메뉴 건너뛰기




Volumn 50, Issue 3, 2012, Pages 459-468

Molecular screening of Streptomyces isolates for antifungal activity and family 19 chitinase enzymes

Author keywords

16S rRNA; family 19 chitinase; phytopathogenic fungi; Streptomyces

Indexed keywords

AGAR; ANTIFUNGAL AGENT; BACTERIAL DNA; CHITIN; CHITINASE; PRIMER DNA; RIBOSOME DNA; RNA 16S;

EID: 84863305113     PISSN: 12258873     EISSN: 19763794     Source Type: Journal    
DOI: 10.1007/s12275-012-2095-4     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 84983185340 scopus 로고    scopus 로고
    • Molecular genetic fingerprint of some Streptomyces isolated from Riyadh city
    • Al-Kahtani, M., AI-Khalil, A., AI-Kadeeb, S., and Hassan, H. Z. 2008. Molecular genetic fingerprint of some Streptomyces isolated from Riyadh city. Saudi J. Biological Sci. 15, 243-251.
    • (2008) Saudi J. Biological Sci. , vol.15 , pp. 243-251
    • Al-Kahtani, M.1    Ai-Khalil, A.2    Ai-Kadeeb, S.3    Hassan, H.Z.4
  • 2
    • 0027323001 scopus 로고
    • Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases
    • Blaak, H., Schnellmann, J., Walter, S., Henrissat, B., and Schrempf, H. 1993. Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases. Eur. J. Biochem. 214, 659-669.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 659-669
    • Blaak, H.1    Schnellmann, J.2    Walter, S.3    Henrissat, B.4    Schrempf, H.5
  • 3
    • 22844452898 scopus 로고    scopus 로고
    • Broadspectrim, a novel antibacterial from Streptomyces sp
    • Bonjar, S., Fooladi, M. H., Mahdavi, M. J., and Shahghasi, A. 2004. Broadspectrim, a novel antibacterial from Streptomyces sp. Biotechnol. 3, 126-130.
    • (2004) Biotechnol , vol.3 , pp. 126-130
    • Bonjar, S.1    Fooladi, M.H.2    Mahdavi, M.J.3    Shahghasi, A.4
  • 4
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G. and Henrissat, B. 1995. Structures and mechanisms of glycosyl hydrolases. Structure3, 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 7
    • 34848877778 scopus 로고    scopus 로고
    • Evidences of biological control capacities of Streptomyces spp. against Sclerotium rolfsii responsible for damping-off disease in sugar beet (Beta vulgaris L.)
    • Errakhi, R., Bouteau, F., Lebrihi, A., and Barakate, M. 2010. Evidences of biological control capacities of Streptomyces spp. against Sclerotium rolfsii responsible for damping-off disease in sugar beet (Beta vulgaris L.). World J. Microbiol. Biotechnol. 23, 1503-1509.
    • (2010) World J. Microbiol. Biotechnol. , vol.23 , pp. 1503-1509
    • Errakhi, R.1    Bouteau, F.2    Lebrihi, A.3    Barakate, M.4
  • 8
    • 0027168279 scopus 로고
    • Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans
    • Fujii, T. and Miyashita, K. 1993. Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans. J. Gen. Microbiol. 139, 677-686.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 677-686
    • Fujii, T.1    Miyashita, K.2
  • 9
    • 0028113585 scopus 로고
    • Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme
    • Heitz, T., Segond, S., Kaumann, S., Georoy, P., Prasad, V., Brunner, F., Fritig, B., and Legrand, M. 1994. Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme. Mol. Gen. Genet. 245, 246-254.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 246-254
    • Heitz, T.1    Segond, S.2    Kaumann, S.3    Georoy, P.4    Prasad, V.5    Brunner, F.6    Fritig, B.7    Legrand, M.8
  • 10
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 11
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293, 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 12
    • 12144263461 scopus 로고    scopus 로고
    • Enrichment of chitinolytic microorganisms: isolation and characterization of a chitinase exhibiting antifungal activity against phytopathogenic fungi from a novel Streptomyces strain
    • Hoster, F., Schmitz, J. E., and Daniel, R. 2005. Enrichment of chitinolytic microorganisms: isolation and characterization of a chitinase exhibiting antifungal activity against phytopathogenic fungi from a novel Streptomyces strain. Appl. Microbiol. Biotechnol. 66, 434-442.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 434-442
    • Hoster, F.1    Schmitz, J.E.2    Daniel, R.3
  • 13
    • 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., Fukada, H., Mitsutomi, M., Watanabe, T., and Itoh, Y. 2002. 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, 1084-1092.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1084-1092
    • Itoh, Y.1    Kawase, T.2    Nikaidou, N.3    Fukada, H.4    Mitsutomi, M.5    Watanabe, T.6    Itoh, Y.7
  • 17
    • 52549097575 scopus 로고    scopus 로고
    • Effect of chitin sources on production of chitinase and chitosanase by Streptomyces griseus HUT 6037
    • Kim, K. and Ji, H.-S. 2001. Effect of chitin sources on production of chitinase and chitosanase by Streptomyces griseus HUT 6037. Biotechnol. Bioprocess Eng. 6, 18-24.
    • (2001) Biotechnol. Bioprocess Eng. , vol.6 , pp. 18-24
    • Kim, K.1    Ji, H.-S.2
  • 18
    • 0019296687 scopus 로고
    • A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences
    • Kimura, M. 1980. A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences. J. Mol. Evol. 16, 111-120.
    • (1980) J. Mol. Evol. , vol.16 , pp. 111-120
    • Kimura, M.1
  • 19
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with antifungal properties
    • Leah, R., Tommerup, H., Svendsen, I., and Mundy, J. 1991. Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J. Biol. Chem. 266, 1564-1573.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 21
    • 85004678184 scopus 로고
    • Nucleotide sequence and analysis of a gene (chiA) for chitinase from Streptomyces lividans 66
    • Miyashita, K. and Fujii, T. 1993. Nucleotide sequence and analysis of a gene (chiA) for chitinase from Streptomyces lividans 66. Biosci. Biotechnol. Biochem. 57, 1691-1698.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1691-1698
    • Miyashita, K.1    Fujii, T.2
  • 22
    • 0031041984 scopus 로고    scopus 로고
    • Nucleotide sequence and expression of a gene (chiB) for a chitinase from Streptomyces lividans
    • Miyashita, K., Fujii, T., Watanabe, W., and Ueno, H. 1997. Nucleotide sequence and expression of a gene (chiB) for a chitinase from Streptomyces lividans. J. Ferment. Bioeng. 83, 26-31.
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 26-31
    • Miyashita, K.1    Fujii, T.2    Watanabe, W.3    Ueno, H.4
  • 23
    • 0025834867 scopus 로고
    • Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66
    • Miyashita, K., Fujii, T., and Sawada, Y. 1991. Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66. J. Gen. Microbiol. 137, 2065-2072.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2065-2072
    • Miyashita, K.1    Fujii, T.2    Sawada, Y.3
  • 24
    • 70350144778 scopus 로고    scopus 로고
    • Chitinase production by Streptomyces sp. Anu 6277
    • Narayana, K. J. P. and Vijayalakshmi, M. 2009. Chitinase production by Streptomyces sp. Anu 6277. Braz. J. Microbiol. 40, 725-733.
    • (2009) Braz. J. Microbiol. , vol.40 , pp. 725-733
    • Narayana K.J.P.Vijayalakshmi, M.1
  • 25
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037
    • Ohno, T., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M., and Watanabe, T. 1996. A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. J. Bacteriol. 178, 5065-5070.
    • (1996) J. Bacteriol. , vol.178 , pp. 5065-5070
    • Ohno, T.1    Armand, S.2    Hata, T.3    Nikaidou, N.4    Henrissat, B.5    Mitsutomi, M.6    Watanabe, T.7
  • 26
    • 0022462534 scopus 로고
    • Philosophy of new drug discovery
    • Omura, S. 1986. Philosophy of new drug discovery. Microbiol. Rev. 50, 259-279.
    • (1986) Microbiol. Rev. , vol.50 , pp. 259-279
    • Omura, S.1
  • 27
    • 0001831324 scopus 로고
    • The role of chitinase of Serratia marcescens in biocontrol of Sclerotium rolfsii
    • Ordentlich, A., Elad, Y., and Chet, I. 1988. The role of chitinase of Serratia marcescens in biocontrol of Sclerotium rolfsii. Phytopathology787, 84-88.
    • (1988) Phytopathology , vol.787 , pp. 84-88
    • Ordentlich, A.1    Elad, Y.2    Chet, I.3
  • 28
    • 33644748414 scopus 로고    scopus 로고
    • Rapid detection and high-resolution discrimination of the genus Streptomyces based on 16S rRNA spacer region and denaturing gradient gel electrophoresis
    • Park, H. S., John, J., and Kilbane, I. I. 2006. Rapid detection and high-resolution discrimination of the genus Streptomyces based on 16S rRNA spacer region and denaturing gradient gel electrophoresis. J. Ind. Microbiol. Biotechnol. 33, 289-297.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 289-297
    • Park, H.S.1    John, J.2    Kilbane, I.I.3
  • 30
    • 0023901367 scopus 로고
    • Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli
    • Robbins, P. W., Albright, C., and Benfield, B. 1988. Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J. Biol. Chem. 263, 443-447.
    • (1988) J. Biol. Chem. , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 31
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • Robbins, P. W., Oberbye, K., Albright, C., Benfield, B., and Pero, J. 1992. Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene111, 69-76.
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Oberbye, K.2    Albright, C.3    Benfield, B.4    Pero, J.5
  • 32
    • 0023052559 scopus 로고
    • Isolation and partial characterization of two antifungal proteins from barley
    • Roberts, W. K. and Selitrennikoff, C. P. 1986. Isolation and partial characterization of two antifungal proteins from barley. Biochim. Biophys. Acta880, 161-170.
    • (1986) Biochim. Biophys. Acta , vol.880 , pp. 161-170
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 33
    • 0032454787 scopus 로고    scopus 로고
    • glkA is involved in glucose repression of chitinase production in Streptomyces lividans
    • Saito, A., Fujii, T., Yoneyama, T., and Miyashita, K. 1998. glkA is involved in glucose repression of chitinase production in Streptomyces lividans. J. Bacteriol. 180, 2911-2914.
    • (1998) J. Bacteriol. , vol.180 , pp. 2911-2914
    • Saito, A.1    Fujii, T.2    Yoneyama, T.3    Miyashita, K.4
  • 34
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou, N. and Nei, M. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 36
    • 49749139790 scopus 로고    scopus 로고
    • Optimization of cultural conditions for production of chitinase by Bacillus laterosporous MML2270 isolated from rice rhizosphere soil
    • Shanmugaiah, V., Mathivanan, N., Balasubramanian, N., and Manoharan, P. T. 2008. Optimization of cultural conditions for production of chitinase by Bacillus laterosporous MML2270 isolated from rice rhizosphere soil. Afr. J. Biotechnol. 7, 2562-2568.
    • (2008) Afr. J. Biotechnol. , vol.7 , pp. 2562-2568
    • Shanmugaiah, V.1    Mathivanan, N.2    Balasubramanian, N.3    Manoharan, P.T.4
  • 37
    • 0001023407 scopus 로고
    • Methods for characterization of Streptomyces species
    • Shirling, E. B. and Gottlieb, D. 1966. Methods for characterization of Streptomyces species. Inst. J. Syst. Bacteriol. 16, 313-340.
    • (1966) Inst. J. Syst. Bacteriol. , vol.16 , pp. 313-340
    • Shirling, E.B.1    Gottlieb, D.2
  • 38
    • 0031768883 scopus 로고    scopus 로고
    • Utilization of prawn waste for chitinase production by the marine fungus Beauveria bassiana by solid state fermentation
    • Suresh, P. V. and Chandrasekaran, M. 1998. Utilization of prawn waste for chitinase production by the marine fungus Beauveria bassiana by solid state fermentation. World J. Microbiol. Biotechnol. 14, 655-660.
    • (1998) World J. Microbiol. Biotechnol. , vol.14 , pp. 655-660
    • Suresh, P.V.1    Chandrasekaran, M.2
  • 39
    • 6944250221 scopus 로고    scopus 로고
    • PCR cloning and heterologous expression of chitinase gene of endophytic Streptomyces aureofaciens CMUAc130
    • Taechowisan, T., Peberdy, F. P., and Lumyong, S. 2004. PCR cloning and heterologous expression of chitinase gene of endophytic Streptomyces aureofaciens CMUAc130. J. Gen. Appl. Microbiol. 50, 177-182.
    • (2004) J. Gen. Appl. Microbiol. , vol.50 , pp. 177-182
    • Taechowisan, T.1    Peberdy, F.P.2    Lumyong, S.3
  • 40
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. 1997. The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 41
    • 0031774327 scopus 로고    scopus 로고
    • Simple and efficient protocol for isolation of high molecular weight DNA from Streptomyces aureofaciens
    • Tripathi, G. and Rawal, S. K. 1998. Simple and efficient protocol for isolation of high molecular weight DNA from Streptomyces aureofaciens. Biotechnol. Tech. 12, 629-631.
    • (1998) Biotechnol. Tech. , vol.12 , pp. 629-631
    • Tripathi, G.1    Rawal, S.K.2
  • 42
    • 0027522209 scopus 로고
    • Cloning and sequence analysis of the gene encoding a thermostable chitinase from Streptomyces thermoviolaceus OPC-520
    • Tsujibo, H., Endo, H., Minoura, K., Miyamoto, K., and Inamori, Y. 1993. Cloning and sequence analysis of the gene encoding a thermostable chitinase from Streptomyces thermoviolaceus OPC-520. Gene134, 113-117.
    • (1993) Gene , vol.134 , pp. 113-117
    • Tsujibo, H.1    Endo, H.2    Minoura, K.3    Miyamoto, K.4    Inamori, Y.5
  • 44
    • 0024955069 scopus 로고
    • Chitinase production by Myrothecium verrucaria and its significant for fungal mycelia degradation
    • Vyas, P. and Deshpande, M. V. 1989. Chitinase production by Myrothecium verrucaria and its significant for fungal mycelia degradation. J. Gen. Appl. Microbiol. 35, 343-350.
    • (1989) J. Gen. Appl. Microbiol. , vol.35 , pp. 343-350
    • Vyas, P.1    Deshpande, M.V.2
  • 45
    • 0026091077 scopus 로고
    • Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP
    • Vyas, P. and Deshpande, M. V. 1991. Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP. J. Gen. Appl. Microbiol. 37, 267-275.
    • (1991) J. Gen. Appl. Microbiol. , vol.37 , pp. 267-275
    • Vyas, P.1    Deshpande, M.V.2
  • 47
    • 0026067797 scopus 로고
    • 16S ribosomal DNA amplification for phylogenetic study
    • Weisburg, W. G., Barns, S. M., Pelletier, D. A., and Lane, D. J. 1991. 16S ribosomal DNA amplification for phylogenetic study. J. Bacteriol. 173, 697-703.
    • (1991) J. Bacteriol. , vol.173 , pp. 697-703
    • Weisburg, W.G.1    Barns, S.M.2    Pelletier, D.A.3    Lane, D.J.4
  • 50
    • 0036119750 scopus 로고    scopus 로고
    • Biological control of phytophthora root rots on alfalfa and soybean with Streptomyces
    • Xiao, K., Kinkel, L. L., and Samac, D. A. 2002. Biological control of phytophthora root rots on alfalfa and soybean with Streptomyces. Biol. Control. 23, 285-295.
    • (2002) Biol. Control. , vol.23 , pp. 285-295
    • Xiao, K.1    Kinkel, L.L.2    Samac, D.A.3
  • 51
    • 75649090821 scopus 로고    scopus 로고
    • Selection of Streptomyces isolates from turkish karstic caves against antibiotic resistant microorganisms
    • Yücel, S. and Yamaç M. 2010. Selection of Streptomyces isolates from turkish karstic caves against antibiotic resistant microorganisms. Pak. J. Pharm. Sci. 23, 1-6.
    • (2010) Pak. J. Pharm. Sci. , vol.23 , pp. 1-6
    • Yücel, S.1    Yamaç, M.2
  • 52
    • 60249099384 scopus 로고    scopus 로고
    • Biological control of rice blast (Magnaporthe oryzae) by use of Streptomyces sindeneusis isolate 263 in greenhouse
    • Zarandi, M. E., Shahidi Bonjar, G. H., Dehkaei, F. P., Moosavi, S. A. A., Farokhi, P. R., and Aghighi, S. 2009. Biological control of rice blast (Magnaporthe oryzae) by use of Streptomyces sindeneusis isolate 263 in greenhouse. Am. J. Appl. Sci. 6, 194-199.
    • (2009) Am. J. Appl. Sci. , vol.6 , pp. 194-199
    • Zarandi, M.E.1    Shahidi Bonjar, G.H.2    Dehkaei, F.P.3    Moosavi, S.A.A.4    Farokhi, P.R.5    Aghighi, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.