메뉴 건너뛰기




Volumn 66, Issue 2, 2000, Pages 664-670

A gene encoding a novel multidomain β-1,4-mannanase from Caldibacillus cellulovorans and action of the recombinant enzyme on kraft pulp

Author keywords

[No Author keywords available]

Indexed keywords

BETA MANNOSIDASE; RECOMBINANT ENZYME;

EID: 0033952913     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.2.664-670.2000     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 0027471408 scopus 로고
    • β-Mannanase of Streptomyces lividans 66: Cloning and DNA sequence of the manA gene and characterization of the enzyme
    • Arcand, N., D. Kluepfel, F. W. Paradis, R. Morosoli, and F. Shareck. 1993. β-Mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme. Biochem. J. 290:857-863.
    • (1993) Biochem. J. , vol.290 , pp. 857-863
    • Arcand, N.1    Kluepfel, D.2    Paradis, F.W.3    Morosoli, R.4    Shareck, F.5
  • 2
    • 0025316285 scopus 로고
    • The Glu residue in the conserved Asn-Glu-Pro sequence of two highly divergent endo-β-1,4-glucanases is essential for enzymatic activity
    • Baird, S. D., M. A. Hefford, D. A. Johnson, W. L. Sung, M. Yaguchi, and V. L. Seligy. 1990. The Glu residue in the conserved Asn-Glu-Pro sequence of two highly divergent endo-β-1,4-glucanases is essential for enzymatic activity. Biochem. Biophys. Res. Commun. 169:1035-1039.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 1035-1039
    • Baird, S.D.1    Hefford, M.A.2    Johnson, D.A.3    Sung, W.L.4    Yaguchi, M.5    Seligy, V.L.6
  • 3
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • Béguin, P. 1990. Molecular biology of cellulose degradation. Annu. Rev. Microbiol. 44:219-248.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 219-248
    • Béguin, P.1
  • 4
    • 0026771506 scopus 로고
    • The catalytic domain of endoglucanase A from Clostridium cellulolyticum: Effects of arginine 79 and histidine 122 mutations on catalysis
    • Belaich, A., H.-P. Fierobe, D. Baty, B. Busetta, C. Bagnara-Tardif, C. Gaudin, and J.-P. Belaich. 1992. The catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis. J. Bacteriol. 174:4677-4682.
    • (1992) J. Bacteriol. , vol.174 , pp. 4677-4682
    • Belaich, A.1    Fierobe, H.-P.2    Baty, D.3    Busetta, B.4    Bagnara-Tardif, C.5    Gaudin, C.6    Belaich, J.-P.7
  • 5
    • 0031630420 scopus 로고    scopus 로고
    • Isolation and expression of genes for hemicellulases from extremely thermophilic culturable and unculturable bacteria
    • Bergquist, P. L., M. D. Gibbs, D. J. Saul, R. A. Reeves, D. D. Morris, and V. S. J. Te'o. 1998. Isolation and expression of genes for hemicellulases from extremely thermophilic culturable and unculturable bacteria. Am. Chem. Soc. Symp. Ser. 687:155-167.
    • (1998) Am. Chem. Soc. Symp. Ser. , vol.687 , pp. 155-167
    • Bergquist, P.L.1    Gibbs, M.D.2    Saul, D.J.3    Reeves, R.A.4    Morris, D.D.5    Te'o, V.S.J.6
  • 6
    • 33748037939 scopus 로고
    • Amylases α and β
    • Bernfeld, P. 1955. Amylases α and β. Methods Enzymol. 1:149-158.
    • (1955) Methods Enzymol. , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 7
    • 0026043410 scopus 로고
    • The characterisation of a thermostable endo-β-1,4-mannanase cloned from "Caldocellum saccharolyticum."
    • Bicho, P. A., T. A. Clarke, K. Mackie, H. W. Morgan, and R. M. Daniel. 1991. The characterisation of a thermostable endo-β-1,4-mannanase cloned from "Caldocellum saccharolyticum." Appl. Microbiol. Biotechnol. 36:337-343.
    • (1991) Appl. Microbiol. Biotechnol. , vol.36 , pp. 337-343
    • Bicho, P.A.1    Clarke, T.A.2    Mackie, K.3    Morgan, H.W.4    Daniel, R.M.5
  • 8
    • 37049156324 scopus 로고
    • Universal buffer solutions and the dissociation constant of veronal
    • Britton, H. T. S., and R. A. Robinson. 1931. Universal buffer solutions and the dissociation constant of veronal. J. Chem. Soc. 1931:1456-1462.
    • (1931) J. Chem. Soc. , vol.1931 , pp. 1456-1462
    • Britton, H.T.S.1    Robinson, R.A.2
  • 9
    • 0030980654 scopus 로고    scopus 로고
    • Structure of the Clostridium stercorarium gene celY encoding the exo-1,4-β-glucanase Avicelase II
    • Bronnenmeier, K., K. Kundt, K. Riedel, W. H. Schwarz, and W. L. Staudenbauer. 1997. Structure of the Clostridium stercorarium gene celY encoding the exo-1,4-β-glucanase Avicelase II. Microbiology 143:891-898.
    • (1997) Microbiology , vol.143 , pp. 891-898
    • Bronnenmeier, K.1    Kundt, K.2    Riedel, K.3    Schwarz, W.H.4    Staudenbauer, W.L.5
  • 10
    • 0000303804 scopus 로고
    • The role of Trichoderma reesei xylanase and mannanase in the treatment of softwood kraft pulp prior to bleaching
    • Buchert, J., J. Salminen, M. Siika-Aho, M. Ranua, and L. Viikari. 1993. The role of Trichoderma reesei xylanase and mannanase in the treatment of softwood kraft pulp prior to bleaching. Holzforschung 47:473-478.
    • (1993) Holzforschung , vol.47 , pp. 473-478
    • Buchert, J.1    Salminen, J.2    Siika-Aho, M.3    Ranua, M.4    Viikari, L.5
  • 11
    • 0023504697 scopus 로고
    • Expression of leucine genes from an extremely thermophilic bacterium in Escherichia coli
    • Croft, J. E., D. R. Love, and P. L. Bergquist. 1987. Expression of leucine genes from an extremely thermophilic bacterium in Escherichia coli. Mol. Gen. Genet. 210:490-497.
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 490-497
    • Croft, J.E.1    Love, D.R.2    Bergquist, P.L.3
  • 12
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 13
    • 0031023550 scopus 로고    scopus 로고
    • Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic euhacterium Thermotoga neapolitana 5068
    • Duffaud, G. D., C. M. McCutchen, P. Leduc, K. N. Parker, and R. M. Kelly. 1997. Purification and characterization of extremely thermostable β-mannanase, β-mannosidase, and α-galactosidase from the hyperthermophilic euhacterium Thermotoga neapolitana 5068. App. Environ. Microbiol. 63: 169-177.
    • (1997) App. Environ. Microbiol. , vol.63 , pp. 169-177
    • Duffaud, G.D.1    McCutchen, C.M.2    Leduc, P.3    Parker, K.N.4    Kelly, R.M.5
  • 14
    • 0031734221 scopus 로고    scopus 로고
    • Gene cloning, DNA sequencing, and expression of thermostable β-mannanase from Bacillus stearothemophilus
    • Ethier, N., G. Talbot, and J. Sygusch. 1998. Gene cloning, DNA sequencing, and expression of thermostable β-mannanase from Bacillus stearothemophilus. Appl. Environ. Microbiol. 64:4428-4432.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4428-4432
    • Ethier, N.1    Talbot, G.2    Sygusch, J.3
  • 15
    • 0141596730 scopus 로고    scopus 로고
    • Isolation and characterization of the 54-kDa and 22-kDa chitinase genes of Serratia marcescens KCTC2172
    • Gal, S. W., J. Y. Choi, C. Y. Kim, Y. H. Cheong, Y. J. Choi, J. D. Bahk, S. Y. Lee, and M. J. Cho. 1997. Isolation and characterization of the 54-kDa and 22-kDa chitinase genes of Serratia marcescens KCTC2172. FEMS Microbiol. Lett. 151:197-204.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 197-204
    • Gal, S.W.1    Choi, J.Y.2    Kim, C.Y.3    Cheong, Y.H.4    Choi, Y.J.5    Bahk, J.D.6    Lee, S.Y.7    Cho, M.J.8
  • 16
    • 0030907121 scopus 로고    scopus 로고
    • Two genes encoding an endoglucanase and a cellulose-binding protein are clustered and co-regulated by a TTA codon in Streptomyces halstedii JM8
    • Garda, A. L., J. M. Fernández-Abalos, P. Sánchez, A. Ruiz-Arribas, and R. I. Santamaria. 1997. Two genes encoding an endoglucanase and a cellulose-binding protein are clustered and co-regulated by a TTA codon in Streptomyces halstedii JM8. Biochem. J. 324:403-411.
    • (1997) Biochem. J. , vol.324 , pp. 403-411
    • Garda, A.L.1    Fernández-Abalos, J.M.2    Sánchez, P.3    Ruiz-Arribas, A.4    Santamaria, R.I.5
  • 17
    • 0030585812 scopus 로고    scopus 로고
    • Sequencing, cloning and expression of the β-1.4 mannanase gene, manA. From the extremely thermophilic anaerobic bacterium, Caldicellulosiruptor Rt8B.4
    • Gibbs, M. D., A. U. Elinder, R. A. Reeves, and P. L. Bergquist. 1996 Sequencing, cloning and expression of the β-1.4 mannanase gene, manA. from the extremely thermophilic anaerobic bacterium, Caldicellulosiruptor Rt8B.4. FEMS Microbiol. Lett. 141:37-43.
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 37-43
    • Gibbs, M.D.1    Elinder, A.U.2    Reeves, R.A.3    Bergquist, P.L.4
  • 18
    • 0032758047 scopus 로고    scopus 로고
    • Sequencing and expression of a β-mannanase gene from the extreme thermophile Dictyoglomus thermophilum Rt46B.1, and characteristics of the recombinant enzyme
    • Gibbs, M. D., R. A. Reeves, A. Sunna, and P. L. Bergquist. 1999. Sequencing and expression of a β-mannanase gene from the extreme thermophile Dictyoglomus thermophilum Rt46B.1, and characteristics of the recombinant enzyme. Curr. Microbiol. 39:351-357.
    • (1999) Curr. Microbiol. , vol.39 , pp. 351-357
    • Gibbs, M.D.1    Reeves, R.A.2    Sunna, A.3    Bergquist, P.L.4
  • 19
    • 0026446665 scopus 로고
    • The β-mannanase from "Caldocellum saccharolyticum" is part of a muitidomain enzyme
    • Gibbs, M. D., D. J. Saul, E. Lüthi, and P. L. Bergquist. 1992 The β-mannanase from "Caldocellum saccharolyticum" is part of a muitidomain enzyme. Appl. Environ. Microbiol. 58:3864-3867.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3864-3867
    • Gibbs, M.D.1    Saul, D.J.2    Lüthi, E.3    Bergquist, P.L.4
  • 20
    • 0023704964 scopus 로고
    • Homology between endoglucanase Z of Erwinia chrysanthemi and endoglucanases of Bacillus subtilis and alkalophilic Bacillus
    • Guiseppi, A., B. Cami, J.-L. Aymeric, G. Ball, and N. Creuzet. 1988. Homology between endoglucanase Z of Erwinia chrysanthemi and endoglucanases of Bacillus subtilis and alkalophilic Bacillus. Mol. Microbiol. 2:159-164.
    • (1988) Mol. Microbiol. , vol.2 , pp. 159-164
    • Guiseppi, A.1    Cami, B.2    Aymeric, J.-L.3    Ball, G.4    Creuzet, N.5
  • 21
    • 0026734330 scopus 로고
    • celA from Bacillus lautus PL236 encodes a novel cellulose-binding endo-β-1,4-glucanase
    • Hansen, C. K., B. Diderichsen, and P. L. Jørgensen. 1992.celA from Bacillus lautus PL236 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    Jørgensen, P.L.3
  • 22
    • 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
  • 23
    • 0032533450 scopus 로고    scopus 로고
    • High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca - Substrate specificity in glycosyl hydrolase family 5
    • Hilge, M., S. M. Gloor, W. Rypniewski, O. Sauer, T. D. Heightman, W. Zimmermann, K. Winterhalter, and K. Pionlek. 1998. High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5. Structure 6:1433-1444.
    • (1998) Structure , vol.6 , pp. 1433-1444
    • Hilge, M.1    Gloor, S.M.2    Rypniewski, W.3    Sauer, O.4    Heightman, T.D.5    Zimmermann, W.6    Winterhalter, K.7    Pionlek, K.8
  • 24
    • 0000791101 scopus 로고
    • Proposed mechanism of the enzymatic bleaching of kraft pulp with xylanases
    • Kantelinen, A., B. Hortling, J. Sundquist, M. Linko, and L. Viikari. 1993. Proposed mechanism of the enzymatic bleaching of kraft pulp with xylanases. Holzforschung 47:318-324.
    • (1993) Holzforschung , vol.47 , pp. 318-324
    • Kantelinen, A.1    Hortling, B.2    Sundquist, J.3    Linko, M.4    Viikari, L.5
  • 25
    • 0031780384 scopus 로고    scopus 로고
    • The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene
    • Kolbe, S., S. Fischer, A. Becirevic, P. Hinz, and H. Schrempf. 1998. The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene. Microbiology 144:1291-1297.
    • (1998) Microbiology , vol.144 , pp. 1291-1297
    • Kolbe, S.1    Fischer, S.2    Becirevic, A.3    Hinz, P.4    Schrempf, H.5
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • London
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0027523710 scopus 로고
    • Identification of an essential glutamate residue in the active site of endoglucanase III from Trichoderma reesei
    • Macarron, R., J. van Beeumen, B. Henrissat, I. de la Mata, and M. Claeyssens. 1993. Identification of an essential glutamate residue in the active site of endoglucanase III from Trichoderma reesei. FEBS Lett. 316:137-140.
    • (1993) FEBS Lett. , vol.316 , pp. 137-140
    • Macarron, R.1    Van Beeumen, J.2    Henrissat, B.3    De La Mata, I.4    Claeyssens, M.5
  • 30
    • 0000197084 scopus 로고
    • Enzymic interactions in the hydrolysis of galactomannan in germinating guar: The role of exo-β-mannanase
    • McCleary, B. V. 1983. Enzymic interactions in the hydrolysis of galactomannan in germinating guar: the role of exo-β-mannanase. Phytochemistry 22: 649-658.
    • (1983) Phytochemistry , vol.22 , pp. 649-658
    • McCleary, B.V.1
  • 32
    • 0033136098 scopus 로고    scopus 로고
    • Family 10 and 11 xylanase genes from Caldicellulosiruptor sp. Rt69B.1
    • Morris, D. D., M. D. Gibbs, M. Ford, J. Thomas, and P. L. Bergquist. 1999. Family 10 and 11 xylanase genes from Caldicellulosiruptor sp. Rt69B.1. Extremophiles 3:103-111.
    • (1999) Extremophiles , vol.3 , pp. 103-111
    • Morris, D.D.1    Gibbs, M.D.2    Ford, M.3    Thomas, J.4    Bergquist, P.L.5
  • 33
    • 0028990024 scopus 로고
    • Correction of the β-mannanase domain of the celC pseudogene from Caldicellulosiruptor saccharolyticus and activity of the gene product on kraft pulp
    • Morris, D. D., R. A. Reeves, M. D. Gibbs, D. J. Saul, and P. L. Bergquist. 1995. Correction of the β-mannanase domain of the celC pseudogene from Caldicellulosiruptor saccharolyticus and activity of the gene product on kraft pulp. Appl. Environ. Microbiol. 61:2262-2269.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2262-2269
    • Morris, D.D.1    Reeves, R.A.2    Gibbs, M.D.3    Saul, D.J.4    Bergquist, P.L.5
  • 34
    • 0031535476 scopus 로고    scopus 로고
    • Chemistry and biochemistry of hemicelluloses - Relationship between hemicellulose structure and enzymes required for hydrolysis
    • Puls, J. 1997. Chemistry and biochemistry of hemicelluloses - relationship between hemicellulose structure and enzymes required for hydrolysis. Macromol. Symp. 120:183-196.
    • (1997) Macromol. Symp. , vol.120 , pp. 183-196
    • Puls, J.1
  • 35
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomycts coelicolor A3(2) chromosome
    • Redenbach, M., H. M. Kieser, D. Denapaite, A. Eichner, J. Cullum, H. Kinashi, and D. A. Hopwood. 1996. A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomycts coelicolor A3(2) chromosome. Mol. Microbiol. 21:77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1    Kieser, H.M.2    Denapaite, D.3    Eichner, A.4    Cullum, J.5    Kinashi, H.6    Hopwood, D.A.7
  • 36
    • 0023254924 scopus 로고
    • Inducible expression vectors incorporating the Escherichia coli atpE transcriptional initiation region
    • Schauder, B., H. Blöcker, R. Frank, and J. E. G. McCarthy. 1987. Inducible expression vectors incorporating the Escherichia coli atpE transcriptional initiation region. Gene 52:279-283.
    • (1987) Gene , vol.52 , pp. 279-283
    • Schauder, B.1    Blöcker, H.2    Frank, R.3    McCarthy, J.E.G.4
  • 37
    • 0028070108 scopus 로고
    • The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms
    • Schnellmann, J., A. Zeltins, H. Blaak, and H. Schrempf. 1994. The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline α-chitin of fungi and other organisms. Mol. Microbiol. 13:807-819.
    • (1994) Mol. Microbiol. , vol.13 , pp. 807-819
    • Schnellmann, J.1    Zeltins, A.2    Blaak, H.3    Schrempf, H.4
  • 41
  • 42
    • 0031000697 scopus 로고    scopus 로고
    • Cloning, DNA sequencing, and expression of the beta-1,4-mannanase gene from a marine Vibrio sp. strain MA-138
    • Tamaru, Y., T. Araki, T. Morishita, T. Kimura, K. Sakka, and K. Ohmiya. 1997. Cloning, DNA sequencing, and expression of the beta-1,4-mannanase gene from a marine Vibrio sp. strain MA-138. J. Ferment. Bioeng. 83:201-205.
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 201-205
    • Tamaru, Y.1    Araki, T.2    Morishita, T.3    Kimura, T.4    Sakka, K.5    Ohmiya, K.6
  • 43
    • 0020032328 scopus 로고
    • Use of Congo red polysaccharide interaction in enumeration and characterization of cellulolytic bacteria from the bovine rumen
    • Teather, R,. M., and P. J. Wood. 1982. Use of Congo red polysaccharide interaction in enumeration and characterization of cellulolytic bacteria from the bovine rumen. Appl. Environ. Microbiol. 43:777-780.
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 777-780
    • Teather, R.M.1    Wood, P.J.2
  • 44
    • 0032955632 scopus 로고    scopus 로고
    • Multiple genes involved in chitin degradation from the marine bacterium Pseudoalteromonas sp. strain S91
    • Techkarnjanaruk, S., and A. E. Goodman. 1999. Multiple genes involved in chitin degradation from the marine bacterium Pseudoalteromonas sp. strain S91. Microbiology 145:925-934.
    • (1999) Microbiology , vol.145 , pp. 925-934
    • Techkarnjanaruk, S.1    Goodman, A.E.2
  • 45
    • 0001594653 scopus 로고
    • Cellulose-binding domains: Classification and properties
    • J. N. Saddler and M. H. Penner (ed.), American Chemical Society, Washington, D.C.
    • Tomme, P., R. A. J. Warren, R. C. J. Miller, D. G. Kilburn, and N. R. Gilkes. 1995. Cellulose-binding domains: classification and properties, p. 142-163. In J. N. Saddler and M. H. Penner (ed.), Enzymatic degradation of insoluble carbohydrates. American Chemical Society, Washington, D.C.
    • (1995) Enzymatic Degradation of Insoluble Carbohydrates , pp. 142-163
    • Tomme, P.1    Warren, R.A.J.2    Miller, R.C.J.3    Kilburn, D.G.4    Gilkes, N.R.5
  • 46
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo, J., R. Lamed, A. J. Chirino, E. Morag, E. A. Bayer, Y. Shoham, and T. A. Steitz. 1996. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 15: 5739-5751.
    • (1996) EMBO J. , vol.15 , 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
  • 48
    • 0000744115 scopus 로고
    • Xylanase enzymes promote pulp bleaching
    • Viikari, L., J. Sundquist, and J. Kettunen. 1991. Xylanase enzymes promote pulp bleaching. Paper Timber 5:384-389.
    • (1991) Paper Timber , vol.5 , pp. 384-389
    • Viikari, L.1    Sundquist, J.2    Kettunen, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.