide and alkaline proteases by Bacillus thuringiensis using wastewater as a raw material
    • Tyagi R.D., Sikati Foko V., Barnabé S., Vidyarthi A., and Valéro J.R. Simultaneous production of biopesticide and alkaline proteases by Bacillus thuringiensis using wastewater as a raw material. Water Sci Technol 46 (2002) 47-254
    • (2002) Water Sci Technol , vol.46 , pp. 47-254
    • Tyagi, R.D.1    Sikati Foko, V.2    Barnabé, S.3    Vidyarthi, A.4    Valéro, J.R.5
  • 44
    • 27944433714 scopus 로고    scopus 로고
    • Wastewater sludge pre-treatment for enhancing entomotoxicity produced by Bacillus thuringiensis var. kurstaki
    • Yezza A., Tyagi R.D., Valero J.R., and Surampalli R.Y. Wastewater sludge pre-treatment for enhancing entomotoxicity produced by Bacillus thuringiensis var. kurstaki. World J Microbiol Biotechnol 21 (2005) 1165-1174
    • (2005) World J Microbiol Biotechnol , vol.21 , pp. 1165-1174
    • Yezza, A.1    Tyagi, R.D.2    Valero, J.R.3    Surampalli, R.Y.4
  • 45
    • 33745470222 scopus 로고    scopus 로고
    • Bioconversion of industrial wastewater and wastewater sludge into Bacillus thuringiensis based biopesticides in pilot fermenter
    • Yezza A., Tyagi R.D., Valero J.R., and Surampalli R.Y. Bioconversion of industrial wastewater and wastewater sludge into Bacillus thuringiensis based biopesticides in pilot fermenter. Biores Technol 26 (2006) 1850-1857
    • (2006) Biores Technol , vol.26 , pp. 1850-1857
    • Yezza, A.1    Tyagi, R.D.2    Valero, J.R.3    Surampalli, R.Y.4
  • 46
    • 0034847596 scopus 로고    scopus 로고
    • Wastewater treatment sludge as a raw material for the production of Bacillus thuringiensis based biopesticides
    • Tirado-Montiel M.L., Tyagi R.D., and Valero J.R. Wastewater treatment sludge as a raw material for the production of Bacillus thuringiensis based biopesticides. Water Res 35 16 (2001) 3807-3816
    • (2001) Water Res , vol.35 , Issue.16 , pp. 3807-3816
    • Tirado-Montiel, M.L.1    Tyagi, R.D.2    Valero, J.R.3
  • 47
    • 0037426295 scopus 로고    scopus 로고
    • Novel alkaline proteases from alkaliphilic bacteria grown on chicken feather
    • Gessesse A., Hatti-Kaul R., Gashe B.A., and Mattiasson B. Novel alkaline proteases from alkaliphilic bacteria grown on chicken feather. Enzyme Microb Technol 32 (2003) 519-524
    • (2003) Enzyme Microb Technol , vol.32 , pp. 519-524
    • Gessesse, A.1    Hatti-Kaul, R.2    Gashe, B.A.3    Mattiasson, B.4
  • 48
    • 0023731881 scopus 로고
    • Inhibition of Bacillus thuringiensis proteases and their effects on crystal toxin proteins and cell free translations
    • Bibilos M., and Andrews Jr. R.E. Inhibition of Bacillus thuringiensis proteases and their effects on crystal toxin proteins and cell free translations. Can J Microbiol 34 (1988) 740-742
    • (1988) Can J Microbiol , vol.34 , pp. 740-742
    • Bibilos, M.1    Andrews Jr., R.E.2
  • 49
    • 0016719994 scopus 로고
    • Metalloprotease from Bacillus thuringiensis
    • Li E., and Yousten A.A. Metalloprotease from Bacillus thuringiensis. Appl Microbiol (1975) 354-361
    • (1975) Appl Microbiol , pp. 354-361
    • Li, E.1    Yousten, A.A.2
  • 50
    • 0022534303 scopus 로고
    • Cloning and sequencing of the intracellular serine protease gene of Bacillus subtilis
    • Koide Y., Nakamura A., Uozumi T., and Beppu T. Cloning and sequencing of the intracellular serine protease gene of Bacillus subtilis. J Bacteriol 67 (1986) 110-116
    • (1986) J Bacteriol , vol.67 , pp. 110-116
    • Koide, Y.1    Nakamura, A.2    Uozumi, T.3    Beppu, T.4
  • 51
    • 0022471036 scopus 로고
    • Activation of intracellular serine proteinase in Bacillus subtilis cells during sporulation
    • Burnett T.J., Shankweiler G.W., and Hageman J.H. Activation of intracellular serine proteinase in Bacillus subtilis cells during sporulation. J Bacteriol 165 (1986) 139-145
    • (1986) J Bacteriol , vol.165 , pp. 139-145
    • Burnett, T.J.1    Shankweiler, G.W.2    Hageman, J.H.3
  • 52
    • 0025057969 scopus 로고
    • Intracellular serine protease of Bacillus subtilis is formed in vivo as an unprocessed, active protease in stationary cells
    • Sheehan S.M., and Switzer R.L. Intracellular serine protease of Bacillus subtilis is formed in vivo as an unprocessed, active protease in stationary cells. J Bacteriol 172 (1990) 473-476
    • (1990) J Bacteriol , vol.172 , pp. 473-476
    • Sheehan, S.M.1    Switzer, R.L.2
  • 53
    • 0020567439 scopus 로고
    • Characterization of Bacillus subtilis mutants with a temperature-sensitive intracellular protease
    • Sastry K.J., Srivastava O.P., Millet J., FitzJames P.C., and Aronson A.I. Characterization of Bacillus subtilis mutants with a temperature-sensitive intracellular protease. J Bacteriol 153 (1983) 511-519
    • (1983) J Bacteriol , vol.153 , pp. 511-519
    • Sastry, K.J.1    Srivastava, O.P.2    Millet, J.3    FitzJames, P.C.4    Aronson, A.I.5
  • 56
    • 0036202545 scopus 로고    scopus 로고
    • Bacillus subtilis sporulation and stationary phase gene expression
    • Phillips Z.E., and Strauch M.A. Bacillus subtilis sporulation and stationary phase gene expression. Cell Mol Life Sci 59 (2002) 392-402
    • (2002) Cell Mol Life Sci , vol.59 , pp. 392-402
    • Phillips, Z.E.1    Strauch, M.A.2
  • 57
    • 0037089590 scopus 로고    scopus 로고
    • A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localization
    • Runder D.Z., and Losick R. A sporulation membrane protein tethers the pro-sigmaK processing enzyme to its inhibitor and dictates its subcellular localization. Genes Dev 16 (2002) 1007-1018
    • (2002) Genes Dev , vol.16 , pp. 1007-1018
    • Runder, D.Z.1    Losick, R.2
  • 58
    • 0141677809 scopus 로고    scopus 로고
    • SpoIVB-mediated cleavage of Spo-IVFA could provide the intracellular signal to activate processing of pro-sigmaK in Bacillus subtilis
    • Dong T.C., and Cutting S.M. SpoIVB-mediated cleavage of Spo-IVFA could provide the intracellular signal to activate processing of pro-sigmaK in Bacillus subtilis. Mol Microbiol 49 (2003) 1425-1434
    • (2003) Mol Microbiol , vol.49 , pp. 1425-1434
    • Dong, T.C.1    Cutting, S.M.2
  • 59
    • 0344983845 scopus 로고    scopus 로고
    • The IspA protease's involvement in the regulation of the sporulation process of Bacillus thuringiensis is revealed by proteomic analysis
    • Chen F.-C., Shen L.-F., Tsai M.-C., and Chak K.-F. The IspA protease's involvement in the regulation of the sporulation process of Bacillus thuringiensis is revealed by proteomic analysis. Biochem Biophys Res Commun 312 (2003) 708-715.
    • (2003) Biochem Biophys Res Commun , vol.312
    • Chen, F.-C.1    Shen, L.-F.2    Tsai, M.-C.3    Chak, K.-F.4
  • 60
    • 0021398927 scopus 로고
    • Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropins, two classes of antibacterial proteins in insects
    • Dalhammar G., and Steiner H. Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropins, two classes of antibacterial proteins in insects. Eur J Biochem 139 2 (1984) 247-252
    • (1984) Eur J Biochem , vol.139 , Issue.2 , pp. 247-252
    • Dalhammar, G.1    Steiner, H.2
  • 61
    • 0034921153 scopus 로고    scopus 로고
    • Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation
    • Grandvalet C., Gominet M., and Lereclus D. Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation. Microbiology 147 (2001) 1805-1813
    • (2001) Microbiology , vol.147 , pp. 1805-1813
    • Grandvalet, C.1    Gominet, M.2    Lereclus, D.3
  • 62
    • 33344467290 scopus 로고    scopus 로고
    • Correlation between entomotoxicity potency and protease activity produced by Bacillus thuringiensis var. kurstaki grown in wastewater sludge
    • Yezza A., Tyagi R.D., Valero J.R., and Surampalli R.Y. Correlation between entomotoxicity potency and protease activity produced by Bacillus thuringiensis var. kurstaki grown in wastewater sludge. Process Biochem 41 (2006) 780-794
    • (2006) Process Biochem , vol.41 , pp. 780-794
    • Yezza, A.1    Tyagi, R.D.2    Valero, J.R.3    Surampalli, R.Y.4
  • 63
    • 12944297132 scopus 로고    scopus 로고
    • Production of Bacillus thuringiensis based biopesticides in batch and fed cultures using wastewater sludge as a raw material
    • Yezza A., Tyagi R.D., Valero J.R., and Surampalli R.Y. Production of Bacillus thuringiensis based biopesticides in batch and fed cultures using wastewater sludge as a raw material. J Ind Microbiol Biotechnol 31 (2004) 545-552
    • (2004) J Ind Microbiol Biotechnol , vol.31 , pp. 545-552
    • Yezza, A.1    Tyagi, R.D.2    Valero, J.R.3    Surampalli, R.Y.4
  • 65
    • 0032762737 scopus 로고    scopus 로고
    • Enhanced growth, sporulation and toxin production by Bacillus thuringiensis kurstaki in oil seed meal extract media containing cystine
    • Vora D., and Shethna Y.I. Enhanced growth, sporulation and toxin production by Bacillus thuringiensis kurstaki in oil seed meal extract media containing cystine. World J Microbiol Biotechnol 15 (1999) 747-749
    • (1999) World J Microbiol Biotechnol , vol.15 , pp. 747-749
    • Vora, D.1    Shethna, Y.I.2
  • 66
    • 34047261790 scopus 로고    scopus 로고
    • Barnabé S. Hydrolyse et oxydation partielle des boues d'épuration comme substrat pour produire Bacillus thuringiensis HD-1. Ph.D thesis, Institut National de la Recherche Scientifique, Eau, Terre et Environnement, Université du Québec, Québec, Canada; 2005. p. 255.
  • 67
    • 22944479287 scopus 로고    scopus 로고
    • Sludge based Bacillus thuringiensis biopesticides: viscosity impacts
    • Brar S.K., Verma M., Tyagi R.D., Valéro J.R., and Surampalli R.Y. Sludge based Bacillus thuringiensis biopesticides: viscosity impacts. Water Res 39 (2005) 3001-3011
    • (2005) Water Res , vol.39 , pp. 3001-3011
    • Brar, S.K.1    Verma, M.2    Tyagi, R.D.3    Valéro, J.R.4    Surampalli, R.Y.5
  • 68
    • 0000933020 scopus 로고    scopus 로고
    • Effect of cultural conditions on spore-crystal yield and toxicity of Bacillus thuringiensis subsp. aizawai (HD133)
    • Morris O.N., Converse V., Kanagaratnam P., and Davies J.S. Effect of cultural conditions on spore-crystal yield and toxicity of Bacillus thuringiensis subsp. aizawai (HD133). J Invertebr Pathol 67 (1996) 129-136
    • (1996) J Invertebr Pathol , vol.67 , pp. 129-136
    • Morris, O.N.1    Converse, V.2    Kanagaratnam, P.3    Davies, J.S.4
  • 69
    • 0141908156 scopus 로고    scopus 로고
    • Specific oxygen uptake rate variations during batch fermentation of Bacillus thuringiensis subspecies kurstaki HD-1
    • Rowe G.E., Margaritis A., and Wei N. Specific oxygen uptake rate variations during batch fermentation of Bacillus thuringiensis subspecies kurstaki HD-1. Biotechnol Prog 19 (2003) 1439-1443
    • (2003) Biotechnol Prog , vol.19 , pp. 1439-1443
    • Rowe, G.E.1    Margaritis, A.2    Wei, N.3
  • 70
    • 15744390784 scopus 로고    scopus 로고
    • Impact of Tween 80 during Bacillus thuringiensis fermentation of wastewater sludges
    • Brar S.K., Verma M., Tyagi R.D., Valéro J.R., and Surampalli R.Y. Impact of Tween 80 during Bacillus thuringiensis fermentation of wastewater sludges. Process Biochem 40 (2005) 2695-2705
    • (2005) Process Biochem , vol.40 , pp. 2695-2705
    • Brar, S.K.1    Verma, M.2    Tyagi, R.D.3    Valéro, J.R.4    Surampalli, R.Y.5
  • 71
    • 0028877394 scopus 로고
    • The protoxin composition of Bacillus thuringiensis insecticidal inclusions affects solubility and toxicity
    • Aronson A.I. The protoxin composition of Bacillus thuringiensis insecticidal inclusions affects solubility and toxicity. Appl Environ Microbiol 61 (1995) 4057-4060
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4057-4060
    • Aronson, A.I.1
  • 73
    • 23044493446 scopus 로고    scopus 로고
    • Using worms to better understand how Bacillus thuringiensis kills insects
    • Crickmore N. Using worms to better understand how Bacillus thuringiensis kills insects. Trends Microbiol 13 8 (2005) 347-350
    • (2005) Trends Microbiol , vol.13 , Issue.8 , pp. 347-350
    • Crickmore, N.1
  • 74
    • 33645307684 scopus 로고    scopus 로고
    • The effect of oxygen on the sporulation, δ-endotoxin synthesis and toxicity of Bacillus thuringiensis H14
    • Sarrafzadeh M.H., and Navarro J.M. The effect of oxygen on the sporulation, δ-endotoxin synthesis and toxicity of Bacillus thuringiensis H14. World J Microbiol Biotechnol 22 (2006) 305-310
    • (2006) World J Microbiol Biotechnol , vol.22 , pp. 305-310
    • Sarrafzadeh, M.H.1    Navarro, J.M.2
  • 75
    • 0003121387 scopus 로고
    • Bacillus thuringiensis growth, sporulation and delta-endotoxin production in oxygen limited and non-limited cultures
    • Avignone-Rossa C., Arcas J., and Mignone C. Bacillus thuringiensis growth, sporulation and delta-endotoxin production in oxygen limited and non-limited cultures. World J Microbiol Biotechnol 8 (1992) 301-304
    • (1992) World J Microbiol Biotechnol , vol.8 , pp. 301-304
    • Avignone-Rossa, C.1    Arcas, J.2    Mignone, C.3
  • 76
    • 0037025317 scopus 로고    scopus 로고
    • N-terminal activation is an essential early step in the mechanism of action of the Bacillus thuringiensis Cry1Ac insecticidal toxin
    • Bravo A., Sánchez J., Kouskoura T., and Crickmore N. N-terminal activation is an essential early step in the mechanism of action of the Bacillus thuringiensis Cry1Ac insecticidal toxin. J Biol Chem 277 27 (2002) 23985-23987
    • (2002) J Biol Chem , vol.277 , Issue.27 , pp. 23985-23987
    • Bravo, A.1    Sánchez, J.2    Kouskoura, T.3    Crickmore, N.4
  • 77
    • 0037267356 scopus 로고    scopus 로고
    • PCR-based identification of Bacillus thuringiensis pesticidal crystal genes
    • Porcar M., and Juarez-Pérez V. PCR-based identification of Bacillus thuringiensis pesticidal crystal genes. FEMS Microbiol Rev 26 (2003) 419-432
    • (2003) FEMS Microbiol Rev , vol.26 , pp. 419-432
    • Porcar, M.1    Juarez-Pérez, V.2
  • 79
    • 0030883387 scopus 로고    scopus 로고
    • CytA enables CryIV endotoxins of Bacillus thuringiensis to overcome high levels of CryIV resistance in the mosquito, Culex quinquefasciatus
    • Wirth M.C., Georghiou G.P., and Federici B.A. CytA enables CryIV endotoxins of Bacillus thuringiensis to overcome high levels of CryIV resistance in the mosquito, Culex quinquefasciatus. Proc National Acad Sci USA 94 (1997) 10536-10540
    • (1997) Proc National Acad Sci USA , vol.94 , pp. 10536-10540
    • Wirth, M.C.1    Georghiou, G.P.2    Federici, B.A.3
  • 80
    • 0031763335 scopus 로고    scopus 로고
    • Cyt1Aa protein of Bacillus thuringiensis is toxic to the cottonwood leaf beetle, Chrysomela scripta, and suppresses high levels of resistance to Cry3Aa
    • Federici B.A., and Bauer L.S. Cyt1Aa protein of Bacillus thuringiensis is toxic to the cottonwood leaf beetle, Chrysomela scripta, and suppresses high levels of resistance to Cry3Aa. Appl Environ Microbiol 64 (1998) 4368-4371
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4368-4371
    • Federici, B.A.1    Bauer, L.S.2
  • 81
    • 0031920488 scopus 로고    scopus 로고
    • Spore coat protein synergizes Bacillus thuringiensis crystal toxicity for the Indianmeal moth (Plodia interpunctella)
    • Johnson D.E., Oppert B., and McGaughey W.H. Spore coat protein synergizes Bacillus thuringiensis crystal toxicity for the Indianmeal moth (Plodia interpunctella). Curr Microbiol 36 (1998) 278-282
    • (1998) Curr Microbiol , vol.36 , pp. 278-282
    • Johnson, D.E.1    Oppert, B.2    McGaughey, W.H.3
  • 82
    • 0025111009 scopus 로고
    • Simple method for the isolation of the antilepidopteran toxin from Bacillus thuringiensis subsp. kurstaki
    • Venkateswerlu G., and Stotzky G. Simple method for the isolation of the antilepidopteran toxin from Bacillus thuringiensis subsp. kurstaki. Biotechnol Appl Biochem 12 (1990) 245-251
    • (1990) Biotechnol Appl Biochem , vol.12 , pp. 245-251
    • Venkateswerlu, G.1    Stotzky, G.2
  • 83
    • 0019013770 scopus 로고
    • Crystal-forming proteins of Bacillus thuringiensis. The limited hydrolysis by endogeneous proteinases as a cause of their apparent multiplicity
    • Chestukhina G.G., Zalunin I.A., Kostina L.I., Kotova T.S., Kattrukha S.P., and Stepanov V.M. Crystal-forming proteins of Bacillus thuringiensis. The limited hydrolysis by endogeneous proteinases as a cause of their apparent multiplicity. Biochem J 187 2 (1980) 457-465
    • (1980) Biochem J , vol.187 , Issue.2 , pp. 457-465
    • Chestukhina, G.G.1    Zalunin, I.A.2    Kostina, L.I.3    Kotova, T.S.4    Kattrukha, S.P.5    Stepanov, V.M.6
  • 84
  • 85
    • 0022458502 scopus 로고
    • Specificity of Bacillus thuringiensis var. colmeri insecticidal δ-endotoxin is determined by differential proteolytic processing of the protoxin by larval gut proteases
    • Haider M.Z., Knowles B.H., and Ellar D.J. Specificity of Bacillus thuringiensis var. colmeri insecticidal δ-endotoxin is determined by differential proteolytic processing of the protoxin by larval gut proteases. Eur J Biochem 156 (1986) 531-540
    • (1986) Eur J Biochem , vol.156 , pp. 531-540
    • Haider, M.Z.1    Knowles, B.H.2    Ellar, D.J.3
  • 86
    • 0025685252 scopus 로고
    • Molecular characterization of immune inhibitor A, a secreted virulence protease from Bacillus thuringiensis
    • Lovgren A., Zhang M., Engstrom A., Dalhammar G., and Lamden R. Molecular characterization of immune inhibitor A, a secreted virulence protease from Bacillus thuringiensis. Mol Microbiol 4 (1990) 2137-2146
    • (1990) Mol Microbiol , vol.4 , pp. 2137-2146
    • Lovgren, A.1    Zhang, M.2    Engstrom, A.3    Dalhammar, G.4    Lamden, R.5
  • 87
    • 0028366037 scopus 로고
    • Intracellular proteolysis and limited diversity of the Bacillus thuringiensis CryIA family of the insecticidal crystal proteins
    • Almond B.D., and Dean D.H. Intracellular proteolysis and limited diversity of the Bacillus thuringiensis CryIA family of the insecticidal crystal proteins. Biochem Biophys Res Commun 201 2 (1994) 788-794
    • (1994) Biochem Biophys Res Commun , vol.201 , Issue.2 , pp. 788-794
    • Almond, B.D.1    Dean, D.H.2
  • 88
    • 0034310227 scopus 로고    scopus 로고
    • Synergism of the spore on insecticidal activity of delta-endotoxin of Bacillus thuringiensis against the diamondback moth, Plutella xylostella (Lepidoptera: Yponomeutidae) is not observed at late stage in bioassay
    • Asano S., Ogiwara K., Indrasith L.S., Takahashi M., Suzuki N., and Hori H. Synergism of the spore on insecticidal activity of delta-endotoxin of Bacillus thuringiensis against the diamondback moth, Plutella xylostella (Lepidoptera: Yponomeutidae) is not observed at late stage in bioassay. Appl Entomol Zool 35 (2000) 583-590
    • (2000) Appl Entomol Zool , vol.35 , pp. 583-590
    • Asano, S.1    Ogiwara, K.2    Indrasith, L.S.3    Takahashi, M.4    Suzuki, N.5    Hori, H.6
  • 90
    • 30744463916 scopus 로고    scopus 로고
    • Starch industry wastewater based stable Bacillus thuringiensis liquid formulations
    • Brar S.K., Verma M., Tyagi R.D., Valéro J.R., and Surampalli R.Y. Starch industry wastewater based stable Bacillus thuringiensis liquid formulations. J Econ Entomol 98 6 (2005) 1890-1898
    • (2005) J Econ Entomol , vol.98 , Issue.6 , pp. 1890-1898
    • Brar, S.K.1    Verma, M.2    Tyagi, R.D.3    Valéro, J.R.4    Surampalli, R.Y.5
  • 91
    • 0026050639 scopus 로고
    • Crystal structures of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • Li J., Carroll J., and Ellar D.J. Crystal structures of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353 (1991) 815-821
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 93
    • 0014007428 scopus 로고
    • Purification and properties of two peptidases from brewer's yeast
    • Felix F., and Brouillet N. Purification and properties of two peptidases from brewer's yeast. Biochim Biophys Acta 122 (1966) 127-144
    • (1966) Biochim Biophys Acta , vol.122 , pp. 127-144
    • Felix, F.1    Brouillet, N.2
  • 94
    • 0017823596 scopus 로고
    • Aminopeptidase I activities in several microorganisms
    • de Marco A.C., and Dick A.J. Aminopeptidase I activities in several microorganisms. Can J Biochem 56 (1978) 66-71
    • (1978) Can J Biochem , vol.56 , pp. 66-71
    • de Marco, A.C.1    Dick, A.J.2
  • 96
    • 0021918104 scopus 로고
    • Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase
    • Hibbs M.S., Hasty K.A., Seyer J.M., Kang A.H., and Mainardi C.L. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J Biol Chem 260 (1985) 2493-2500
    • (1985) J Biol Chem , vol.260 , pp. 2493-2500
    • Hibbs, M.S.1    Hasty, K.A.2    Seyer, J.M.3    Kang, A.H.4    Mainardi, C.L.5
  • 97
    • 0008125284 scopus 로고
    • Proteolytic enzymes: serine and cysteine peptidases
    • Barett A.J. Proteolytic enzymes: serine and cysteine peptidases. Methods Enzymol 244 (1994) 1-15
    • (1994) Methods Enzymol , vol.244 , pp. 1-15
    • Barett, A.J.1
  • 98
    • 0002873247 scopus 로고
    • Proteolytic enzymes: aspartic and metallopeptidases
    • Barett A.J. Proteolytic enzymes: aspartic and metallopeptidases. Methods Enzymol 248 (1995) 183
    • (1995) Methods Enzymol , vol.248 , pp. 183
    • Barett, A.J.1
  • 99
    • 6844251001 scopus 로고    scopus 로고
    • Comparative analysis of intracellular proteases in sporulated Bacillus thuringiensis strains
    • Reddy S.T., and Venkateswerlu G. Comparative analysis of intracellular proteases in sporulated Bacillus thuringiensis strains. Biotechnol Lett 20 3 (1998) 279-281
    • (1998) Biotechnol Lett , vol.20 , Issue.3 , pp. 279-281
    • Reddy, S.T.1    Venkateswerlu, G.2
  • 100
    • 0034131455 scopus 로고    scopus 로고
    • The interactions between soybean trypsin inhibitor and δ-endotoxin of Bacillus thuringiensis in Helicoverpa armigera larva
    • Zhang J.H., Wang C.Z., and Qin J.D. The interactions between soybean trypsin inhibitor and δ-endotoxin of Bacillus thuringiensis in Helicoverpa armigera larva. J Invertebr Pathol 75 (2000) 259-266
    • (2000) J Invertebr Pathol , vol.75 , pp. 259-266
    • Zhang, J.H.1    Wang, C.Z.2    Qin, J.D.3
  • 101
    • 0033984398 scopus 로고    scopus 로고
    • Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal N-endotoxin of Bacillus thuringiensis subsp. tenebrionis
    • Reddy S.T., Kumar N.S., and Venkateswerlu G. Identification and purification of the 69-kDa intracellular protease involved in the proteolytic processing of the crystal N-endotoxin of Bacillus thuringiensis subsp. tenebrionis. FEMS Microbiol Lett 183 (2000) 63-66
    • (2000) FEMS Microbiol Lett , vol.183 , pp. 63-66
    • Reddy, S.T.1    Kumar, N.S.2    Venkateswerlu, G.3
  • 102
    • 0001701325 scopus 로고
    • Midgut protease activities in 12 phytophagous lepidopteran larvae: dietary and protease inhibitor interactions
    • Christeller J.T., Laing W.A., Markwick N.P., and Burgess E.P.J. Midgut protease activities in 12 phytophagous lepidopteran larvae: dietary and protease inhibitor interactions. Insect Biochem Mol Biol 22 (1992) 735-746
    • (1992) Insect Biochem Mol Biol , vol.22 , pp. 735-746
    • Christeller, J.T.1    Laing, W.A.2    Markwick, N.P.3    Burgess, E.P.J.4
  • 103
    • 0026914204 scopus 로고
    • Processing of δ-endotoxin from Bacillus thuringiensis subsp. Kurstaki HD-1 and HD-73 by gut juices of various insect larvae
    • Ogiwara K., Indrasith L.S., Asano S., and Hori H. Processing of δ-endotoxin from Bacillus thuringiensis subsp. Kurstaki HD-1 and HD-73 by gut juices of various insect larvae. J Invertebr Pathol 60 (1992) 121-126
    • (1992) J Invertebr Pathol , vol.60 , pp. 121-126
    • Ogiwara, K.1    Indrasith, L.S.2    Asano, S.3    Hori, H.4
  • 105
    • 0030159151 scopus 로고    scopus 로고
    • Luminal proteases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin
    • Oppert B., Kramer K.J., Johnson D., Upton S.J., and McGaughey W.H. Luminal proteases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin. Insect Biochem Mol Biol 26 (1996) 571-583
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 571-583
    • Oppert, B.1    Kramer, K.J.2    Johnson, D.3    Upton, S.J.4    McGaughey, W.H.5
  • 106
    • 0030764154 scopus 로고    scopus 로고
    • Protease-mediated insect resistance to Bacillus thuringiensis toxins
    • Oppert B., Kramer K.J., Beeman R.W., Johnson D., and McGaughey W.H. Protease-mediated insect resistance to Bacillus thuringiensis toxins. J Biol Chem 272 (1997) 23473-23476
    • (1997) J Biol Chem , vol.272 , pp. 23473-23476
    • Oppert, B.1    Kramer, K.J.2    Beeman, R.W.3    Johnson, D.4    McGaughey, W.H.5
  • 107
    • 0031725639 scopus 로고    scopus 로고
    • Degradation of Bacillus thuringiensis δ-endotoxin in host insect gut juice
    • Pang A.S.D., and Gringorten J.L. Degradation of Bacillus thuringiensis δ-endotoxin in host insect gut juice. FEMS Microbiol Lett 167 (1998) 281-285
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 281-285
    • Pang, A.S.D.1    Gringorten, J.L.2
  • 108
    • 0032111202 scopus 로고    scopus 로고
    • Processing of δ-endotoxin of Bacillus thuringiensis subsp. kurstaki HD-1 in Heliothis armigera midgut juice and the effects of protease inhibitors
    • Shao Z., Cui Y., Liu X., Yi H., Ji J., and Yu Z. Processing of δ-endotoxin of Bacillus thuringiensis subsp. kurstaki HD-1 in Heliothis armigera midgut juice and the effects of protease inhibitors. J Invertebr Pathol 72 (1998) 73-81
    • (1998) J Invertebr Pathol , vol.72 , pp. 73-81
    • Shao, Z.1    Cui, Y.2    Liu, X.3    Yi, H.4    Ji, J.5    Yu, Z.6
  • 109
    • 0033848481 scopus 로고    scopus 로고
    • Activation Pattern and Toxicity of the Cry11Bb1 toxin of Bacillus thuringiensis Subsp. Medellin
    • Segura C., Guzman F., Patarroyo M.E., and Orduz S. Activation Pattern and Toxicity of the Cry11Bb1 toxin of Bacillus thuringiensis Subsp. Medellin. J Invertebr Pathol 76 (2000) 56-62
    • (2000) J Invertebr Pathol , vol.76 , pp. 56-62
    • Segura, C.1    Guzman, F.2    Patarroyo, M.E.3    Orduz, S.4
  • 110
    • 0037181168 scopus 로고    scopus 로고
    • Cadherin-like receptor binding facilitates proteolytic cleavage of helix K-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin
    • Gomez I., Sanchez J., Miranda R., Bravo A., and Soberon M. Cadherin-like receptor binding facilitates proteolytic cleavage of helix K-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin. FEBS Lett 513 (2002) 242-246
    • (2002) FEBS Lett , vol.513 , pp. 242-246
    • Gomez, I.1    Sanchez, J.2    Miranda, R.3    Bravo, A.4    Soberon, M.5
  • 111
    • 0036489165 scopus 로고    scopus 로고
    • Characterization of a novel insect digestive DNase with a highly alkaline pH optimum
    • Schernthaner J.P., Milne R.E., and Kaplan H. Characterization of a novel insect digestive DNase with a highly alkaline pH optimum. Insect Biochem Mol Biol 32 (2002) 255-263
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 255-263
    • Schernthaner, J.P.1    Milne, R.E.2    Kaplan, H.3
  • 112
    • 0027328983 scopus 로고
    • Non-enzymatic glycosylation of Lepidopteran-active Bacillus thuringiensis protein crystals
    • Bhattacharya M., Plantz B.A., Swanson-Kobler J.D., and Nickerson K.W. Non-enzymatic glycosylation of Lepidopteran-active Bacillus thuringiensis protein crystals. Appl Environ Microbiol 59 8 (1993) 2666-2672
    • (1993) Appl Environ Microbiol , vol.59 , Issue.8 , pp. 2666-2672
    • Bhattacharya, M.1    Plantz, B.A.2    Swanson-Kobler, J.D.3    Nickerson, K.W.4
  • 113
    • 0030114708 scopus 로고    scopus 로고
    • Digestion of δ-endotoxin by gut proteases may explain reduced sensitivity of advanced instar larvae of Spodoptera littoralis to CryIC
    • Keller M., Sneh B., Strizhov N., Prudovsky E., Regev A., Koncz C., et al. Digestion of δ-endotoxin by gut proteases may explain reduced sensitivity of advanced instar larvae of Spodoptera littoralis to CryIC. Insect Biochem Mol Biol 26 (1996) 365-373
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 365-373
    • Keller, M.1    Sneh, B.2    Strizhov, N.3    Prudovsky, E.4    Regev, A.5    Koncz, C.6
  • 114
    • 0002015602 scopus 로고    scopus 로고
    • Protease interactions with Bacillus thuringiensis insecticidal toxins
    • Oppert B. Protease interactions with Bacillus thuringiensis insecticidal toxins. Arch Insect Biochem Physiol 42 (1999) 1-12
    • (1999) Arch Insect Biochem Physiol , vol.42 , pp. 1-12
    • Oppert, B.1
  • 116
    • 0345466593 scopus 로고    scopus 로고
    • Comparison of midgut proteases in Bacillus thuringiensis susceptible and resistant European corn borer, Ostrinia nubilalis (Lepidoptera: Pyralidae)
    • Huang F., Zhu K.Y., Buschman L.L., Higgins R.A., and Oppert B. Comparison of midgut proteases in Bacillus thuringiensis susceptible and resistant European corn borer, Ostrinia nubilalis (Lepidoptera: Pyralidae). Pest Biochem Physiol 65 (1999) 132-139
    • (1999) Pest Biochem Physiol , vol.65 , pp. 132-139
    • Huang, F.1    Zhu, K.Y.2    Buschman, L.L.3    Higgins, R.A.4    Oppert, B.5
  • 117
    • 0030831169 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the insecticidal fragment of CryV
    • Sekar V., Held B., Tippett J., Amirhusin B., Robeff P., Wang K., et al. Biochemical and molecular characterization of the insecticidal fragment of CryV. Appl Environ Microbiol 63 7 (1997) 2798-2801
    • (1997) Appl Environ Microbiol , vol.63 , Issue.7 , pp. 2798-2801
    • Sekar, V.1    Held, B.2    Tippett, J.3    Amirhusin, B.4    Robeff, P.5    Wang, K.6
  • 118
    • 0034068898 scopus 로고    scopus 로고
    • Genetic and biochemical approach for characterization of resistance to Bacillus thuringiensis toxin Cry1Ac in a field population of the diamondback moth, Plutella xylostella
    • Sayyed A.H., Haward R., Herrero S., Ferre J., and Wright D.J. Genetic and biochemical approach for characterization of resistance to Bacillus thuringiensis toxin Cry1Ac in a field population of the diamondback moth, Plutella xylostella. Appl Environ Microbiol 66 (2000) 1509-1516
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1509-1516
    • Sayyed, A.H.1    Haward, R.2    Herrero, S.3    Ferre, J.4    Wright, D.J.5
  • 119
    • 0034040939 scopus 로고    scopus 로고
    • Mosquito immune responses and malaria transmission: lessons from insect model systems and implications for vertebrate innate immunity and vaccine development
    • Barillas-Mury C., Wizel B., and Han Y.S. Mosquito immune responses and malaria transmission: lessons from insect model systems and implications for vertebrate innate immunity and vaccine development. Insect Biochem Mol Biol 30 (2000) 429-442
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 429-442
    • Barillas-Mury, C.1    Wizel, B.2    Han, Y.S.3
  • 120
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • Jiang H., and Kanost M.R. The clip-domain family of serine proteinases in arthropods. Insect Biochem Mol Biol 30 (2000) 95-105
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 121
    • 0034669169 scopus 로고    scopus 로고
    • Molecular interactions between Anopheles stephensi midgut cells and Plasmodium berghei: the time bomb theory of ookinete invasion of mosquitoes
    • Han Y.S., Thompson J., Kafatos F.C., and Barillas-Mury C. Molecular interactions between Anopheles stephensi midgut cells and Plasmodium berghei: the time bomb theory of ookinete invasion of mosquitoes. EMBO J 19 (2000) 6030-6040
    • (2000) EMBO J , vol.19 , pp. 6030-6040
    • Han, Y.S.1    Thompson, J.2    Kafatos, F.C.3    Barillas-Mury, C.4
  • 122
    • 0035313205 scopus 로고    scopus 로고
    • How Bacillus thuringiensis has evolved specific toxins to colonize the insect world
    • de Maagd R.A., Bravo A., and Crickmore N. How Bacillus thuringiensis has evolved specific toxins to colonize the insect world. Trends Genet 17 (2001) 193-199
    • (2001) Trends Genet , vol.17 , pp. 193-199
    • de Maagd, R.A.1    Bravo, A.2    Crickmore, N.3
  • 123
    • 0035292636 scopus 로고    scopus 로고
    • Different mechanisms of resistance to Bacillus thuringiensis toxins in the indianmeal moth
    • Herrero S., Oppert B., and Ferre J. Different mechanisms of resistance to Bacillus thuringiensis toxins in the indianmeal moth. Appl Environ Microbiol 67 (2001) 1085-1089
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1085-1089
    • Herrero, S.1    Oppert, B.2    Ferre, J.3
  • 124
    • 0036009754 scopus 로고    scopus 로고
    • Changes in protease activity and Cry3Aa toxin binding in the Colorado potato beetle: implications for insect resistance to Bacillus thuringiensis toxins
    • Loseva O., Ibrahim M., Candas M., Noah Koller C., Bauer L.S., and Bulla Jr. L.A. Changes in protease activity and Cry3Aa toxin binding in the Colorado potato beetle: implications for insect resistance to Bacillus thuringiensis toxins. Insect Biochem Mol Biol 32 (2002) 567-577
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 567-577
    • Loseva, O.1    Ibrahim, M.2    Candas, M.3    Noah Koller, C.4    Bauer, L.S.5    Bulla Jr., L.A.6
  • 125
    • 0036006844 scopus 로고    scopus 로고
    • Biochemistry and genetics of insect resistance to Bacillus thuringiensis
    • Ferre J., and Van Rie J. Biochemistry and genetics of insect resistance to Bacillus thuringiensis. Annu Rev Entomol 47 (2002) 501-533
    • (2002) Annu Rev Entomol , vol.47 , pp. 501-533
    • Ferre, J.1    Van Rie, J.2
  • 126
    • 0036840198 scopus 로고    scopus 로고
    • Altered glycosylation of 63- and 68-kilodalton microvillar proteins in Heliothis virescens correlates with reduced Cry1 toxin binding, decreased pore formation, and increased resistance to Bacillus thuringiensis Cry1 toxins
    • Jurat-Fuentes J.L., Gould F.L., and Adang M.J. Altered glycosylation of 63- and 68-kilodalton microvillar proteins in Heliothis virescens correlates with reduced Cry1 toxin binding, decreased pore formation, and increased resistance to Bacillus thuringiensis Cry1 toxins. Appl Environ Microbiol 68 (2002) 5711-5717
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5711-5717
    • Jurat-Fuentes, J.L.1    Gould, F.L.2    Adang, M.J.3
  • 127
    • 0037248290 scopus 로고    scopus 로고
    • Characterization and comparison of midgut proteases of Bacillus thuringiensis susceptible and resistant diamondback moth (Plutellidae: Lepidoptera)
    • Mohan M., and Gujar G.T. Characterization and comparison of midgut proteases of Bacillus thuringiensis susceptible and resistant diamondback moth (Plutellidae: Lepidoptera). J Invertebr Pathol 82 (2003) 1-11
    • (2003) J Invertebr Pathol , vol.82 , pp. 1-11
    • Mohan, M.1    Gujar, G.T.2
  • 128
    • 1642534361 scopus 로고    scopus 로고
    • Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say)
    • Rausell C., Garcia-Robles I., Sanchez J., Munoz-Garaya C., Martinez-Ramirez A.C., Real M.D., et al. Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say). Biochim et Biophys Acta 1660 (2004) 99-105
    • (2004) Biochim et Biophys Acta , vol.1660 , pp. 99-105
    • Rausell, C.1    Garcia-Robles, I.2    Sanchez, J.3    Munoz-Garaya, C.4    Martinez-Ramirez, A.C.5    Real, M.D.6
  • 129
    • 16544393124 scopus 로고    scopus 로고
    • The Bacillus thuringiensis Cry1Aa toxin: effects of trypsin and chymotrypsin site mutations on toxicity and stability
    • Bah A., van Frankenhuyzen K., Brousseau R., and Masson L. The Bacillus thuringiensis Cry1Aa toxin: effects of trypsin and chymotrypsin site mutations on toxicity and stability. J Invertebr Pathol 85 (2004) 120-127
    • (2004) J Invertebr Pathol , vol.85 , pp. 120-127
    • Bah, A.1    van Frankenhuyzen, K.2    Brousseau, R.3    Masson, L.4
  • 130
    • 21244432421 scopus 로고    scopus 로고
    • Many roads to resistance: how invertebrates adapt to Bt toxins
    • Griffitts J.S., and Aroian R.V. Many roads to resistance: how invertebrates adapt to Bt toxins. BioEssays 27 (2005) 614-624
    • (2005) BioEssays , vol.27 , pp. 614-624
    • Griffitts, J.S.1    Aroian, R.V.2
  • 131
    • 84966146220 scopus 로고
    • New strain of Bacillus thuringiensis with activity against coleopteran insects
    • Harnstadt C., Soares G.C., Wilcox E.R., and Edwards D.L. New strain of Bacillus thuringiensis with activity against coleopteran insects. Bio/Technol 4 (1986) 305-308
    • (1986) Bio/Technol , vol.4 , pp. 305-308
    • Harnstadt, C.1    Soares, G.C.2    Wilcox, E.R.3    Edwards, D.L.4
  • 132
    • 34047257847 scopus 로고    scopus 로고
    • Lamontagne E. Caractérisation de nouvelles souches de Bacillus thuringiensis d'intérêt pour la production de biopesticides et d'enzymes par fermentation de boues d'épuration municipales. Master's thesis, Institut Nationale de la Recherche Scientifique-Eau, Terre et Environnement, Université du Québec, Canada; 2004. p. 112.
  • 133
    • 0023914794 scopus 로고
    • The mosquito larvicidal activity of 130 kDa delta-endotoxin of Bacillus thuringiensis var israelensis residues in the 72 kDa amino terminal fragment
    • Paointara M., Angusthasombat C., and Panyim S. The mosquito larvicidal activity of 130 kDa delta-endotoxin of Bacillus thuringiensis var israelensis residues in the 72 kDa amino terminal fragment. Biochem Biophys Res Commun 153 (1988) 294-300
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 294-300
    • Paointara, M.1    Angusthasombat, C.2    Panyim, S.3
  • 134
    • 0023956418 scopus 로고
    • Cloning and expression of two homologous genes of Bacillus thuringiensis subsp. israelensis which encode 130-kilodalton mosquitocidal proteins
    • Ward S.E., and Ellar D.J. Cloning and expression of two homologous genes of Bacillus thuringiensis subsp. israelensis which encode 130-kilodalton mosquitocidal proteins. J Bacteriol 70 (1988) 727-735
    • (1988) J Bacteriol , vol.70 , pp. 727-735
    • Ward, S.E.1    Ellar, D.J.2
  • 135
    • 0026890951 scopus 로고
    • Comparison of Bacillus thuringiensis subsp. israelensis Cry IVA and Cry IVB cloned toxins reveals synergism in vivo
    • Angsuthanasombat C., Crickmore N., and Ellar D.J. Comparison of Bacillus thuringiensis subsp. israelensis Cry IVA and Cry IVB cloned toxins reveals synergism in vivo. FEMS Microbiol Lett 94 (1988) 63-68
    • (1988) FEMS Microbiol Lett , vol.94 , pp. 63-68
    • Angsuthanasombat, C.1    Crickmore, N.2    Ellar, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.