메뉴 건너뛰기




Volumn 180, Issue 17, 1998, Pages 4435-4441

Chitinolytic activity in Chromobacterium violaceum: Substrate analysis and regulation by quorum sensing

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CELL WALL SKELETON; CHITIN; CHITINASE; HOMOSERINE; N ACETYLGLUCOSAMINE; SIGNAL PEPTIDE;

EID: 0031752045     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.17.4435-4441.1998     Document Type: Article
Times cited : (214)

References (60)
  • 1
    • 0026315624 scopus 로고
    • Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii
    • Bassler, B. L., C. Yu, Y. C. Lee, and S. Roseman. 1991. Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266:24276-24286.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24276-24286
    • Bassler, B.L.1    Yu, C.2    Lee, Y.C.3    Roseman, S.4
  • 2
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases A and B from Serratia marcescens
    • Brurberg, M. B., I. F. Nes, and V. G. H. Eijsink. 1996. Comparative studies of chitinases A and B from Serratia marcescens. Microbiology 142:1581-1589.
    • (1996) Microbiology , vol.142 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.H.3
  • 3
    • 0025742889 scopus 로고
    • Cloning and expression of a chitinase gene from Aeromonas hydrophila in Escherichia coli
    • Chen, J. P., F. Nagayama, and M. C. Chang. 1991. Cloning and expression of a chitinase gene from Aeromonas hydrophila in Escherichia coli. Appl. Environ. Microbiol. 57:2426-2428.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2426-2428
    • Chen, J.P.1    Nagayama, F.2    Chang, M.C.3
  • 4
    • 0030809293 scopus 로고    scopus 로고
    • Chitinolytic activity of the acaropathogenic fungi Hirsutella thompsonii and Hirsutella necatrix
    • Chemin, L., A. Gafni, R. Moses-Koch, U. Gerson, and A. Szteinberg. 1997. Chitinolytic activity of the acaropathogenic fungi Hirsutella thompsonii and Hirsutella necatrix. Can. J. Microbiol. 43:440-446.
    • (1997) Can. J. Microbiol. , vol.43 , pp. 440-446
    • Chemin, L.1    Gafni, A.2    Moses-Koch, R.3    Gerson, U.4    Szteinberg, A.5
  • 5
    • 0028989744 scopus 로고
    • Chitinolytic Enterobacter agglomerans antagonistic to fungal plant pathogens
    • Chernin, L., Z. Ismailov, S. Haran, and I. Chet. 1995. Chitinolytic Enterobacter agglomerans antagonistic to fungal plant pathogens. Appl. Environ. Microbiol. 61:1720-1726.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1720-1726
    • Chernin, L.1    Ismailov, Z.2    Haran, S.3    Chet, I.4
  • 6
    • 0031038259 scopus 로고    scopus 로고
    • Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans
    • Chemin, L. S., L. de la Fuenta, V. Sobolev, S. Haran, C. E. Vorgias, A. B. Oppenheim, and I. Chet. 1997. Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans. Appl. Environ. Microbiol. 63:834-839.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 834-839
    • Chemin, L.S.1    De La Fuenta, L.2    Sobolev, V.3    Haran, S.4    Vorgias, C.E.5    Oppenheim, A.B.6    Chet, I.7
  • 7
    • 0028826419 scopus 로고
    • A global regulator of secondary metabolite production in Pseudomonas fluorescens Pf-5
    • Corbell, N., and J. E. Loper. 1995. A global regulator of secondary metabolite production in Pseudomonas fluorescens Pf-5. J. Bacteriol. 177:6230-6236.
    • (1995) J. Bacteriol. , vol.177 , pp. 6230-6236
    • Corbell, N.1    Loper, J.E.2
  • 8
    • 0023663179 scopus 로고
    • Nucleotide sequence of the regulatory locus controlling expression of bacterial genes for bioluminescence
    • Engebrecht, J., and M. Silverman. 1987. Nucleotide sequence of the regulatory locus controlling expression of bacterial genes for bioluminescence. Nucleic Acids Res. 15:10455-10467.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10455-10467
    • Engebrecht, J.1    Silverman, M.2
  • 9
    • 0029818809 scopus 로고    scopus 로고
    • Census and consensus in bacterial ecosystems: The LuxR-LuxI family of quorum-sensing transcriptional regulators
    • Fuqua, C., S. C. Winans, and E. P. Greenberg. 1996. Census and consensus in bacterial ecosystems: the LuxR-LuxI family of quorum-sensing transcriptional regulators. Annu. Rev. Microbiol. 50:727-751.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 727-751
    • Fuqua, C.1    Winans, S.C.2    Greenberg, E.P.3
  • 10
    • 0027957161 scopus 로고
    • Quorum sensing in bacteria: The LuxR-LuxI family of cell-density responsive transcriptional regulators
    • Fuqua, W. C., S. C. Winans, and E. P. Greenberg. 1994. Quorum sensing in bacteria: the LuxR-LuxI family of cell-density responsive transcriptional regulators. J. Bacteriol. 176:269-275.
    • (1994) J. Bacteriol. , vol.176 , pp. 269-275
    • Fuqua, W.C.1    Winans, S.C.2    Greenberg, E.P.3
  • 12
    • 0029770421 scopus 로고    scopus 로고
    • Molecular mechanisms of lytic enzymes involved in the biocontrol activity of Trichoderma harzianum
    • Haran, S., H. Schikler, and I. Chet. 1996. Molecular mechanisms of lytic enzymes involved in the biocontrol activity of Trichoderma harzianum. Microbiology 142:2321-2331.
    • (1996) Microbiology , vol.142 , pp. 2321-2331
    • Haran, S.1    Schikler, H.2    Chet, I.3
  • 13
    • 0029124479 scopus 로고
    • New components of the chitinolytic system of Trichoderma harzianum
    • Haran, S., H. Schikler, A. Oppenheim, and I. Chet. 1995. New components of the chitinolytic system of Trichoderma harzianum. Mycol. Res. 99:441-446.
    • (1995) Mycol. Res. , vol.99 , pp. 441-446
    • Haran, S.1    Schikler, H.2    Oppenheim, A.3    Chet, I.4
  • 15
    • 0014908229 scopus 로고
    • Formation of biologically active substances by rhizosphere bacteria and their effect on plant growth
    • Hussain, A., and V. Vancura. 1970. Formation of biologically active substances by rhizosphere bacteria and their effect on plant growth. Folia Microbiol. 15:468-478.
    • (1970) Folia Microbiol. , vol.15 , pp. 468-478
    • Hussain, A.1    Vancura, V.2
  • 16
    • 0026313858 scopus 로고
    • Evidence that chitinase produced by Aeromonas caviae is involved in the biological control of soil-borne plant pathogens by this bacterium
    • Inbar, J., and I. Chet. 1991. Evidence that chitinase produced by Aeromonas caviae is involved in the biological control of soil-borne plant pathogens by this bacterium. Soil Biol. Biochem. 23:973-978.
    • (1991) Soil Biol. Biochem. , vol.23 , pp. 973-978
    • Inbar, J.1    Chet, I.2
  • 17
    • 0031431260 scopus 로고    scopus 로고
    • Production and purification of a chitinase from Ewingella americana, a recently described pathogen of the mushroom, Agaricus bisporus
    • Inglis, P. W., and J. F. Peberdy. 1997. Production and purification of a chitinase from Ewingella americana, a recently described pathogen of the mushroom, Agaricus bisporus. FEMS Microbiol. Lett. 157:189-194.
    • (1997) FEMS Microbiol. Lett. , vol.157 , pp. 189-194
    • Inglis, P.W.1    Peberdy, J.F.2
  • 18
    • 0023387947 scopus 로고
    • Translocation of Vibrio harveyi N,N′-diacetychitobiase to the outer membrane of Escherichia coli
    • Jannatipour, M., R. W. Soto-Gil, L. C. Childers, and J. W. Zyskind. 1987. Translocation of Vibrio harveyi N,N′-diacetychitobiase to the outer membrane of Escherichia coli. J. Bacteriol. 169:3785-3791.
    • (1987) J. Bacteriol. , vol.169 , pp. 3785-3791
    • Jannatipour, M.1    Soto-Gil, R.W.2    Childers, L.C.3    Zyskind, J.W.4
  • 20
    • 0024041235 scopus 로고
    • Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens
    • Joshi, S., M. Kozlowski, G. Sekaraj, V. N. Iyer, and R. W. Davies. 1988. Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens. J. Bacteriol. 170:2984-2988.
    • (1988) J. Bacteriol. , vol.170 , pp. 2984-2988
    • Joshi, S.1    Kozlowski, M.2    Sekaraj, G.3    Iyer, V.N.4    Davies, R.W.5
  • 21
    • 0030478209 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Characterization of an N,N′-diacetyl-chitobiose transport system
    • Keyhani, N. O., L.-X. Wang, Y. C. Lee, and S. Roseman. 1996. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Characterization of an N,N′-diacetyl-chitobiose transport system. J. Biol. Chem. 271:33409-33413.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33409-33413
    • Keyhani, N.O.1    Wang, L.-X.2    Lee, Y.C.3    Roseman, S.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0003128645 scopus 로고
    • Biological activities of bacteria used in plant pathogen control
    • I. Chet (ed.), Wiley-Liss, Inc., New York, N.Y.
    • Lam, S. T., and T. D. Gaffney. 1993. Biological activities of bacteria used in plant pathogen control, p. 291-320. In I. Chet (ed.), Biotechnology in plant disease control. Wiley-Liss, Inc., New York, N.Y.
    • (1993) Biotechnology in Plant Disease Control , pp. 291-320
    • Lam, S.T.1    Gaffney, T.D.2
  • 24
    • 0029145808 scopus 로고
    • Multiple homologues of LuxR and LuxI control expression of virulence determinants and secondary metabolites through quorum sensing in Pseudomonas aeruginosa PAO1
    • Latin, A., M. K. Winson, M. Foglino, B. W. Bycroft, G. S. A. B. Stewart, A. Lazdunski, and P. Williams. 1995. Multiple homologues of LuxR and LuxI control expression of virulence determinants and secondary metabolites through quorum sensing in Pseudomonas aeruginosa PAO1. Mol. Microbiol. 17:333-343.
    • (1995) Mol. Microbiol. , vol.17 , pp. 333-343
    • Latin, A.1    Winson, M.K.2    Foglino, M.3    Bycroft, B.W.4    Stewart, G.S.A.B.5    Lazdunski, A.6    Williams, P.7
  • 25
    • 0026592642 scopus 로고
    • Global control in Pseudomonas fluorescens mediating antibiotic synthesis and suppression of black root rot of tobacco
    • Laville, J., C. Voisard, C. Keel, M. Maurhofer, G. Defago, and D. Haas. 1992. Global control in Pseudomonas fluorescens mediating antibiotic synthesis and suppression of black root rot of tobacco. Proc. Natl. Acad. Sci. USA 89:1562-1566.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1562-1566
    • Laville, J.1    Voisard, C.2    Keel, C.3    Maurhofer, M.4    Defago, G.5    Haas, D.6
  • 27
    • 0025075165 scopus 로고
    • Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Use of casein in gel wash buffer
    • McGrew, B. R., and D. M. Green. 1990. Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis: use of casein in gel wash buffer. Anal. Biochem. 189: 68-74.
    • (1990) Anal. Biochem. , vol.189 , pp. 68-74
    • McGrew, B.R.1    Green, D.M.2
  • 28
    • 0028566948 scopus 로고
    • Genetics of bacterial bioluminescence
    • Meighen, E. A. 1994. Genetics of bacterial bioluminescence. Annu. Rev. Genet. 28:117-139.
    • (1994) Annu. Rev. Genet. , vol.28 , pp. 117-139
    • Meighen, E.A.1
  • 29
    • 0014540906 scopus 로고
    • The chitinase of Serratia marcescens
    • Monreal, J., and E. T. Rees. 1969. The chitinase of Serratia marcescens. Can. J. Microbiol. 15:689-696.
    • (1969) Can. J. Microbiol. , vol.15 , pp. 689-696
    • Monreal, J.1    Rees, E.T.2
  • 30
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., N. Arold, D. Taube, and W. Ehrhardt. 1988. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9:255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 31
    • 0001009925 scopus 로고
    • Effect of lactose, ethanol and cycloheximide on the translocation pattern of radioactive compounds and sclerotium formation in Sclerotium rolfsii
    • Okon, Y., I. Chet, and Y. Henis. 1973. Effect of lactose, ethanol and cycloheximide on the translocation pattern of radioactive compounds and sclerotium formation in Sclerotium rolfsii. J. Gen. Microbiol. 74:251-255.
    • (1973) J. Gen. Microbiol. , vol.74 , pp. 251-255
    • Okon, Y.1    Chet, I.2    Henis, Y.3
  • 32
    • 0027299747 scopus 로고
    • Expression of Pseudomonas aeruginosa virulence genes requires cell-to-cell communication
    • Passador, L., J. M. Cook, M. J. Gambello, L. Rust, and B. H. Iglewski. 1993. Expression of Pseudomonas aeruginosa virulence genes requires cell-to-cell communication. Science 260:1127-1130.
    • (1993) Science , vol.260 , pp. 1127-1130
    • Passador, L.1    Cook, J.M.2    Gambello, M.J.3    Rust, L.4    Iglewski, B.H.5
  • 33
    • 0011386124 scopus 로고
    • Phylogenetic relationships of chitinases
    • R. A. A. Muzzarelli (ed.), European Chitin Society, Ancona, Italy
    • Perrakis, A., K. S. Wilson, I. Chet, A. B. Oppenheim, and C. E. Vorgias. 1993. Phylogenetic relationships of chitinases, p. 217-232. In R. A. A. Muzzarelli (ed.), Chitin enzymology. European Chitin Society, Ancona, Italy.
    • (1993) Chitin Enzymology , pp. 217-232
    • Perrakis, A.1    Wilson, K.S.2    Chet, I.3    Oppenheim, A.B.4    Vorgias, C.E.5
  • 34
    • 0029962341 scopus 로고    scopus 로고
    • Phenazine antibiotic production in Pseudomonas aureofaciens: Role in rhizosphere ecology and pathogen suppression
    • Pierson III, L. S., and E. A. Pierson. 1996. Phenazine antibiotic production in Pseudomonas aureofaciens: role in rhizosphere ecology and pathogen suppression. FEMS Microbiol. Lett. 136:101-108.
    • (1996) FEMS Microbiol. Lett. , vol.136 , pp. 101-108
    • Pierson III, L.S.1    Pierson, E.A.2
  • 35
    • 0027252653 scopus 로고
    • A small diffusible signal molecule is responsible for the global control of virulence and exoenzyme production in the plant pathogen Erwinia carotovora
    • Pirhonen, M., D. Flego, R. Heikinheimo, and E. T. Palva. 1993. A small diffusible signal molecule is responsible for the global control of virulence and exoenzyme production in the plant pathogen Erwinia carotovora. EMBO J. 12:2467-2476.
    • (1993) EMBO J. , vol.12 , pp. 2467-2476
    • Pirhonen, M.1    Flego, D.2    Heikinheimo, R.3    Palva, E.T.4
  • 36
    • 0030770243 scopus 로고    scopus 로고
    • Chitinolytic activity of an endophytic strain of Bacillus cereus
    • Pleban, S., L. Chernin, and I. Chet. 1997. Chitinolytic activity of an endophytic strain of Bacillus cereus. Lett. Appl. Microbiol. 25:284-288.
    • (1997) Lett. Appl. Microbiol. , vol.25 , pp. 284-288
    • Pleban, S.1    Chernin, L.2    Chet, I.3
  • 37
    • 0030919474 scopus 로고    scopus 로고
    • The global activator GacA of Pseudomonas aeruginosa PAO positively controls the production of the autoinducer N-butyryl-homoserine lactone and the formation of the virulence factors pyocyanin, cyanide, and lipase
    • Reimmann, C., M. Beyeler, A. Latifi, H. Winteler, M. Foglino, A. Lazdunski, and D. Haas. 1997. The global activator GacA of Pseudomonas aeruginosa PAO positively controls the production of the autoinducer N-butyryl-homoserine lactone and the formation of the virulence factors pyocyanin, cyanide, and lipase. Mol. Microbiol. 24:309-319.
    • (1997) Mol. Microbiol. , vol.24 , pp. 309-319
    • Reimmann, C.1    Beyeler, M.2    Latifi, A.3    Winteler, H.4    Foglino, M.5    Lazdunski, A.6    Haas, D.7
  • 38
    • 0028003862 scopus 로고
    • Genetic evidence that the gacA gene encodes the cognate response regulator for the lemA sensor in Pseudomonas syringae
    • Rich, J. J., T. G. Kinscherf, T. Kitten, and D. K. Willis. 1994. Genetic evidence that the gacA gene encodes the cognate response regulator for the lemA sensor in Pseudomonas syringae. J. Bacteriol. 176:7468-7475.
    • (1994) J. Bacteriol. , vol.176 , pp. 7468-7475
    • Rich, J.J.1    Kinscherf, T.G.2    Kitten, T.3    Willis, D.K.4
  • 39
    • 0020392369 scopus 로고
    • Serratia marcescens chitinase: One step purification and use for the determination of chitin
    • Roberts, R. L., and E. Cabib. 1982. Serratia marcescens chitinase: one step purification and use for the determination of chitin. Ann. Chem. 127:402-412.
    • (1982) Ann. Chem. , vol.127 , pp. 402-412
    • Roberts, R.L.1    Cabib, E.2
  • 40
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts, W. K., and C. P. Selitrennikoff. 1988. Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol. 134:169-176.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 41
    • 0020891975 scopus 로고
    • The determination of soil chitinase activity, conditions for assay and ecological studies
    • Rodriguez-Kabana, R., G. Godoy, G. Morgan-Jones, and R. A. Shelby. 1983. The determination of soil chitinase activity, conditions for assay and ecological studies. Plant Soil 75:95-106.
    • (1983) Plant Soil , vol.75 , pp. 95-106
    • Rodriguez-Kabana, R.1    Godoy, G.2    Morgan-Jones, G.3    Shelby, R.A.4
  • 43
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: Their involvement in morphogenesis and host-parasite interaction
    • Sahai, A. S., and M. S. Manocha. 1993. Chitinases of fungi and plants: their involvement in morphogenesis and host-parasite interaction. FEMS Microbiol. Rev. 11:317-338.
    • (1993) FEMS Microbiol. Rev. , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 44
    • 48749145579 scopus 로고
    • Chitinase is an inducible enzyme in Beauveria bassiana
    • Smith, R. J., and E. A. Grula. 1983. Chitinase is an inducible enzyme in Beauveria bassiana. J. Invest. Pathol. 42:319-326.
    • (1983) J. Invest. Pathol. , vol.42 , pp. 319-326
    • Smith, R.J.1    Grula, E.A.2
  • 45
    • 0020508078 scopus 로고
    • Utilization of chitin as sole carbon and nitrogen source by Chromobacterium violaceum
    • Streichsbier, F. 1983. Utilization of chitin as sole carbon and nitrogen source by Chromobacterium violaceum. FEMS Microbiol. Lett. 19:129-132.
    • (1983) FEMS Microbiol. Lett. , vol.19 , pp. 129-132
    • Streichsbier, F.1
  • 46
    • 0030981929 scopus 로고    scopus 로고
    • Chitin degradation proteins produced by the marine bacterium Vibrio harveyi growing on different forms of chitin
    • Svitil, A. L., S. M. Ni Chadhain, J. A. Moore, and D. L. Kirchman. 1997. Chitin degradation proteins produced by the marine bacterium Vibrio harveyi growing on different forms of chitin. Appl. Environ. Microbiol. 63:408-413.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 408-413
    • Svitil, A.L.1    Ni Chadhain, S.M.2    Moore, J.A.3    Kirchman, D.L.4
  • 48
    • 0029942280 scopus 로고    scopus 로고
    • Quorum sensing: A population-density component in the determination of bacterial phenotype
    • Swift, S., J. P. Throup, G. P. C. Salmond, P. Williams, and G. S. A. B. Stewart. 1996. Quorum sensing: a population-density component in the determination of bacterial phenotype. Trends Biochem. Sci. 21:214-219.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 214-219
    • Swift, S.1    Throup, J.P.2    Salmond, G.P.C.3    Williams, P.4    Stewart, G.S.A.B.5
  • 49
    • 0030743041 scopus 로고    scopus 로고
    • Use of a promoterless lacZ gene insertion to investigate chitinase gene expression in the marine bacterium Pseudoalteromonas sp. strain S9
    • Techkarnjanaruk, S., S. Pongpattanakitshole, and A. E. Goodman. 1997. Use of a promoterless lacZ gene insertion to investigate chitinase gene expression in the marine bacterium Pseudoalteromonas sp. strain S9. Appl. Environ. Microbiol. 63:2989-2996.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2989-2996
    • Techkarnjanaruk, S.1    Pongpattanakitshole, S.2    Goodman, A.E.3
  • 52
    • 0027401151 scopus 로고
    • Detection and quantification of N-acetyl-β-D-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels
    • Tronsmo, A., and G. Harman. 1993. Detection and quantification of N-acetyl-β-D-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels. Anal. Biochem. 208:74-79.
    • (1993) Anal. Biochem. , vol.208 , pp. 74-79
    • Tronsmo, A.1    Harman, G.2
  • 54
    • 0030900026 scopus 로고    scopus 로고
    • Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium
    • Wang, S.-L., and W.-T. Chang. 1997. Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium. Appl. Environ. Microbiol. 63:380-386.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 380-386
    • Wang, S.-L.1    Chang, W.-T.2
  • 59
    • 0030735452 scopus 로고    scopus 로고
    • N-Acyl-homoserine lactone-mediated regulation of phenazine gene expression by Pseudomonas aureofaciens 30-84 in the wheat rhizosphere
    • Wood, D. W., F. Gong, M. M. Daykin, P. Williams, and L. S. Pierson III. 1997. N-Acyl-homoserine lactone-mediated regulation of phenazine gene expression by Pseudomonas aureofaciens 30-84 in the wheat rhizosphere. J. Bacteriol. 179:7663-7670.
    • (1997) J. Bacteriol. , vol.179 , pp. 7663-7670
    • Wood, D.W.1    Gong, F.2    Daykin, M.M.3    Williams, P.4    Pierson III, L.S.5
  • 60
    • 0022516180 scopus 로고
    • Chitinase determinants of Vibrio vulnificus: Gene cloning and applications of a chitinase probe
    • Wortman, A. T., C. C. Somerville, and R. R. Colwell. 1986. Chitinase determinants of Vibrio vulnificus: gene cloning and applications of a chitinase probe. Appl. Environ. Microbiol. 52:142-145.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 142-145
    • Wortman, A.T.1    Somerville, C.C.2    Colwell, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.