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Volumn 20, Issue 5, 2010, Pages 893-903

A cellulolytic and xylanolytic enzyme complex from an alkalothermoanaerobacterium, Tepidimicrobium xylanilyticum BT14

Author keywords

Alkalothermoanaerobacterium; Cellulolytic and xylanolytic enzyme complex; Corn hull; Ethanol; Tepidimicrobium xylanilyticum

Indexed keywords

ACETIC ACID; ALCOHOL; BACTERIAL RNA; CELLULASE; COHESIN; MICROCRYSTALLINE CELLULOSE; RNA 16S; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 77955011149     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0911.11025     Document Type: Article
Times cited : (29)

References (52)
  • 2
    • 33845954264 scopus 로고    scopus 로고
    • Application of cellulases from an alkalothermophilic Thermomonospora sp. in biopolishing of denims
    • Anish, R., M. S. Rahman, and M. Rao. 2007. Application of cellulases from an alkalothermophilic Thermomonospora sp. in biopolishing of denims. Biotechnol. Bioeng. 96: 48-56.
    • (2007) Biotechnol. Bioeng , vol.96 , pp. 48-56
    • Anish, R.1    Rahman, M.S.2    Rao, M.3
  • 3
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer, E. A., J.-P. Belaich, Y. Shoham, and R. Lamed. 2004. The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides. Annu. Rev. Microbiol. 58: 521-554.
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.-P.2    Shoham, Y.3    Lamed, R.4
  • 4
    • 0021078758 scopus 로고
    • Adherence of Clostridium thermocellum to cellulose
    • Bayer, E. A., R. Kenig, and R. Lamed. 1983. Adherence of Clostridium thermocellum to cellulose. J. Bacteriol. 156: 818-827.
    • (1983) J. Bacteriol , vol.156 , pp. 818-827
    • Bayer, E.A.1    Kenig, R.2    Lamed, R.3
  • 5
    • 0027984011 scopus 로고
    • The cellulosome -a treasure-trove for biotechnology
    • Bayer, E. A., E. Morag, and R. Lamed. 1994. The cellulosome-a treasure-trove for biotechnology. Trends Biotechnol. 12: 379-386.
    • (1994) Trends Biotechnol , vol.12 , pp. 379-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 6
    • 33750319406 scopus 로고    scopus 로고
    • Effect of sulfur-containing compounds on Bacillus cellulosome-associated 'CMCase' and 'avicelase' activities
    • Beukes, N. and B. I. Pletschke. 2006. Effect of sulfur-containing compounds on Bacillus cellulosome-associated 'CMCase' and 'avicelase' activities. FEMS Microbiol. Lett. 264: 226-231.
    • (2006) FEMS Microbiol. Lett , vol.264 , pp. 226-231
    • Beukes, N.1    Pletschke, B.I.2
  • 7
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degrading enzymes and their potential industrial applications
    • Bhat, M. K. and S. Bhat. 1997. Cellulose degrading enzymes and their potential industrial applications. Biotechnol. Adv. 15: 583-620.
    • (1997) Biotechnol. Adv , vol.15 , pp. 583-620
    • Bhat, M.K.1    Bhat, S.2
  • 9
    • 36949013920 scopus 로고    scopus 로고
    • Effect of multiple copies of cohesins on cellulase and hemicellulase activities of Clostridium cellulovorans mini-cellulosomes
    • Cha, J., S. Matsuoka, H. Chan, H. Yukawa, M. Inui, and R. H. Doi. 2007. Effect of multiple copies of cohesins on cellulase and hemicellulase activities of Clostridium cellulovorans mini-cellulosomes. J. Microbiol. Biotechnol. 17: 1782-1788.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 1782-1788
    • Cha, J.1    Matsuoka, S.2    Chan, H.3    Yukawa, H.4    Inui, M.5    Doi, R.H.6
  • 11
    • 3142757398 scopus 로고    scopus 로고
    • Cellulosomes: Plant-cell-wall-degrading enzyme complexes
    • Doi, R. H. and A. Kosugi. 2004. Cellulosomes: Plant-cell-wall-degrading enzyme complexes. Nat. Rev. Microbiol. 2: 541-551.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 541-551
    • Doi, R.H.1    Kosugi, A.2
  • 12
    • 0030841646 scopus 로고    scopus 로고
    • Clostridium thermocellum JW20 (ATCC 31549) is a coculture with Thermoanaerobacter ethanolicus
    • Erbeznik, M., C. Jones, K. Dawson, and H. Strobel. 1997. Clostridium thermocellum JW20 (ATCC 31549) is a coculture with Thermoanaerobacter ethanolicus. Appl. Environ. Microbiol. 63: 2949-2951.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 2949-2951
    • Erbeznik, M.1    Jones, C.2    Dawson, K.3    Strobel, H.4
  • 13
    • 33750019696 scopus 로고    scopus 로고
    • Isolation and characterization of two novel ethanol-tolerant facultative-anaerobic thermophilic bacteria strains from waste compost
    • Fong, J. C. N., C. J. Svenson, K. Nakasugi, C. T. C. Leong, J. P. Bowman, B. Chen, D. R. Glenn, B. A. Neilan, and P. L. Rogers. 2006. Isolation and characterization of two novel ethanol-tolerant facultative-anaerobic thermophilic bacteria strains from waste compost. Extremophiles 10: 363-372.
    • (2006) Extremophiles , vol.10 , pp. 363-372
    • Fong, J.C.N.1    Svenson, C.J.2    Nakasugi, K.3    Leong, C.T.C.4    Bowman, J.P.5    Chen, B.6    Glenn, D.R.7    Neilan, B.A.8    Rogers, P.L.9
  • 14
    • 0000738385 scopus 로고    scopus 로고
    • Endospore-forming Gram-positive rods and cocci
    • D. Claus and R. C. W. Berkerley (eds.), Springer Press, Baltimore
    • Garrity, G. 2001. Endospore-forming Gram-positive rods and cocci, pp. 1104-1207. In D. Claus and R. C. W. Berkerley (eds.). Bergey's Manual of Systematic Bacteriology, Vol. 2. Springer Press, Baltimore.
    • (2001) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1104-1207
    • Garrity, G.1
  • 15
    • 0035314559 scopus 로고    scopus 로고
    • Studies on carboxymethyl cellulase produced by an alkalothermophilic actinomycete
    • George, S. P., A. Ahmad, and M. B. Rao. 2001. Studies on carboxymethyl cellulase produced by an alkalothermophilic actinomycete. Bioresource Technol. 77: 171-175.
    • (2001) Bioresource Technol , vol.77 , pp. 171-175
    • George, S.P.1    Ahmad, A.2    Rao, M.B.3
  • 18
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles: Some applications of their products for biotechnology. Microbiol
    • Horikoshi, K. 1999. Alkaliphiles: Some applications of their products for biotechnology. Microbiol. Mol. Biol. Rev. 63: 735-750.
    • (1999) Mol. Biol. Rev , vol.63 , pp. 735-750
    • Horikoshi, K.1
  • 19
    • 77956868541 scopus 로고
    • A roll tube method for cultivation of strict anaerobes
    • J. R. Norris and D. W. Ribbons (eds.), Academic Press Inc., New York
    • Hungate, R. E. 1969. A roll tube method for cultivation of strict anaerobes, pp. 117-132. In J. R. Norris and D. W. Ribbons (eds.). Methods in Microbiology, Vol. 3B. Academic Press Inc., New York.
    • (1969) Methods in Microbiology , vol.3 B , pp. 117-132
    • Hungate, R.E.1
  • 20
    • 13844256879 scopus 로고    scopus 로고
    • Purification and properties of a low molecular weight 1,4-[3-D-glucan glucohydrolase having one active site for carboxymethyl cellulose and xylan from an alkalothermophilic Thermomonospora sp
    • Jagtap, S. and M. Rao. 2005. Purification and properties of a low molecular weight 1,4-[3-D-glucan glucohydrolase having one active site for carboxymethyl 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
  • 21
    • 17844396234 scopus 로고    scopus 로고
    • Characterization of a novel, ultra-large xylanolytic complex (xylanosome) from Streptomyces olivaceoviridis E-86
    • Jiang, Z. Q., W. Deng, X. T. Li, Z. L. Ai, L. T. Li, and I. Kusakabe. 2005. Characterization of a novel, ultra-large xylanolytic complex (xylanosome) from Streptomyces olivaceoviridis E-86. Enzyme Microb. Technol. 36: 923-929.
    • (2005) Enzyme Microb. Technol , vol.36 , pp. 923-929
    • Jiang, Z.Q.1    Deng, W.2    Li, X.T.3    Ai, Z.L.4    Li, L.T.5    Kusakabe, I.6
  • 23
    • 0037639959 scopus 로고    scopus 로고
    • Towards a standardized format for the description of a novel species (of an established genus): Ochrobactrum gallinifaecis sp. nov
    • Kämpfer, P., S. Buczolits, A. Albrecht, H.-J. Busse, and E. Stackebrandt. 2003. Towards a standardized format for the description of a novel species (of an established genus): Ochrobactrum gallinifaecis sp. nov. Int. J. Syst. Evol. Microbiol. 53: 893-896.
    • (2003) Int. J. Syst. Evol. Microbiol , vol.53 , pp. 893-896
    • Kämpfer, P.1    Buczolits, S.2    Albrecht, A.3    Busse, H.-J.4    Stackebrandt, E.5
  • 24
    • 22144492290 scopus 로고    scopus 로고
    • Degradation of corn fiber by Clostridium cellulovorans cellulases and hemicellulases and contribution of scaffolding protein CbpA
    • Koukiekolo, R., H.-Y. Cho, A. Kosugi, M. Inui, H. Yukawa, and R. H. Doi. 2005. Degradation of corn fiber by Clostridium cellulovorans cellulases and hemicellulases and contribution of scaffolding protein CbpA. Appl. Environ. Microbiol. 71: 3504-3511.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 3504-3511
    • Koukiekolo, R.1    Cho, H.-Y.2    Kosugi, A.3    Inui, M.4    Yukawa, H.5    Doi, R.H.6
  • 26
    • 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 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0030814693 scopus 로고    scopus 로고
    • Thermoanaerobacter mathranii sp. nov., an ethanol-producing, extremely thermophilic anaerobic bacterium from a hot spring in Iceland
    • Larsen, L., P. Nielson, and B. K. Ahring. 1997. Thermoanaerobacter mathranii sp. nov., an ethanol-producing, extremely thermophilic anaerobic bacterium from a hot spring in Iceland. Arch. Microbiol. 168: 114-119.
    • (1997) Arch. Microbiol , vol.168 , pp. 114-119
    • Larsen, L.1    Nielson, P.2    Ahring, B.K.3
  • 29
    • 0038721163 scopus 로고    scopus 로고
    • Isolation and some properties of cellulose-degrading Vibrio sp. LX-3 with agar-liquefying ability from soil
    • Li, X., X. Dong, C. Zhao, Z. Chen, and F. Chen. 2003. Isolation and some properties of cellulose-degrading Vibrio sp. LX-3 with agar-liquefying ability from soil. World J. Microbiol. Biotechnol. 19: 375-379.
    • (2003) World. J. Microbiol. Biotechnol , vol.19 , pp. 375-379
    • Li, X.1    Dong, X.2    Zhao, C.3    Chen, Z.4    Chen, F.5
  • 30
    • 67349086113 scopus 로고    scopus 로고
    • Isolation and identification of a newly isolated Alternaria sp. ND-16 and characterization of xylanase
    • Li, Y., Z. Liu, F. Cui, L. Ping, C. Qiu, G. Li, and L. Yan. 2009. Isolation and identification of a newly isolated Alternaria sp. ND-16 and characterization of xylanase. Appl. Biochem. Biotechnol. 157: 36-49.
    • (2009) Appl. Biochem. Biotechnol , vol.157 , pp. 36-49
    • Li, Y.1    Liu, Z.2    Cui, F.3    Ping, L.4    Qiu, C.5    Li, G.6    Yan, L.7
  • 32
    • 0001387731 scopus 로고
    • Isolation and characterization of Clostridium stercorarium sp. nov., cellulolytic thermophile
    • Madden, R. H. 1983. Isolation and characterization of Clostridium stercorarium sp. nov., cellulolytic thermophile. Int. J. Syst. Bacteriol. 33: 837-840.
    • (1983) Int. J. Syst. Bacteriol , vol.33 , pp. 837-840
    • Madden, R.H.1
  • 33
    • 33748751574 scopus 로고    scopus 로고
    • A thermostable alkaline active endo-[3-1-4-xylanase from Bacillus halodurans S7: Purification and characterization
    • Mamo, G, R. Hatti-Kaul, and B. Mattiasson. 2006. A thermostable alkaline active endo-[3-1-4-xylanase from Bacillus halodurans S7: Purification and characterization. Enzyme Microb. Technol. 39: 1492-1498.
    • (2006) Enzyme Microb. Technol , vol.39 , pp. 1492-1498
    • Mamo, G.1    Hatti-Kaul, R.2    Mattiasson, B.3
  • 35
    • 0029635955 scopus 로고
    • Purification and characterization of a thermophilic alkaline xylanase from thermoalkaliphilic Bacillus sp. strain TAR-1
    • Nakamura, S., Y. Ishiguro, R. Nakai, K. Wakabayashi, R. Aono, and K. Horikoshi. 1995. Purification and characterization of a thermophilic alkaline xylanase from thermoalkaliphilic Bacillus sp. strain TAR-1. J. Mol. Catal. B Enz. 1: 7-15.
    • (1995) J. Mol. Catal. B Enz , vol.1 , pp. 7-15
    • Nakamura, S.1    Ishiguro, Y.2    Nakai, R.3    Wakabayashi, K.4    Aono, R.5    Horikoshi, K.6
  • 36
    • 0017366937 scopus 로고
    • Cellulolytic and physiological properties of Clostridium thermocellum. Arch
    • Ng, T. K., P. J. Weimer, and J. G. Zeikus. 1977. Cellulolytic and physiological properties of Clostridium thermocellum. Arch. Microbiol. 114: 1-7.
    • (1977) Microbiol , vol.114 , pp. 1-7
    • Ng, T.K.1    Weimer, P.J.2    Zeikus, J.G.3
  • 37
    • 70450245151 scopus 로고    scopus 로고
    • Tepidimicrobium xylanilyticum sp. nov., an anaerobic xylanolytic bacterium, and emended description of the genus Tepidimicrobium
    • Niu, L., L. Song, X. Liu, and X. Dong. 2009. Tepidimicrobium xylanilyticum sp. nov., an anaerobic xylanolytic bacterium, and emended description of the genus Tepidimicrobium. Int. J. Syst. Evol. Microbiol. 59: 2698-2701.
    • (2009) Int. J. Syst. Evol. Microbiol , vol.59 , pp. 2698-2701
    • Niu, L.1    Song, L.2    Liu, X.3    Dong, X.4
  • 38
    • 17044443785 scopus 로고    scopus 로고
    • Fermentation of lignocellulosic hydrolysates for ethanol production _rfsti Enzyme Microb. Technol
    • Olsson, L. and B. Hahn-Hägerdal. 1996. Fermentation of lignocellulosic hydrolysates for ethanol production. Enzyme Microb. Technol. 18: 312-331.
    • (1996) , vol.18 , pp. 312-331
    • Olsson, L.1    Hahn-Hägerdal, B.2
  • 39
    • 33646083242 scopus 로고    scopus 로고
    • Paenibacillus curdlanolyticus strain B-6 xylanolytic-cellulolytic enzyme system that degrades insoluble polysaccharides
    • Pason, P., K. L. Kyu, and K. Ratanakhanokchai. 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
  • 40
    • 0345490830 scopus 로고    scopus 로고
    • Purification and properties of a xylan-binding endoxylanase from alkaliphilic Bacillus sp. strain K-1
    • Ratanakhanokchai, K., K. L. Kyu, and M. Tantichareon. 1999. Purification and properties of a xylan-binding endoxylanase from alkaliphilic Bacillus sp. strain K-1. Appl. Environ. Microbiol. 65: 694-697.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 694-697
    • Ratanakhanokchai, K.1    Kyu, K.L.2    Tantichareon, M.3
  • 41
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • Shoham, Y., R. Lamed, and E. A. Bayer. 1999. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol. 7: 275-280.
    • (1999) Trends Microbiol , vol.7 , pp. 275-280
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 43
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • Somogyi, M. 1952. Notes on sugar determination. J. Biol. Chem. 195: 19-23.
    • (1952) J. Biol. Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 45
    • 0028028182 scopus 로고
    • Taxonomic note: A place for DNA-DNA reassociation and 16S rRNA sequence analysis in the present species definition in bacteriology
    • Stackebrandt, E. and B. M. Goebel. 1994. Taxonomic note: A place for DNA-DNA reassociation and 16S rRNA sequence analysis in the present species definition in bacteriology. Int. J. Syst. Bacteriol. 44: 846-849.
    • (1994) Int. J. Syst. Bacteriol , vol.44 , pp. 846-849
    • Stackebrandt, E.1    Goebel, B.M.2
  • 46
    • 33750195557 scopus 로고    scopus 로고
    • Purification of xylanase from Bacillus sp. K-8 by using corn husk column
    • Tachaapaikoon, C., K. L. Kyu, and K. Ratanakhanokchai. 2006. Purification of xylanase from Bacillus sp. K-8 by using corn husk column. Proc. Biochem. 41: 2441-2445.
    • (2006) Proc. Biochem , vol.41 , pp. 2441-2445
    • Tachaapaikoon, C.1    Kyu, K.L.2    Ratanakhanokchai, K.3
  • 47
    • 0033025021 scopus 로고    scopus 로고
    • Optimization of extracellular lignocellulolytic enzyme production by a thermophilic actinomycete Thermomonospora fusca BD25
    • Tuncer, M., A. S. Ball, A. Rob, and M. T. Wilson. 1999. Optimization of extracellular lignocellulolytic enzyme production by a thermophilic actinomycete Thermomonospora fusca BD25. Enzyme Microb. Technol. 25: 38-47.
    • (1999) Enzyme Microb. Technol , vol.25 , pp. 38-47
    • Tuncer, M.1    Ball, A.S.2    Rob, A.3    Wilson, M.T.4
  • 48
    • 64549113059 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding a multidomain endo-[3-1,4-xylanase from Paenibacillus curdlanolyticus B-6, and characterization of the recombinant enzyme
    • Waeonukul, R., P. Pason, K. L. Kyu, K. Sakka, A. Kosugi, Y. Mori, and K. Ratanakhanokchai. 2009. Cloning, sequencing, and expression of the gene encoding a multidomain endo-[3-1,4-xylanase from Paenibacillus curdlanolyticus B-6, and characterization of the recombinant enzyme. J. Microbiol. Biotechnol. 19: 277-285.
    • (2009) J. Microbiol. Biotechnol , vol.19 , pp. 277-285
    • Waeonukul, R.1    Pason, P.2    Kyu, K.L.3    Sakka, K.4    Kosugi, A.5    Mori, Y.6    Ratanakhanokchai, K.7
  • 49
    • 33947157565 scopus 로고    scopus 로고
    • What is (and is not) vital to advancing cellulosic ethanol
    • Wyman, C. E. 2007. What is (and is not) vital to advancing cellulosic ethanol. Trends Biotechnol. 25: 153-157.
    • (2007) Trends Biotechnol , vol.25 , pp. 153-157
    • Wyman, C.E.1
  • 50
    • 0001714350 scopus 로고
    • Thermophilic bacteria: Ecology, physiology and technology
    • Zeikus, J. G. 1979. Thermophilic bacteria: Ecology, physiology and technology. Enzyme Microb. Technol. 1: 243-252.
    • (1979) Enzyme Microb. Technol , vol.1 , pp. 243-252
    • Zeikus, J.G.1
  • 51
    • 27144488659 scopus 로고    scopus 로고
    • Clostridium alkalicellum sp. nov., an obligately alkaliphilic cellulolytic bacterium from a soda lake in the Baikal region
    • Zhilina, T. N., V. V. Kevbrin, T. P. Tourova, A. M. Lysenko, N. A. Kostrikina, and G. A. Zavarzin. 2005. Clostridium alkalicellum sp. nov., an obligately alkaliphilic cellulolytic bacterium from a soda lake in the Baikal region. Microbiology 74: 557-566.
    • (2005) Microbiology , vol.74 , pp. 557-566
    • Zhilina, T.N.1    Kevbrin, V.V.2    Tourova, T.P.3    Lysenko, A.M.4    Kostrikina, N.A.5    Zavarzin, G.A.6


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