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Volumn 103, Issue 4, 2007, Pages 1081-1089

Bacillus pumilus SG2 isolated from saline conditions produces and secretes two chitinases

Author keywords

Bacillus pumilus; Family 18 chitinases; Gene cloning; Halotolerant; Regulation

Indexed keywords

BACTERIOLOGY; GENES;

EID: 34848826214     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2007.03340.x     Document Type: Article
Times cited : (37)

References (39)
  • 1
    • 27844612307 scopus 로고    scopus 로고
    • Extreme environments as a resource for microorganisms and novel biocatalysts
    • Antranikian, G., Vorgias, C.E. Bertoldo, C. (2005) Extreme environments as a resource for microorganisms and novel biocatalysts. Adv Biochem Eng Biotechnol 96, 219 262.
    • (2005) Adv Biochem Eng Biotechnol , vol.96 , pp. 219-262
    • Antranikian, G.1    Vorgias, C.E.2    Bertoldo, C.3
  • 3
  • 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 Biohem 72, 248 254.
    • (1976) Anal Biohem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0023210141 scopus 로고
    • The synthesis and degradation of chitin
    • Cabib, E. (1986) The synthesis and degradation of chitin. Adv Enzymol Relat Areas Mol Biol 59, 59 101.
    • (1986) Adv Enzymol Relat Areas Mol Biol , vol.59 , pp. 59-101
    • Cabib, E.1
  • 6
    • 0032856344 scopus 로고    scopus 로고
    • Water-soluble chitin as a wound healing accelerator
    • Cho, Y.W., Cho, Y.N., Cheng, S.H., Yoo, G. Ko, S.W. (1999) Water-soluble chitin as a wound healing accelerator. Biomaterials 20, 2139 2145.
    • (1999) Biomaterials , vol.20 , pp. 2139-2145
    • Cho, Y.W.1    Cho, Y.N.2    Cheng, S.H.3    Yoo, G.4    Ko, S.W.5
  • 7
    • 15444365716 scopus 로고    scopus 로고
    • An agglutinating chitinase with two chitin-binding domains confers fungal protection in transgenic potato
    • Chye, M.L., Zhao, K.J., He, Z.M., Ramalingam, S. Fung, K.L. (2005) An agglutinating chitinase with two chitin-binding domains confers fungal protection in transgenic potato. Planta 220, 717 730.
    • (2005) Planta , vol.220 , pp. 717-730
    • Chye, M.L.1    Zhao, K.J.2    He, Z.M.3    Ramalingam, S.4    Fung, K.L.5
  • 8
    • 33745039979 scopus 로고    scopus 로고
    • Review of fungal chitinases
    • Duo-Chuan, L. (2006) Review of fungal chitinases. Mycopathologia 161, 345 360.
    • (2006) Mycopathologia , vol.161 , pp. 345-360
    • Duo-Chuan, L.1
  • 9
    • 0019739408 scopus 로고
    • Purification and characteristics of two beta-N-acetylhexosaminidases from the tobacco hornworm, Manduca sexta (L.; Lepidoptera: Sphingidae)
    • Dziadik-Turner, C., Koga, D., Mai, M.S. Kramer, K.J. (1981) Purification and characteristics of two beta-N-acetylhexosaminidases from the tobacco hornworm, Manduca sexta (L.; Lepidoptera: Sphingidae). Arch Biochem Biophys 212, 546 560.
    • (1981) Arch Biochem Biophys , vol.212 , pp. 546-560
    • Dziadik-Turner, C.1    Koga, D.2    Mai, M.S.3    Kramer, K.J.4
  • 10
    • 0026709204 scopus 로고
    • What's new in chitinase research?
    • Flach, J., Pilet, P.E. Jolles, P. (1992) What's new in chitinase research? Experientia 48, 701 716.
    • (1992) Experientia , vol.48 , pp. 701-716
    • Flach, J.1    Pilet, P.E.2    Jolles, P.3
  • 11
    • 0035203403 scopus 로고    scopus 로고
    • A class I chitinase from soybean seed coat
    • Gijzen, M., Kuflu, K., Qutob, D. Chernys, J.T. (2001) A class I chitinase from soybean seed coat. J Exp Bot 52, 2283 2289.
    • (2001) J Exp Bot , vol.52 , pp. 2283-2289
    • Gijzen, M.1    Kuflu, K.2    Qutob, D.3    Chernys, J.T.4
  • 12
    • 0033290243 scopus 로고    scopus 로고
    • Aggressive and defensive roles for chitinases
    • Gooday, G.W. (1999) Aggressive and defensive roles for chitinases. EXS 87, 157 169.
    • (1999) EXS , vol.87 , pp. 157-169
    • Gooday, G.W.1
  • 13
    • 0028907495 scopus 로고
    • Catabolite repression in Bacillus subtilis: A global regulatory mechanism for the gram-positive bacteria?
    • Hueck, C.J. Hillen, W. (1995) Catabolite repression in Bacillus subtilis: a global regulatory mechanism for the gram-positive bacteria? Mol Microbiol 15, 395 401.
    • (1995) Mol Microbiol , vol.15 , pp. 395-401
    • Hueck, C.J.1    Hillen, W.2
  • 14
    • 33745489151 scopus 로고    scopus 로고
    • Purification, characterization and gene cloning of 46 kDa chitinase (Chi46) from Trichoderma reesei PC-3-7 and its expression in Escherichia coli
    • Ike, M., Nagamatsu, K., Shioya, A., Nogawa, M., Ogasawara, W., Okada, H. Morikawa, Y. (2006) Purification, characterization and gene cloning of 46 kDa chitinase (Chi46) from Trichoderma reesei PC-3-7 and its expression in Escherichia coli. Appl Microbiol Biotechnol 71, 294 303.
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 294-303
    • Ike, M.1    Nagamatsu, K.2    Shioya, A.3    Nogawa, M.4    Ogasawara, W.5    Okada, H.6    Morikawa, Y.7
  • 15
    • 0141504461 scopus 로고    scopus 로고
    • Application of chitin and chitosan derivatives in the pharmaceutical field
    • Kato, Y., Onishi, H. Machida, Y. (2003) Application of chitin and chitosan derivatives in the pharmaceutical field. Curr Pharm Biotechnol 4, 303 309.
    • (2003) Curr Pharm Biotechnol , vol.4 , pp. 303-309
    • Kato, Y.1    Onishi, H.2    MacHida, Y.3
  • 16
    • 0037393710 scopus 로고    scopus 로고
    • Molecular cloning, sequencing and expression of the gene encoding a novel chitinase a from a marine bacterium, Pseudomonas sp. PE2, and its domain structure
    • Kitamura, E. Kamei, Y. (2003) Molecular cloning, sequencing and expression of the gene encoding a novel chitinase A from a marine bacterium, Pseudomonas sp. PE2, and its domain structure. Appl Microbiol Biotechnol 61, 140 149.
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 140-149
    • Kitamura, E.1    Kamei, Y.2
  • 17
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in prokaryotes, eukaryotes, and organelles
    • Kozak, M. (1983) Comparison of initiation of protein synthesis in prokaryotes, eukaryotes, and organelles. Microbiol Rev 47, 1 45.
    • (1983) Microbiol Rev , vol.47 , pp. 1-45
    • Kozak, M.1
  • 18
    • 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
  • 19
    • 0036902507 scopus 로고    scopus 로고
    • Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity
    • Liu, M., Cai, Q.X., Liu, H.Z., Zhang, B.H., Yan, J.P. Yuan, Z.M. (2002) Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity. J Appl Microbiol 93, 374 379.
    • (2002) J Appl Microbiol , vol.93 , pp. 374-379
    • Liu, M.1    Cai, Q.X.2    Liu, H.Z.3    Zhang, B.H.4    Yan, J.P.5    Yuan, Z.M.6
  • 22
    • 84942782727 scopus 로고
    • Antifungal hydrolases in pea tissue: I. purification and characterization of two chitinases and two beta-1, 3-Glucanases differentially regulated during development and in response to fungal infection
    • Mauch, F., Hadwiger, L.A. Boller, T. (1988) Antifungal hydrolases in pea tissue: I. purification and characterization of two chitinases and two beta-1, 3-Glucanases differentially regulated during development and in response to fungal infection. Plant Physiol 87, 325 333.
    • (1988) Plant Physiol , vol.87 , pp. 325-333
    • Mauch, F.1    Hadwiger, L.A.2    Boller, T.3
  • 23
    • 0033288483 scopus 로고    scopus 로고
    • Native, industrial and fossil chitins
    • Muzzarelli, R.A. (1999) Native, industrial and fossil chitins. EXS 87, 1 6.
    • (1999) EXS , vol.87 , pp. 1-6
    • Muzzarelli, R.A.1
  • 26
    • 1542269017 scopus 로고    scopus 로고
    • HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria
    • Poncet, S., Mijakovic, I., Nessler, S., Gueguen-Chaignon, V., Chaptal, V., Galinier, A., Boel, G., Maze, A. et al. (2004) HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria. Biochim Biophys Acta 1697, 123 135.
    • (2004) Biochim Biophys Acta , vol.1697 , pp. 123-135
    • Poncet, S.1    Mijakovic, I.2    Nessler, S.3    Gueguen-Chaignon, V.4    Chaptal, V.5    Galinier, A.6    Boel, G.7    Maze, A.8
  • 27
    • 0037491315 scopus 로고    scopus 로고
    • Removal of metals from aqueous solutions using natural chitinous materials
    • Rae, I.B. Gibb, S.W. (2003) Removal of metals from aqueous solutions using natural chitinous materials. Water Sci Technol 47, 189 196.
    • (2003) Water Sci Technol , vol.47 , pp. 189-196
    • Rae, I.B.1    Gibb, S.W.2
  • 29
    • 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., Yolota, 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    Yolota, A.2    Kurokawa, H.3    Wakayama, M.4    Moriguchi, M.5
  • 31
    • 0015609730 scopus 로고
    • A common error in measurements of 340 nm
    • Schales, O. (1973) A common error in measurements of 340 nm. Clin Chem 19, 434 435.
    • (1973) Clin Chem , vol.19 , pp. 434-435
    • Schales, O.1
  • 32
    • 0023130821 scopus 로고
    • Regulation of a plant pathogenesis-related enzyme: Inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin
    • Shinshi, H., Mohnen, D. Meins, F. Jr. (1987) Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci USA 84, 89 93.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 89-93
    • Shinshi, H.1    Mohnen, D.2    Meins Jr., F.3
  • 35
    • 0038495578 scopus 로고    scopus 로고
    • Production, properties, and some new applications of chitin and its derivatives
    • Synowiecki, J. Al-Khateeb, N.A. (2003) Production, properties, and some new applications of chitin and its derivatives. Crit Rev Food Sci Nutr 43, 145 171.
    • (2003) Crit Rev Food Sci Nutr , vol.43 , pp. 145-171
    • Synowiecki, J.1    Al-Khateeb, N.A.2
  • 36
    • 20444419814 scopus 로고    scopus 로고
    • Characterization and antifungal activity of gazyumaru (Ficus microcarpa) latex chitinases: Both the chitin-binding and the antifungal activities of class I chitinase are reinforced with increasing ionic strength
    • Taira, T., Ohdomari, A., Nakama, N., Shimoji, M. Ishihara, M. (2005) Characterization and antifungal activity of gazyumaru (Ficus microcarpa) latex chitinases: both the chitin-binding and the antifungal activities of class I chitinase are reinforced with increasing ionic strength. Biosci Biotechnol Biochem 69, 811 818.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 811-818
    • Taira, T.1    Ohdomari, A.2    Nakama, N.3    Shimoji, M.4    Ishihara, M.5
  • 37
    • 3843052542 scopus 로고    scopus 로고
    • Comparative evolutionary histories of chitinase genes in the genus Zea and family Poaceae
    • Tiffin, P. (2004) Comparative evolutionary histories of chitinase genes in the genus Zea and family Poaceae. Genetics 167, 1331 1340.
    • (2004) Genetics , vol.167 , pp. 1331-1340
    • Tiffin, P.1
  • 39
    • 0035826283 scopus 로고    scopus 로고
    • Microbial reclamation of shellfish wastes for the production of chitinases
    • Wang, S. Hwang, J. (2001) Microbial reclamation of shellfish wastes for the production of chitinases. Enz Microb Technol 28, 376 382.
    • (2001) Enz Microb Technol , vol.28 , pp. 376-382
    • Wang, S.1    Hwang, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.