메뉴 건너뛰기




Volumn 26, Issue 8, 2010, Pages 1437-1443

Antifungal chitinases from Bacillus pumilus SG2: Preliminary report

Author keywords

Antifungal; Bacillus; Chitinase; Enzyme assay; Purification

Indexed keywords

ACTIVE SITE; AMINO ACID RESIDUES; AMMONIUM SULFATE PRECIPITATION; ANTI-FUNGAL; ANTI-FUNGAL ACTIVITY; BACILLUS; BACILLUS CULTURE; BACILLUS PUMILUS; CELL-WALL FORMATION; CHITINASE ENZYMES; CHITINASES; DOMAIN ANALYSIS; EXTRACELLULAR CHITINASES; HALOTOLERANT BACTERIA; OOMYCETES; OPTIMUM PH; PHYTOPHTHORA; PHYTOPHTHORA CAPSICI; PUMILUS; RHIZOCTONIA SOLANI; SALINE SOIL;

EID: 77954456380     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-010-0318-6     Document Type: Article
Times cited : (34)

References (40)
  • 1
    • 34848826214 scopus 로고    scopus 로고
    • Bacillus pumilus SG2 isolated from saline conditions produces and secretes two chitinases
    • doi:10.1111/j.1365-2672.2007.03340.x
    • Ahmadian G, Degrassi G, Venturi V, Zeigler DR, Soudi M, Zanguinejad P (2007) Bacillus pumilus SG2 isolated from saline conditions produces and secretes two chitinases. J Appl Microbiol 103: 1081-1089. doi: 10. 1111/j. 1365-2672. 2007. 03340. x.
    • (2007) J Appl Microbiol , vol.103 , pp. 1081-1089
    • Ahmadian, G.1    Degrassi, G.2    Venturi, V.3    Zeigler, D.R.4    Soudi, M.5    Zanguinejad, P.6
  • 2
    • 0034997585 scopus 로고    scopus 로고
    • Biological control of Fusarium moniliforme in maize
    • doi:10.1016/j.foodcont.2005.12.013
    • Bacon CW, Yates IE, Hinton DM, Meredith F (2001) Biological control of Fusarium moniliforme in maize. Environ Health Perspect 2: 325-332. doi: 10. 1016/j. foodcont. 2005. 12. 013.
    • (2001) Environ Health Perspect , vol.2 , pp. 325-332
    • Bacon, C.W.1    Yates, I.E.2    Hinton, D.M.3    Meredith, F.4
  • 3
    • 0035617311 scopus 로고    scopus 로고
    • Distribution of chitinase in rice (Oryza sativa L) seed and characterization of a hull specific chitinase
    • Baek JH, Han BK, Jo DH (2001) Distribution of chitinase in rice (Oryza sativa L) seed and characterization of a hull specific chitinase. J Biochem Mol Biol 34: 310-315.
    • (2001) J Biochem Mol Biol , vol.34 , pp. 310-315
    • Baek, J.H.1    Han, B.K.2    Jo, D.H.3
  • 5
    • 0016378451 scopus 로고
    • Recent developments of antibiotic research and classification of antibiotics according to chemical structure
    • doi:10.1016/S0065-2164(08)70573-2
    • Beahdy J (1974) Recent developments of antibiotic research and classification of antibiotics according to chemical structure. Adv Appl Microbiol 18: 309-406. doi: 10. 1016/S0065-2164(08)70573-2.
    • (1974) Adv Appl Microbiol , vol.18 , pp. 309-406
    • Beahdy, J.1
  • 6
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene, purification, properties, and possible function
    • doi:10.1007/BF00394536
    • Boller T, Gehri A, Mauch F, Vogeli U (1983) Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta 157: 22-31. doi: 10. 1007/BF00394536.
    • (1983) Planta , vol.157 , pp. 22-31
    • Boller, T.1    Gehri, A.2    Mauch, F.3    Vogeli, U.4
  • 7
    • 0037240823 scopus 로고    scopus 로고
    • Production by Bacillus pumilus (MSH) of an antifungal compound that is active against Mucoraceae and Aspergillus species: Preliminary report
    • doi:10.1099/jmm.0.04935-0
    • Bottone EJ, Peluso RW (2003) Production by Bacillus pumilus (MSH) of an antifungal compound that is active against Mucoraceae and Aspergillus species: preliminary report. J Medical Microbiol 52: 69-74. doi: 10. 1099/jmm. 0. 04935-0.
    • (2003) J Medical Microbiol , vol.52 , pp. 69-74
    • Bottone, E.J.1    Peluso, R.W.2
  • 8
    • 0034901363 scopus 로고    scopus 로고
    • Isolation, identification and evaluation of bacterial antagonists against Botrytis elliptica on lily
    • doi:10.1046/j.1439-0434.2001.00627.x
    • Chiou AL, Wu WS (2001) Isolation, identification and evaluation of bacterial antagonists against Botrytis elliptica on lily. J Phytopathol 149: 319-324. doi: 10. 1046/j. 1439-0434. 2001. 00627. x.
    • (2001) J Phytopathol , vol.149 , pp. 319-324
    • Chiou, A.L.1    Wu, W.S.2
  • 9
    • 0027600382 scopus 로고
    • Antagonistic action of the bacterium Bacillus licheniformis M-4 toward the amoeba Naegleria fowleri
    • doi:10.1111/j.1550-7408.1993.tb04923.x
    • Cordovilla P, Valdivia E, Gonzalez-Segura A, Galvez A, Martinez-Bueno M, Maqueda M (1993) Antagonistic action of the bacterium Bacillus licheniformis M-4 toward the amoeba Naegleria fowleri. J Eukaryot Microbiol 40: 323-328. doi: 10. 1111/j. 1550-7408. 1993. tb04923. x.
    • (1993) J Eukaryot Microbiol , vol.40 , pp. 323-328
    • Cordovilla, P.1    Valdivia, E.2    Gonzalez-Segura, A.3    Galvez, A.4    Martinez-Bueno, M.5    Maqueda, M.6
  • 10
    • 0027962712 scopus 로고
    • Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to groundnut rust, Puccinia arachidis
    • doi:10.1007/BF00414876
    • Gunarantna KR, Balasubramanian R (1994) Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to groundnut rust, Puccinia arachidis. World J Microbiol Biotechnol 10: 342-345. doi: 10. 1007/BF00414876.
    • (1994) World J Microbiol Biotechnol , vol.10 , pp. 342-345
    • Gunarantna, K.R.1    Balasubramanian, R.2
  • 11
    • 0034414956 scopus 로고    scopus 로고
    • Purification and characterization of acidic chitinase from gizzards of broiler (Gallus gallus L.)
    • Han BK, Moon JK, Ryu YW, Park YH, Jo DH (2000) Purification and characterization of acidic chitinase from gizzards of broiler (Gallus gallus L.). J Biochem Mol Biol 33: 326-331.
    • (2000) J Biochem Mol Biol , vol.33 , pp. 326-331
    • Han, B.K.1    Moon, J.K.2    Ryu, Y.W.3    Park, Y.H.4    Jo, D.H.5
  • 12
    • 0005611576 scopus 로고
    • Increased constitutive chitinase activity in transformed Trichoderma harzianum
    • doi:10.1006/bcon.1993.1016
    • Haran S, Schickler H, Chet I (1993) Increased constitutive chitinase activity in transformed Trichoderma harzianum. Biol Control 3: 101-108. doi: 10. 1006/bcon. 1993. 1016.
    • (1993) Biol Control , vol.3 , pp. 101-108
    • Haran, S.1    Schickler, H.2    Chet, I.3
  • 13
    • 21244486744 scopus 로고    scopus 로고
    • Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9
    • Huang CJ, Wang TK, Chung SC, Chen CY (2005) Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9. J Biochem Mol Biol 38: 82-88.
    • (2005) J Biochem Mol Biol , vol.38 , pp. 82-88
    • Huang, C.J.1    Wang, T.K.2    Chung, S.C.3    Chen, C.Y.4
  • 14
    • 26844552531 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular chitinase from the antifungal biocontrol agent Streptomyces halstedii
    • doi:10.1007/s10529-005-1315-y
    • Joo GJ (2005) Purification and characterization of an extracellular chitinase from the antifungal biocontrol agent Streptomyces halstedii. Biotechnol Lett 27: 1483-1486. doi: 10. 1007/s10529-005-1315-y.
    • (2005) Biotechnol Lett , vol.27 , pp. 1483-1486
    • Joo, G.J.1
  • 15
    • 0025264286 scopus 로고
    • Pumilucidin, a complex of new antiviral antibiotics. Production, isolation, chemical properties, structure and biological activity
    • Karuse N, Tenyo O, Kobaru S, Kamei H, Miyaki T, Konishi M, Oki T (1990) Pumilucidin, a complex of new antiviral antibiotics. Production, isolation, chemical properties, structure and biological activity. J Antibiot 43: 267-280.
    • (1990) J Antibiot , vol.43 , pp. 267-280
    • Karuse, N.1    Tenyo, O.2    Kobaru, S.3    Kamei, H.4    Miyaki, T.5    Konishi, M.6    Oki, T.7
  • 16
    • 0017646341 scopus 로고
    • The peptide antibiotics of Bacillus: Chemistry, biogenesis and possible functions
    • Katz E, Demain AL (1977) The peptide antibiotics of Bacillus: chemistry, biogenesis and possible functions. Bacteriol Rev 41: 449-474.
    • (1977) Bacteriol Rev , vol.41 , pp. 449-474
    • Katz, E.1    Demain, A.L.2
  • 17
    • 0030907157 scopus 로고    scopus 로고
    • Bacillus sp. L324-92 for biological control of three rot diseases of the wheat grown with reduced tillage
    • doi:10.1094/PHYTO.1997.87.5.551
    • Kim DS, Cork RJ, Weller DM (1997) Bacillus sp. L324-92 for biological control of three rot diseases of the wheat grown with reduced tillage. Phytopathology 87: 551-558. doi: 10. 1094/PHYTO. 1997. 87. 5. 551.
    • (1997) Phytopathology , vol.87 , pp. 551-558
    • Kim, D.S.1    Cork, R.J.2    Weller, D.M.3
  • 18
    • 0035595131 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptide from bovine skin
    • Kim SK, Kim YT, Byun HG, Park PJ, Ito H (2001) Purification and characterization of antioxidative peptide from bovine skin. J Biochem Mol Biol 34: 219-224.
    • (2001) J Biochem Mol Biol , vol.34 , pp. 219-224
    • Kim, S.K.1    Kim, Y.T.2    Byun, H.G.3    Park, P.J.4    Ito, H.5
  • 19
    • 0026599547 scopus 로고
    • Evaluation of the antifungal activity of the purified chitinase I from the filamentous fungus Aphanocladium album
    • doi:10.1111/j.1574-6968.1992.tb05135.x
    • Kunz C, Ludwig A, Boller T (1992) Evaluation of the antifungal activity of the purified chitinase I from the filamentous fungus Aphanocladium album. FEMS Microbiol Lett 90: 105-109. doi: 10. 1111/j. 1574-6968. 1992. tb05135. x.
    • (1992) FEMS Microbiol Lett , vol.90 , pp. 105-109
    • Kunz, C.1    Ludwig, A.2    Boller, T.3
  • 21
    • 0034761842 scopus 로고    scopus 로고
    • Cloning and sequencing of two genes encoding chitinases A and B from Bacillus cereus CH
    • doi:10.1139/cjm-47-10-895
    • Mabuchi N, Araki Y (2001) Cloning and sequencing of two genes encoding chitinases A and B from Bacillus cereus CH. Can J Microbiol 47: 895-902. doi: 10. 1139/cjm-47-10-895.
    • (2001) Can J Microbiol , vol.47 , pp. 895-902
    • Mabuchi, N.1    Araki, Y.2
  • 22
    • 0030726362 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain
    • Marimoto K, Karita S, Kimura T, Sakka K, Hmiya K (1997) Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J Bacteriol 179: 7306-7314.
    • (1997) J Bacteriol , vol.179 , pp. 7306-7314
    • Marimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Hmiya, K.5
  • 23
    • 0008378919 scopus 로고    scopus 로고
    • Production of chitinase by Fusarium chlamydosporum, a mycoparasite to groundnut rust, Puccinia arachidis
    • Mathivana N, Kabilan V, Murugesan K (1997) Production of chitinase by Fusarium chlamydosporum, a mycoparasite to groundnut rust, Puccinia arachidis. Indian J Exp Biol 35: 890-893.
    • (1997) Indian J Exp Biol , vol.35 , pp. 890-893
    • Mathivana, N.1    Kabilan, V.2    Murugesan, K.3
  • 24
    • 0026475202 scopus 로고
    • Cloned chitinase in fungal pathogen control strategies
    • doi:10.1016/0167-7799(92)90281-Y
    • Oppenheim AB, Chet I (1992) Cloned chitinase in fungal pathogen control strategies. Trends Biotechnol 10: 392-394. doi: 10. 1016/0167-7799(92)90281-Y.
    • (1992) Trends Biotechnol , vol.10 , pp. 392-394
    • Oppenheim, A.B.1    Chet, I.2
  • 25
    • 0034791873 scopus 로고    scopus 로고
    • Suppression of maize root diseases caused by Macrophomina phaseolina, Fusarium moniliforme and Fusarium graminearum by plant growth promoting rhizobacteria
    • doi:10.1078/0944-5013-00103
    • Pal KK, Tilak KV, Saxena AK, Dey R, Singh CS (2001) Suppression of maize root diseases caused by Macrophomina phaseolina, Fusarium moniliforme and Fusarium graminearum by plant growth promoting rhizobacteria. Microbiol Res 156: 209-223. doi: 10. 1078/0944-5013-00103.
    • (2001) Microbiol Res , vol.156 , pp. 209-223
    • Pal, K.K.1    Tilak, K.V.2    Saxena, A.K.3    Dey, R.4    Singh, C.S.5
  • 27
    • 0026331471 scopus 로고
    • A complex chitinolytic system in exponentially growing mycelium of Mucor rouxii: Properties and function
    • doi:10.1099/00221287-137-12-2797
    • Rast DM, Horsch M, Further R, Gooday GW (1991) A complex chitinolytic system in exponentially growing mycelium of Mucor rouxii: properties and function. J Gen Microbiol 137: 2707-2810. doi: 10. 1099/00221287-137-12-2797.
    • (1991) J Gen Microbiol , vol.137 , pp. 2707-2810
    • Rast, D.M.1    Horsch, M.2    Further, R.3    Gooday, G.W.4
  • 28
    • 0026517235 scopus 로고
    • Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus
    • doi:10.1016/0378-1119(92)90604-N
    • Robbins PW, Overbye K, Pero J (1992) Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene 111: 69-76. doi: 10. 1016/0378-1119(92)90604-N.
    • (1992) Gene , vol.111 , pp. 69-76
    • Robbins, P.W.1    Overbye, K.2    Pero, J.3
  • 29
    • 0001194009 scopus 로고    scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • doi:10.1099/00221287-134-1-169
    • Roberts WK, Selitrennikoff CP (1998) Plant and bacterial chitinases differ in antifungal activity. J Gen Microbiol 134: 169-176. doi: 10. 1099/00221287-134-1-169.
    • (1998) J Gen Microbiol , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 30
    • 0031663817 scopus 로고    scopus 로고
    • Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost
    • Sakai K, Yokota A, Kurokawa H, Wakayama M, Moriguchi M (1998) Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost. Appl Environ Microbiol 64: 3397-3402.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3397-3402
    • Sakai, K.1    Yokota, A.2    Kurokawa, H.3    Wakayama, M.4    Moriguchi, M.5
  • 31
    • 0000841453 scopus 로고
    • Secretion of extracellular enzymes by Verticillium psalliotae Treschow and Verticillium lecanii (Zimm.) Viegas during growth on uredospores of the soybean rust fungus in liquid cultures
    • doi:10.1111/j.1439-0434.1991.tb04741.x
    • Saksirirat W, Hoppe HH (1991) Secretion of extracellular enzymes by Verticillium psalliotae Treschow and Verticillium lecanii (Zimm.) Viegas during growth on uredospores of the soybean rust fungus in liquid cultures. J Phytopathol 131: 161-173. doi: 10. 1111/j. 1439-0434. 1991. tb04741. x.
    • (1991) J Phytopathol , vol.131 , pp. 161-173
    • Saksirirat, W.1    Hoppe, H.H.2
  • 32
    • 0001615271 scopus 로고
    • Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate
    • Spizizen J (1958) Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc Natl Acad Sci USA 44: 1072-1078.
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 1072-1078
    • Spizizen, J.1
  • 33
    • 0031980431 scopus 로고    scopus 로고
    • Multiple chitinase enzymes from a single gene of Bacillus licheniformis TP-1
    • doi:10.1016/S0922-338X(97)85672-3
    • Tantimavanich S, Pantuwatana S, Bhumiratana A, Panbangred W (1998) Multiple chitinase enzymes from a single gene of Bacillus licheniformis TP-1. J Ferment Bioeng 85: 259-265. doi: 10. 1016/S0922-338X(97)85672-3.
    • (1998) J Ferment Bioeng , vol.85 , pp. 259-265
    • Tantimavanich, S.1    Pantuwatana, S.2    Bhumiratana, A.3    Panbangred, W.4
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • doi:10.1093/nar/22.22.4673
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680. doi: 10. 1093/nar/22. 22. 4673.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA (1996) Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J 21: 5739-5751.
    • (1996) EMBO J , vol.21 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 36
    • 0027534187 scopus 로고
    • Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7
    • Tsujibo H, Okami Y, Tanno H, Inamori Y (1993) Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J Bacteriol 175: 176-181.
    • (1993) J Bacteriol , vol.175 , pp. 176-181
    • Tsujibo, H.1    Okami, Y.2    Tanno, H.3    Inamori, Y.4
  • 37
    • 0025561986 scopus 로고
    • Purification and some properties of extracellular chitinase from Streptomyces sp. S-84
    • doi:10.2323/jgam.36.377
    • Ueno H, Miyashita K, Swada Y, Oba Y (1990) Purification and some properties of extracellular chitinase from Streptomyces sp. S-84. J Gen Appl Microbiol 36: 377-392. doi: 10. 2323/jgam. 36. 377.
    • (1990) J Gen Appl Microbiol , vol.36 , pp. 377-392
    • Ueno, H.1    Miyashita, K.2    Swada, Y.3    Oba, Y.4
  • 38
    • 0031801241 scopus 로고    scopus 로고
    • Bacillus isolates from the spermosphere of peas and dwarf French beans with antifungal activity against Botrytis cinerea and Pythium species
    • doi:10.1046/j.1365-2672.1998.00411.x
    • Walker R, Powell AA, Seddon B (1998) Bacillus isolates from the spermosphere of peas and dwarf French beans with antifungal activity against Botrytis cinerea and Pythium species. J Appl Microbiol 84: 791-801. doi: 10. 1046/j. 1365-2672. 1998. 00411. x.
    • (1998) J Appl Microbiol , vol.84 , pp. 791-801
    • Walker, R.1    Powell, A.A.2    Seddon, B.3
  • 39
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation
    • Watanabe T, Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H (1994) The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J Bacteriol 176: 4465-4472.
    • (1994) J Bacteriol , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 40
    • 0032847740 scopus 로고    scopus 로고
    • Chitinase gene expression during mycoparasitic interaction of Trichoderma harzianum with its host
    • doi:10.1006/fgbi.1998.1111
    • Zeilinger S, Galhaup C, Payer K, Woo SL, Mach RL, Fekete C, Lorito M, Kubicek CP (1999) Chitinase gene expression during mycoparasitic interaction of Trichoderma harzianum with its host. Fungal Genet Biol 26: 131-140. doi: 10. 1006/fgbi. 1998. 1111.
    • (1999) Fungal Genet Biol , vol.26 , pp. 131-140
    • Zeilinger, S.1    Galhaup, C.2    Payer, K.3    Woo, S.L.4    Mach, R.L.5    Fekete, C.6    Lorito, M.7    Kubicek, C.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.