메뉴 건너뛰기




Volumn 48, Issue 6, 2008, Pages 464-472

Cloning of two cellulase genes from endophytic Paenibacillus polymyxa GS01 and comparison with cel44C-man26A

Author keywords

cel5A gene; cel5b gene; Cellulase; CMC SDS PAGE; Endophytic bacteria; Ginseng; Paenibacillus polymyxa GS01

Indexed keywords

BACTERIAL DNA; CELLULASE; GLYCOSIDASE; RECOMBINANT PROTEIN;

EID: 57349120152     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.200700281     Document Type: Article
Times cited : (36)

References (45)
  • 1
    • 84966143176 scopus 로고
    • Enzymatic treatment of clover root hairs removes a barrier to Rhizobium-host specificity
    • Al-Mallah, M.K., Davey, M.R. and Cocking, E.C., 1987. Enzymatic treatment of clover root hairs removes a barrier to Rhizobium-host specificity. Biotechnology, 5, 1319-1322.
    • (1987) Biotechnology , vol.5 , pp. 1319-1322
    • Al-Mallah, M.K.1    Davey, M.R.2    Cocking, E.C.3
  • 3
    • 0025214242 scopus 로고
    • Molecular cloning, expression, and characterization of endo-β-1,4-glucanase genes from Bacillus polymyxa and Bacillus circulans
    • Baird, S., Johnson, D.A. and Seligy, V.L., 1990. Molecular cloning, expression, and characterization of endo-β-1,4-glucanase genes from Bacillus polymyxa and Bacillus circulans. J. Bacteriol., 172, 1576-1586.
    • (1990) J. Bacteriol , vol.172 , pp. 1576-1586
    • Baird, S.1    Johnson, D.A.2    Seligy, V.L.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. Biochem., 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 33751003227 scopus 로고    scopus 로고
    • A cel44C-man26A gene of endophytic Paenibacillus polymyxa GS01 has multi-glycosyl hydrolases in two catalytic domains
    • Cho, K.M., Hong, S.Y., Lee, S.M., Kim, Y.H., Kahng, G.G., Kim, H. and Yun, H.D., 2006. A cel44C-man26A gene of endophytic Paenibacillus polymyxa GS01 has multi-glycosyl hydrolases in two catalytic domains. Appl. Microbiol. Biotechnol., 73, 618-630.
    • (2006) Appl. Microbiol. Biotechnol , vol.73 , pp. 618-630
    • Cho, K.M.1    Hong, S.Y.2    Lee, S.M.3    Kim, Y.H.4    Kahng, G.G.5    Kim, H.6    Yun, H.D.7
  • 6
    • 34547608146 scopus 로고    scopus 로고
    • Endophytic bacterial communities in ginseng and their antifungal activity against pathogens
    • Cho, K.M., Hong, S.Y., Lee, S.M., Kim, Y.H., Kahng, G.G., Lim, Y.P., Kim, H. and Yun, H.D., 2007. Endophytic bacterial communities in ginseng and their antifungal activity against pathogens. Microbial Ecol., 54, 341-351.
    • (2007) Microbial Ecol , vol.54 , pp. 341-351
    • Cho, K.M.1    Hong, S.Y.2    Lee, S.M.3    Kim, Y.H.4    Kahng, G.G.5    Lim, Y.P.6    Kim, H.7    Yun, H.D.8
  • 7
    • 27944458038 scopus 로고    scopus 로고
    • Colonization and population changes of a biocontrol agent, Paenibacillus polymyxa E681, in seeds and roots
    • Choi, O., Kim, J., Ryu, C.M. and Park, C.S., 2004. Colonization and population changes of a biocontrol agent, Paenibacillus polymyxa E681, in seeds and roots. Plant Pathol., J., 20, 97-102.
    • (2004) Plant Pathol., J , vol.20 , pp. 97-102
    • Choi, O.1    Kim, J.2    Ryu, C.M.3    Park, C.S.4
  • 8
    • 0027494513 scopus 로고
    • Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: Evidence for an evolutionary "mix-and-match" of enzyme domains
    • Cooper, V.J.C. and Salmond, G.P., 1993. Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary "mix-and-match" of enzyme domains. Mol. Gen. Genet., 241, 341-350.
    • (1993) Mol. Gen. Genet , vol.241 , pp. 341-350
    • Cooper, V.J.C.1    Salmond, G.P.2
  • 10
    • 33646014149 scopus 로고    scopus 로고
    • Survival of gfp-tagged antagonistic bacteria in the rhizophere of tomato plants and their effects on the indigenous bacterial community
    • Götz, M., Gomes, N.C.M., Dratwinski, A., Costa, R., Berg, G., Peixoto, R., Mendonς-Hagle, L., Smalla, K., 2006. Survival of gfp-tagged antagonistic bacteria in the rhizophere of tomato plants and their effects on the indigenous bacterial community. FEMS Microbiol. Ecol., 56, 207-218.
    • (2006) FEMS Microbiol. Ecol , vol.56 , pp. 207-218
    • Götz, M.1    Gomes, N.C.M.2    Dratwinski, A.3    Costa, R.4    Berg, G.5    Peixoto, R.6    Mendonς-Hagle, L.7    Smalla, K.8
  • 12
    • 0026734330 scopus 로고
    • celA from Bacillus lautus PL36 encodes a novel cellulose-binding endo-β-1,4-glucanase
    • Hansen, C.K., Diderichsen, B. and Jorgensen, P.L., 1992. celA from Bacillus lautus PL36 encodes a novel cellulose-binding endo-β-1,4-glucanase. J. Bacteriol., 174, 3522-3531.
    • (1992) J. Bacteriol , vol.174 , pp. 3522-3531
    • Hansen, C.K.1    Diderichsen, B.2    Jorgensen, P.L.3
  • 13
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B. and Davies, G., 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol., 7, 637-644.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 14
    • 0032571552 scopus 로고    scopus 로고
    • A scheme for designating enzymes that hydrolases the polysaccharides in the cells of plants
    • Henrissat, B., Teeri, T.T. and Warren, R.A.J., 1998. A scheme for designating enzymes that hydrolases the polysaccharides in the cells of plants. FEBS Lett., 425, 352-354.
    • (1998) FEBS Lett , vol.425 , pp. 352-354
    • Henrissat, B.1    Teeri, T.T.2    Warren, R.A.J.3
  • 15
    • 33845637907 scopus 로고    scopus 로고
    • Characterization of an extracellular xylanase in Paenibacillus sp. HY-8 isolated from an herbivorous longicorn beetle
    • Heo, S., Kwak, J., Oh, H.W., Park, D.S., Bae, K.S., Shin, D.H. and Park, H.Y., 2006. Characterization of an extracellular xylanase in Paenibacillus sp. HY-8 isolated from an herbivorous longicorn beetle. J. Microbiol. Biotechnol., 16, 1753-1759.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1753-1759
    • Heo, S.1    Kwak, J.2    Oh, H.W.3    Park, D.S.4    Bae, K.S.5    Shin, D.H.6    Park, H.Y.7
  • 16
    • 0009739306 scopus 로고
    • Ultrastructure of bacterial penetration in plants
    • Huan, J.S., 1986. Ultrastructure of bacterial penetration in plants. Annu. Rev. Phytopathol., 24, 141-157.
    • (1986) Annu. Rev. Phytopathol , vol.24 , pp. 141-157
    • Huan, J.S.1
  • 17
    • 13844256879 scopus 로고    scopus 로고
    • Purification and properties of a low molecular weight 1,4-β-D-glucan glucohydrolase having on active site for carboxymehtyl cellulose and xylan from an alkalothermophilic Thermomonospora sp
    • Jagtap, S. and Rao, M., 2005. Purification and properties of a low molecular weight 1,4-β-D-glucan glucohydrolase having on active site for carboxymehtyl cellulose and xylan from an alkalothermophilic Thermomonospora sp. Biochem. Biophys. Res. Commun., 329, 111-116.
    • (2005) Biochem. Biophys. Res. Commun , vol.329 , pp. 111-116
    • Jagtap, S.1    Rao, M.2
  • 18
    • 0025172134 scopus 로고
    • Multiple endo-beta-1,4-glucanase- encoding genes from Bacillus lautus PL236 and characterization of the celB gene
    • Jorgensen, P.L. and Hansen, C.K., 1990. Multiple endo-beta-1,4-glucanase- encoding genes from Bacillus lautus PL236 and characterization of the celB gene. Gene, 93, 55-60.
    • (1990) Gene , vol.93 , pp. 55-60
    • Jorgensen, P.L.1    Hansen, C.K.2
  • 19
    • 0037177815 scopus 로고    scopus 로고
    • Biochemical and genetic properties of Paenibacillus glycosyl hydrolase having chitosanase activity and discoidin domain
    • Kimoto, H., Kusaoke, H., Yamamoto, I., Fujii, Y., Onodera, T. and Taketo, A., 2002. Biochemical and genetic properties of Paenibacillus glycosyl hydrolase having chitosanase activity and discoidin domain. J. Biol. Chem., 277, 14695-14702.
    • (2002) J. Biol. Chem , vol.277 , pp. 14695-14702
    • Kimoto, H.1    Kusaoke, H.2    Yamamoto, I.3    Fujii, Y.4    Onodera, T.5    Taketo, A.6
  • 20
    • 8644255235 scopus 로고    scopus 로고
    • Purification and characterization of two thermostable xylanases from Paenibacillus sp. DG-22
    • Lee, Y.E. and Lim, P.O., 2004. Purification and characterization of two thermostable xylanases from Paenibacillus sp. DG-22. J. Microbiol. Biotechnol., 14, 1014-1021.
    • (2004) J. Microbiol. Biotechnol , vol.14 , pp. 1014-1021
    • Lee, Y.E.1    Lim, P.O.2
  • 21
    • 20944451101 scopus 로고    scopus 로고
    • Cloning of celC, third cellulase gene, from Pectobacterium carotovorum subsp. carotovorum LY34 and its comparison to those of Pectobacterium sp
    • Lim, W.J., Ryu, S.K., Park, S.R., Kim, M.K., An, C.L., Hong, S.Y., Shin, E.C., Lee , J.Y., Lim, Y.P. and Yun, H.D., 2005. Cloning of celC, third cellulase gene, from Pectobacterium carotovorum subsp. carotovorum LY34 and its comparison to those of Pectobacterium sp. J. Microbiol. Biotechnol., 15, 302-309.
    • (2005) J. Microbiol. Biotechnol , vol.15 , pp. 302-309
    • Lim, W.J.1    Ryu, S.K.2    Park, S.R.3    Kim, M.K.4    An, C.L.5    Hong, S.Y.6    Shin, E.C.7    Lee, J.Y.8    Lim, Y.P.9    Yun, H.D.10
  • 23
    • 31344479544 scopus 로고    scopus 로고
    • Ethanol fermentation from biomass resources: Current state and prospects
    • Lin, Y. and Tanaka, S., 2006. Ethanol fermentation from biomass resources: current state and prospects. Appl. Microbiol. Bitechnol., 69, 627-642.
    • (2006) Appl. Microbiol. Bitechnol , vol.69 , pp. 627-642
    • Lin, Y.1    Tanaka, S.2
  • 24
    • 0042171781 scopus 로고    scopus 로고
    • Molecular cloning and expression in Escherichia coli of an exolevanase gene from the endophytic bacterium Gluconacetobacter diazotrophicus SRT4
    • Menendez, C., Hemandez, L., Selman, G., Mendoza, M.F., Hevia, P., Sotolongo, M. and Arrieta, J.G., 2002. Molecular cloning and expression in Escherichia coli of an exolevanase gene from the endophytic bacterium Gluconacetobacter diazotrophicus SRT4. Curr. Microbiol., 45, 5-12.
    • (2002) Curr. Microbiol , vol.45 , pp. 5-12
    • Menendez, C.1    Hemandez, L.2    Selman, G.3    Mendoza, M.F.4    Hevia, P.5    Sotolongo, M.6    Arrieta, J.G.7
  • 25
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for the determination of reducing sugar
    • Miller, G.L., 1959. Use of dinitrosalicylic acid reagent for the determination of reducing sugar. Anal. Chem., 31, 426-428.
    • (1959) Anal. Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 26
    • 0037373344 scopus 로고    scopus 로고
    • Molecular cloning of endo-β-D-1,4-glucnase genes, rce1, rce2, and rce3, from Rhizopus oryzae
    • Moriya, T., Murashima, K., Nakne, A., Yanai, K., Sumida, N., Koga, J., Murakami, T. and Kono, T., 2003. Molecular cloning of endo-β-D-1,4-glucnase genes, rce1, rce2, and rce3, from Rhizopus oryzae. J. Bacteriol., 185, 1749-1759.
    • (2003) J. Bacteriol , vol.185 , pp. 1749-1759
    • Moriya, T.1    Murashima, K.2    Nakne, A.3    Yanai, K.4    Sumida, N.5    Koga, J.6    Murakami, T.7    Kono, T.8
  • 27
    • 0034711446 scopus 로고    scopus 로고
    • Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum
    • Mosbah, A., Belaïch. A., Bornet. O., Belaïch, J.P., Henrissat, B. and Darbon H., 2000. Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum. J. Mol. Biol., 24, 201-217.
    • (2000) J. Mol. Biol , vol.24 , pp. 201-217
    • Mosbah, A.1    Belaïch, A.2    Bornet, O.3    Belaïch, J.P.4    Henrissat, B.5    Darbon, H.6
  • 28
    • 0031590710 scopus 로고    scopus 로고
    • Characterization of Erwinia carotovora subsp. carotovora LY34 endo-1,4-β- glucnase gene and rapid identification of their gene products
    • Park, Y.W., Lim, S.T., Cho, S.J. and Yun, H.D., 1997. Characterization of Erwinia carotovora subsp. carotovora LY34 endo-1,4-β- glucnase gene and rapid identification of their gene products. Biochem. Biophys. Res. Commun., 241, 636-641.
    • (1997) Biochem. Biophys. Res. Commun , vol.241 , pp. 636-641
    • Park, Y.W.1    Lim, S.T.2    Cho, S.J.3    Yun, H.D.4
  • 29
    • 33646083242 scopus 로고    scopus 로고
    • Paenibacillus curdlanolyticus strain B-6 xylanolytic-cellulolytic enzyme system that degrades insoluble polysaccharides
    • Pason, P., Kyu, K.L. and Ratanakhanokchai, K., 2006. Paenibacillus curdlanolyticus strain B-6 xylanolytic-cellulolytic enzyme system that degrades insoluble polysaccharides. Appl. Environ. Microbiol., 72, 2483-2490.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 2483-2490
    • Pason, P.1    Kyu, K.L.2    Ratanakhanokchai, K.3
  • 30
    • 0035102159 scopus 로고    scopus 로고
    • Molecular cloning and characterization of multidomain endoglucanase from Paenibacillus sp. BP-23: Evaluation of its performance in pulp refining
    • Pastor, F.I.J., Pujol, X., Blanco, A., Vidal, T., Torres, A.L. and Díaz, P., 2001. Molecular cloning and characterization of multidomain endoglucanase from Paenibacillus sp. BP-23: evaluation of its performance in pulp refining. Appl. Microbiol. Biotechnol., 55, 61-68.
    • (2001) Appl. Microbiol. Biotechnol , vol.55 , pp. 61-68
    • Pastor, F.I.J.1    Pujol, X.2    Blanco, A.3    Vidal, T.4    Torres, A.L.5    Díaz, P.6
  • 31
    • 85149604906 scopus 로고    scopus 로고
    • Pleban, S., Chernin, L. and Chet, I., 1997. Chitinolytic activity of an endophytic strain of Bacillus cereus. Lett. Appl. Mcirobiol., 25, 284-288.
    • Pleban, S., Chernin, L. and Chet, I., 1997. Chitinolytic activity of an endophytic strain of Bacillus cereus. Lett. Appl. Mcirobiol., 25, 284-288.
  • 32
    • 0030855242 scopus 로고    scopus 로고
    • Bacterial endophytes in cotton: Mechanisms of entering the plant
    • Quadt-Hallmann, A., Benhamou, A.N. and Kleopper, J.W., 1997. Bacterial endophytes in cotton: mechanisms of entering the plant. Can. J. Microbiol., 43, 577-582.
    • (1997) Can. J. Microbiol , vol.43 , pp. 577-582
    • Quadt-Hallmann, A.1    Benhamou, A.N.2    Kleopper, J.W.3
  • 33
    • 0031966083 scopus 로고    scopus 로고
    • Life in grasses: Diazotrophic endophytes
    • Reinhold-Hurek, B. and Hurek, T., 1998. Life in grasses: diazotrophic endophytes. Trend. Microbiol., 6, 139-144.
    • (1998) Trend. Microbiol , vol.6 , pp. 139-144
    • Reinhold-Hurek, B.1    Hurek, T.2
  • 34
    • 0034917190 scopus 로고    scopus 로고
    • Characterization of pectin lyase produced by an endophytic strain isolated from coffee cherries
    • Sakiyama, C.C.H., Paula, E.M., Pereira, P.C., Borges, A.C. and Silva, D.O., 2001. Characterization of pectin lyase produced by an endophytic strain isolated from coffee cherries. Lett. Appl. Microbiol., 33, 117-121.
    • (2001) Lett. Appl. Microbiol , vol.33 , pp. 117-121
    • Sakiyama, C.C.H.1    Paula, E.M.2    Pereira, P.C.3    Borges, A.C.4    Silva, D.O.5
  • 36
    • 0038045561 scopus 로고    scopus 로고
    • Exo-mode of action of cellobiohydrolase Cel48C from Paenibacillus sp. BP-23
    • Sánchez, M.M., Pastor, F.I.J. and Diaz, P., 2003. Exo-mode of action of cellobiohydrolase Cel48C from Paenibacillus sp. BP-23. Eur. J. Biochem., 270, 2913-2919.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2913-2919
    • Sánchez, M.M.1    Pastor, F.I.J.2    Diaz, P.3
  • 37
    • 0032559380 scopus 로고    scopus 로고
    • Crystal structure of beta-glycosidase A from Bacillus polymyxa: Insights in to the catalytic activity in family 1 glycosyl hydrolasess
    • Sanz-Aparzicio, J., Hermoso, J.A., Martinez-Ripoll, M., Lequerica, J.L. and Polaina, J., 1998. Crystal structure of beta-glycosidase A from Bacillus polymyxa: insights in to the catalytic activity in family 1 glycosyl hydrolasess. J. Mol. Biol., 275, 491-502.
    • (1998) J. Mol. Biol , vol.275 , pp. 491-502
    • Sanz-Aparzicio, J.1    Hermoso, J.A.2    Martinez-Ripoll, M.3    Lequerica, J.L.4    Polaina, J.5
  • 38
    • 0242473815 scopus 로고    scopus 로고
    • Production and characterization of a thermostable alpha-amylase from Nocardiopsis sp. endophyte of yam bean
    • Stamford, T.L., Stamfod, N.P., Coelho, L.C. and Araujo, J.M., 2001. Production and characterization of a thermostable alpha-amylase from Nocardiopsis sp. endophyte of yam bean. Bioresour. Technol., 76, 137-141.
    • (2001) Bioresour. Technol , vol.76 , pp. 137-141
    • Stamford, T.L.1    Stamfod, N.P.2    Coelho, L.C.3    Araujo, J.M.4
  • 39
    • 0036178871 scopus 로고    scopus 로고
    • Production and characterization of a thermostable glucoamylase from Streptosporangium sp. endophyte of maize leaves
    • Stamford, T.L., Stamfod, N.P., Coelho, L.C. and Araujo, J.M., 2002. Production and characterization of a thermostable glucoamylase from Streptosporangium sp. endophyte of maize leaves. Bioresour. Technol., 83, 105-109.
    • (2002) Bioresour. Technol , vol.83 , pp. 105-109
    • Stamford, T.L.1    Stamfod, N.P.2    Coelho, L.C.3    Araujo, J.M.4
  • 41
    • 0020032328 scopus 로고
    • Use of congo red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from bovine rumen
    • Teahter, R.M. and Wood, P.J., 1982. Use of congo red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from bovine rumen. Microbiology, 43, 777-780.
    • (1982) Microbiology , vol.43 , pp. 777-780
    • Teahter, R.M.1    Wood, P.J.2
  • 42
    • 32044467100 scopus 로고    scopus 로고
    • Paenibacillus polymyxa invades plantroots and forms biofilms
    • Timmusk, S., Grantcharova, N. and Wagner, E.G.H., 2005. Paenibacillus polymyxa invades plantroots and forms biofilms. Appl. Environ. Microbiol., 71, 7292-7300.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 7292-7300
    • Timmusk, S.1    Grantcharova, N.2    Wagner, E.G.H.3
  • 43
    • 0035807441 scopus 로고    scopus 로고
    • Evaluation of plant growth promoting and colonization ability of endophytic diazotrophs from deep water rice
    • Verma, S.C., Ladha, J.K. and Tripathi, A.K., 2001. Evaluation of plant growth promoting and colonization ability of endophytic diazotrophs from deep water rice. J. Biotechnol., 81, 127-141.
    • (2001) J. Biotechnol , vol.81 , pp. 127-141
    • Verma, S.C.1    Ladha, J.K.2    Tripathi, A.K.3
  • 44
    • 0034922896 scopus 로고    scopus 로고
    • Fuel ethanol production from lignocellulose: A challenge for metabolic engineering and process integration
    • Zaldivar, J., Nielsen, J. and Olsson, L., 2001. Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Appl. Microbiol. Biotechnol., 56, 17-34.
    • (2001) Appl. Microbiol. Biotechnol , vol.56 , pp. 17-34
    • Zaldivar, J.1    Nielsen, J.2    Olsson, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.