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Volumn 64, Issue 11, 1998, Pages 4428-4432

Gene cloning, DNA sequencing, and expression of thermostable β- mannanase from Bacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

BETA MANNOSIDASE;

EID: 0031734221     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.11.4428-4432.1998     Document Type: Article
Times cited : (46)

References (55)
  • 1
    • 0024377332 scopus 로고
    • Two Bacillus β-mannanases having different COOH termini are produced in Escherichia coli carrying pMAH5
    • Akino, T., C. Kato, and K. Horikoshi. 1989. Two Bacillus β-mannanases having different COOH termini are produced in Escherichia coli carrying pMAH5. Appl. Environ. Microbiol. 55:3178-3183.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 3178-3183
    • Akino, T.1    Kato, C.2    Horikoshi, K.3
  • 2
    • 0025375675 scopus 로고
    • Hemicellulases of Bacillus species: Preliminary comparative studies on production and properties of mannanases and galactanases
    • Araujo, A., and O. P. Ward. 1990. Hemicellulases of Bacillus species: preliminary comparative studies on production and properties of mannanases and galactanases. J. Appl. Bacteriol. 68:253-261.
    • (1990) J. Appl. Bacteriol. , vol.68 , pp. 253-261
    • Araujo, A.1    Ward, O.P.2
  • 3
    • 0027471408 scopus 로고
    • Mannanase of Streptomyces lividans 66: Cloning and DNA sequence of the manA gene and characterization of the enzyme
    • Arcand, N., D. Kluepfel, F. D. 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.D.3    Morosoli, R.4    Shareck, F.5
  • 4
    • 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
  • 5
    • 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
  • 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
    • 0026817470 scopus 로고
    • Purification of recombinant antigenic epitopes of the human 68-kDa (U1) ribonucleoprotein antigen using the expression system pH6EX3 followed by metal chelating affinity chromatography
    • Berthold, H., M. Scanarini, C. C. Abney, B. Frorath, and W. Northemann. 1992. Purification of recombinant antigenic epitopes of the human 68-kDa (U1) ribonucleoprotein antigen using the expression system pH6EX3 followed by metal chelating affinity chromatography. Protein Expr. Purif. 3:50-56.
    • (1992) Protein Expr. Purif. , vol.3 , pp. 50-56
    • Berthold, H.1    Scanarini, M.2    Abney, C.C.3    Frorath, B.4    Northemann, W.5
  • 8
    • 15644372258 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding a (1-4)-β-mannan endohydrolase from the seeds of germinated tomato (Lycopersicon esculentum)
    • Bewley, J. D., R. A. Burton, Y. Morohashi, and G. B. Fincher. 1997. Molecular cloning of a cDNA encoding a (1-4)-β-mannan endohydrolase from the seeds of germinated tomato (Lycopersicon esculentum). Planta 203:454-459.
    • (1997) Planta , vol.203 , pp. 454-459
    • Bewley, J.D.1    Burton, R.A.2    Morohashi, Y.3    Fincher, G.B.4
  • 9
    • 0028985356 scopus 로고
    • A non-modular endo-β-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa
    • Braithwaite, K. L., G. W. Black, G. P. Hazlewood, B. R. S. Ali, and H. J. Gilbert. 1995. A non-modular endo-β-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa. Biochem. J. 305:1005-1010.
    • (1995) Biochem. J. , vol.305 , pp. 1005-1010
    • Braithwaite, K.L.1    Black, G.W.2    Hazlewood, G.P.3    Ali, B.R.S.4    Gilbert, H.J.5
  • 11
    • 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
  • 13
    • 0028146008 scopus 로고
    • Expression, cloning, purification and characterization of a β-1,4-mannanase from Aspergillus aculeatus
    • Christgau, S., S. Kauppinen, J. Vind, L. V. Kofod, and H. Dalbøge. 1994. Expression, cloning, purification and characterization of a β-1,4-mannanase from Aspergillus aculeatus. Biochem. Mol. Biol. Int. 33:917-925.
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 917-925
    • Christgau, S.1    Kauppinen, S.2    Vind, J.3    Kofod, L.V.4    Dalbøge, H.5
  • 14
    • 0011956915 scopus 로고
    • Mannanase and xylanase treatment of softwood chemical pulps: Effects on pulp properties and bleachability
    • T. K. Kirk and H. M. Chang (ed.), Butterworth-Heineman, Toronto, Canada
    • Clark, T. A., A. G. McDonald, D. J. Senior, and P. R. Mayers. 1990. Mannanase and xylanase treatment of softwood chemical pulps: effects on pulp properties and bleachability, p. 153-167. In T. K. Kirk and H. M. Chang (ed.), Biotechnology in pulp and paper manufacture. Butterworth-Heineman, Toronto, Canada.
    • (1990) Biotechnology in Pulp and Paper Manufacture , pp. 153-167
    • Clark, T.A.1    McDonald, A.G.2    Senior, D.J.3    Mayers, P.R.4
  • 15
    • 0016906505 scopus 로고
    • Hemicellulases: Their occurrence. Purification, properties and mode of action
    • Dekker, R. F., and G. N. Richards. 1976. Hemicellulases: their occurrence. purification, properties and mode of action. Adv. Carbohydr. Chem. Biochem. 32:277-352.
    • (1976) Adv. Carbohydr. Chem. Biochem. , vol.32 , pp. 277-352
    • Dekker, R.F.1    Richards, G.N.2
  • 16
    • 0028786027 scopus 로고
    • The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain
    • Fanutti, C., T. Ponyi, G. W. Black, G. P. Hazlewood, and H. J. Gilbert. 1995 The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain. J. Biol. Chem. 270:29314-29322.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29314-29322
    • Fanutti, C.1    Ponyi, T.2    Black, G.W.3    Hazlewood, G.P.4    Gilbert, H.J.5
  • 17
    • 0023096671 scopus 로고
    • Truncation analysis of an alkaline cellulase from an alkalophilic Bacillus species
    • Fukumori, F., T. Kudo, and K. Horikoshi. 1987. Truncation analysis of an alkaline cellulase from an alkalophilic Bacillus species. FEMS Microbiol. Lett 40:311-314.
    • (1987) FEMS Microbiol. Lett , vol.40 , pp. 311-314
    • Fukumori, F.1    Kudo, T.2    Horikoshi, K.3
  • 19
    • 0026446665 scopus 로고
    • The β-mannanase from "Caldocellum saccharolyticum" is part of a multidomam enzyme
    • Gibbs, M. D., D. J. Saul, E. Lüthi, and P. L. Bergquist. 1992. The β-mannanase from "Caldocellum saccharolyticum" is part of a multidomam 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
    • 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. 141:37-13.
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 37-113
    • Gibbs, M.D.1    Elinder, A.U.2    Reeves, R.A.3    Bergquist, P.L.4
  • 21
    • 0028984077 scopus 로고
    • Purification and characterization of α-L-arabinofuranosidase from Bacillus stearothermophilus T-6
    • Gilead, S. and Y. Shoham. 1995. Purification and characterization of α-L-arabinofuranosidase from Bacillus stearothermophilus T-6. Appl. Environ. Microbiol. 61:170-174.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 170-174
    • Gilead, S.1    Shoham, Y.2
  • 22
    • 0023704964 scopus 로고
    • Homology between endoglucanase Z of Erwinia chrysanthemi and endoglucanases at 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 at 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
  • 23
    • 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
  • 24
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • Khasin, A., I. Alchanati, and Y. Shoham. 1993. Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6. Appl. Environ. Microbiol. 59:1725-1730.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1725-1730
    • Khasin, A.1    Alchanati, I.2    Shoham, Y.3
  • 25
    • 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
  • 26
    • 0025877830 scopus 로고
    • Cloning sequence analysis, and expression in Escherichia coli of a gene coding for a β-mannanase from extremely thermophilic bacterium "Caldocellum saccharolyticum."
    • Lüthi, E., N. B. Jasmat, R. A. Grayling, D. R. Love, and P. L. Bergquist. 1991. Cloning sequence analysis, and expression in Escherichia coli of a gene coding for a β-mannanase from extremely thermophilic bacterium "Caldocellum saccharolyticum." Appl. Environ. Microbiol. 57:694-700.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 694-700
    • Lüthi, E.1    Jasmat, N.B.2    Grayling, R.A.3    Love, D.R.4    Bergquist, P.L.5
  • 27
    • 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
  • 29
    • 0001174333 scopus 로고
    • β-D-Mannanases
    • McCleary, B. V. 1988. β-D-Mannanases. Methods Enzymol. 160:596-610.
    • (1988) Methods Enzymol. , vol.160 , pp. 596-610
    • McCleary, B.V.1
  • 32
    • 0030221824 scopus 로고    scopus 로고
    • Evidence that the piromyces gene family encoding endo-1,4-mannanase arose through gene duplication
    • Millward-Sadler, S. J., J. Hall, G. W. Black, G. P. Hazlewood, and H. J. Gilbert. 1996. Evidence that the piromyces gene family encoding endo-1,4-mannanase arose through gene duplication. FEMS Microhiol. Lett. 141:183-188.
    • (1996) FEMS Microhiol. Lett. , vol.141 , pp. 183-188
    • Millward-Sadler, S.J.1    Hall, J.2    Black, G.W.3    Hazlewood, G.P.4    Gilbert, H.J.5
  • 33
    • 0028990024 scopus 로고
    • Correction of the β-mannanase domain of the celC pseudogene from Caldocellulosiruptor 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 Caldocellulosiruptor 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
    • 0025608736 scopus 로고
    • Purification and properties of thermostable xylanase and β-xylosidase produced by a newly isolated Bacillus stearothermophilus strain
    • Nanmori, T., T. Watanabe, R. Shinke, A. Kohno, and Y. Kawamura. 1990. Purification and properties of thermostable xylanase and β-xylosidase produced by a newly isolated Bacillus stearothermophilus strain. J. Bacteriol. 172:6669-6672.
    • (1990) J. Bacteriol. , vol.172 , pp. 6669-6672
    • Nanmori, T.1    Watanabe, T.2    Shinke, R.3    Kohno, A.4    Kawamura, Y.5
  • 35
    • 0025810284 scopus 로고
    • Secretion incompetence of bovine pancreatic trypsin inhibitor expressed in Escherichia coli
    • Nilsson, B., C. Bermar-Marks, I. D. Kuntz, and S. Anderson. 1991. Secretion incompetence of bovine pancreatic trypsin inhibitor expressed in Escherichia coli. J. Biol. Chem. 266:2970-2977.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2970-2977
    • Nilsson, B.1    Bermar-Marks, C.2    Kuntz, I.D.3    Anderson, S.4
  • 36
    • 0020638192 scopus 로고
    • A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides
    • Perlman, D., and H. O. Halvorson. 1983. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J. Mol. Biol. 167:391-409.
    • (1983) J. Mol. Biol. , vol.167 , pp. 391-409
    • Perlman, D.1    Halvorson, H.O.2
  • 37
    • 0022555852 scopus 로고
    • Transcription termination and the regulation of gene expression
    • Platt, T. 1986. Transcription termination and the regulation of gene expression. Annu. Rev. Biochem. 55:339-372.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 339-372
    • Platt, T.1
  • 40
    • 0010496060 scopus 로고
    • Fundamental investigations on the reaction of xylanases and mannanases on sprucewood chemical pulps
    • Beijing, China
    • Saake, B., T. A. Clark, and J. Puls. 1993. Fundamental investigations on the reaction of xylanases and mannanases on sprucewood chemical pulps, p. 605-613. In The Seventh International Symposium of Wood Pulping Chemistry. Beijing, China.
    • (1993) The Seventh International Symposium of Wood Pulping Chemistry , pp. 605-613
    • Saake, B.1    Clark, T.A.2    Puls, J.3
  • 43
    • 0028932041 scopus 로고
    • Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain
    • Stålbrand, H., A. Saloheimo, J. Vehmaanperä, B. Henrissat, and M. Penttilä. 1995. Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain. Appl. Environ. Microbiol. 61:1090-1097.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1090-1097
    • Stålbrand, H.1    Saloheimo, A.2    Vehmaanperä, J.3    Henrissat, B.4    Penttilä, M.5
  • 46
    • 0025002095 scopus 로고
    • Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus
    • Talbot, G., and J. Sygusch. 1990. Purification and characterization of thermostable β-mannanase and α-galactosidase from Bacillus stearothermophilus. Appl. Environ. Microbiol. 56:3505-3510.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3505-3510
    • Talbot, G.1    Sygusch, J.2
  • 47
    • 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
  • 49
    • 0000744115 scopus 로고
    • Xylanase enzymes promote pulp bleaching
    • Viikari, L. 1991. Xylanase enzymes promote pulp bleaching. Pap. Timber 5:384-389.
    • (1991) Pap. Timber , vol.5 , pp. 384-389
    • Viikari, L.1
  • 51
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • von Heijne, G. 1985. Signal sequences. The limits of variation. J. Mol. Biol. 184:99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 53
    • 0031018728 scopus 로고    scopus 로고
    • Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with similarity to fungal cellobiohydrolase I and β-mannanase, respectively, is regulated by the carbon source
    • Yagüe, E., M. Mehak-Zunic, L. Morgan, D. A. Wood, and C. F. Thurston. 1997. Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with similarity to fungal cellobiohydrolase I and β-mannanase, respectively, is regulated by the carbon source. Microbiology 143:239-244.
    • (1997) Microbiology , vol.143 , pp. 239-244
    • Yagüe, E.1    Mehak-Zunic, M.2    Morgan, L.3    Wood, D.A.4    Thurston, C.F.5
  • 54
    • 0011213735 scopus 로고
    • Molecular cloning and expression of a xylanase gene from Bacillus polymyxa in Escherichia coli
    • Yang, R. C. A., C. R. MacKenzie, D. Bilous, V. L. Seligy, and S. A. Narang. 1988. Molecular cloning and expression of a xylanase gene from Bacillus polymyxa in Escherichia coli. Appl. Environ. Microbiol. 54:1023-1029.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1023-1029
    • Yang, R.C.A.1    MacKenzie, C.R.2    Bilous, D.3    Seligy, V.L.4    Narang, S.A.5


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