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Volumn 16, Issue 8, 2006, Pages 1269-1275

Selection of multienzyme complex-producing bacteria under aerobic cultivation

Author keywords

Cellulase cellulose binding factor; Lignocellulosic substances; Multienzyme complex; Xylanase xylan binding factor

Indexed keywords

CELLULASE; CELLULOSE; CELLULOSOME; MICROCRYSTALLINE CELLULOSE; MULTIENZYME COMPLEX; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 33748685036     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (36)
  • 1
    • 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
  • 2
    • 0022512490 scopus 로고
    • Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose
    • Bayer, E. A. and R. Lamed. 1991. Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose. J. Bacteriol. 167: 828-836.
    • (1991) J. Bacteriol. , vol.167 , pp. 828-836
    • Bayer, E.A.1    Lamed, R.2
  • 3
    • 0027984011 scopus 로고
    • The cellulosome: A treasuretrove for biotechnology
    • Bayer, E. A., E. Morag, and R. Lamed. 1994. The cellulosome: A treasuretrove 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
  • 4
    • 0021855251 scopus 로고
    • Organization and distribution of the cellulosome in Clostridium thermocellum
    • Bayer, E. A., E. Setter, and R. Lamed. 1985. Organization and distribution of the cellulosome in Clostridium thermocellum. J. Bacteriol. 163: 552-559.
    • (1985) J. Bacteriol. , vol.163 , pp. 552-559
    • Bayer, E.A.1    Setter, E.2    Lamed, R.3
  • 6
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • Beguin, P. and J. P. Aubert. 1994. The biological degradation of cellulose. FEMS Microbiol. Rev. 13: 25-58.
    • (1994) FEMS Microbiol. Rev. , vol.13 , pp. 25-58
    • Beguin, P.1    Aubert, J.P.2
  • 7
    • 0015358796 scopus 로고
    • Growth and cellulase formation by Cellvibrio fulvus
    • Berg, B., B. V. Hofstan, and B. Petterson. 1972. Growth and cellulase formation by Cellvibrio fulvus. J. Appl. Bacteriol. 35: 201-214.
    • (1972) J. Appl. Bacteriol. , vol.35 , pp. 201-214
    • Berg, B.1    Hofstan, B.V.2    Petterson, B.3
  • 8
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely, P. 1985. Microbial xylanolytic systems. Trends Biotechnol. 3: 286-290.
    • (1985) Trends Biotechnol. , vol.3 , pp. 286-290
    • Biely, P.1
  • 9
    • 0002340670 scopus 로고
    • Comparative biochemistry of fungal and bacterial cellulolytic enzyme systems
    • Coughlan, M. P. and L. G. Ljungdahl. 1988. Comparative biochemistry of fungal and bacterial cellulolytic enzyme systems. FEMS Symp. 43: 11-30.
    • (1988) FEMS Symp. , vol.43 , pp. 11-30
    • Coughlan, M.P.1    Ljungdahl, L.G.2
  • 12
    • 0024312683 scopus 로고
    • Cloning of a Thermomonospora fusca xylanase gene and its expression in Escherichia coli and Streptomyces lividans
    • Ghangas, G. S., Y. J. Hu, and O. B. Wilson. 1989. Cloning of a Thermomonospora fusca xylanase gene and its expression in Escherichia coli and Streptomyces lividans. J. Bacteriol. 171: 2963-2969.
    • (1989) J. Bacteriol. , vol.171 , pp. 2963-2969
    • Ghangas, G.S.1    Hu, Y.J.2    Wilson, O.B.3
  • 13
    • 0024387764 scopus 로고
    • Factors affecting adhesion of Fibrobacter succinogenes subsp. succinogenes S85 and adherence-defective mutants to cellulose
    • Gong, J. and C. W. Forsberg. 1989. Factors affecting adhesion of Fibrobacter succinogenes subsp. succinogenes S85 and adherence-defective mutants to cellulose. Appl. Environ. Microbiol. 55: 3039-3044.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 3039-3044
    • Gong, J.1    Forsberg, C.W.2
  • 14
    • 1542315486 scopus 로고    scopus 로고
    • Xylan hydrolysis by treatment with endoxylanase and beta-xylosidase expressed in yeast
    • Heo, S. Y., J. K. Kim, Y. M. Kim, and S. W. Nam. 2004. Xylan hydrolysis by treatment with endoxylanase and beta-xylosidase expressed in yeast. J. Microbiol. Biotechnol. 14: 171-177.
    • (2004) J. Microbiol. Biotechnol. , vol.14 , pp. 171-177
    • Heo, S.Y.1    Kim, J.K.2    Kim, Y.M.3    Nam, S.W.4
  • 16
    • 1642330045 scopus 로고    scopus 로고
    • A novel, ultra-large xylanolytic complex (xylanosome) secreted by Streptomyces olivaceoviridis
    • Jiang, Z. Q., W. Deng, L. T. Li, C. H. Ding, I. Kusakabe, and S. S. Tan. 2004. A novel, ultra-large xylanolytic complex (xylanosome) secreted by Streptomyces olivaceoviridis. Biotechnol. Lett. 26: 431-436.
    • (2004) Biotechnol. Lett. , vol.26 , pp. 431-436
    • Jiang, Z.Q.1    Deng, W.2    Li, L.T.3    Ding, C.H.4    Kusakabe, I.5    Tan, S.S.6
  • 17
    • 0036826318 scopus 로고    scopus 로고
    • Surface immobilization on silica of endoxylanase produced from recombinant Bacillus subtilis
    • Kang, S. C., H. J. Kim, S. W. Nam, and D. K. Oh. 2002. Surface immobilization on silica of endoxylanase produced from recombinant Bacillus subtilis. J. Microbiol. Biotechnol. 12: 766-772.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 766-772
    • Kang, S.C.1    Kim, H.J.2    Nam, S.W.3    Oh, D.K.4
  • 18
    • 0037299771 scopus 로고    scopus 로고
    • Isolation and characteristics of Trichoderma harzianum FJ1 producing cellulases and xylanase
    • Kim, K. C., S. S. Yoo, Y. A. Oh, and S. J. Kim. 2003. Isolation and characteristics of Trichoderma harzianum FJ1 producing cellulases and xylanase. J. Microbiol. Biotechnol. 13: 1-8.
    • (2003) J. Microbiol. Biotechnol. , vol.13 , pp. 1-8
    • Kim, K.C.1    Yoo, S.S.2    Oh, Y.A.3    Kim, S.J.4
  • 19
    • 0025605767 scopus 로고
    • Trends in biochemistry and enzymology of cellulose degradation
    • Klyosov, A. 1990. Trends in biochemistry and enzymology of cellulose degradation. Biochemistry 29: 10577-10585.
    • (1990) Biochemistry , vol.29 , pp. 10577-10585
    • Klyosov, A.1
  • 20
    • 0026080368 scopus 로고
    • Cellulosome-like entities in Bacteroides cellulosovens
    • Lamed, R., E. Morag, O. Mor-Yosef, and E. A. Bayer. 1991. Cellulosome-like entities in Bacteroides cellulosovens. Curr. Microbiol. 22: 27-33.
    • (1991) Curr. Microbiol. , vol.22 , pp. 27-33
    • Lamed, R.1    Morag, E.2    Mor-Yosef, O.3    Bayer, E.A.4
  • 21
    • 0021016163 scopus 로고
    • Characterization of a cellulose binding, cellulase-containing complex in Clostridium thermocellum
    • Lamed, R., L. E. Setter, and E. A. Bayer. 1983. Characterization of a cellulose binding, cellulase-containing complex in Clostridium thermocellum. J. Bacteriol. 156: 828-836.
    • (1983) J. Bacteriol. , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, L.E.2    Bayer, E.A.3
  • 22
    • 8644255235 scopus 로고    scopus 로고
    • Purification and characterization of two thermostable xylanases from Paenibacillus sp. DG-22
    • Lee, Y. E. and P. O. Lim. 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
  • 25
    • 0001728210 scopus 로고
    • Macromolecular organization of the cellulolytic enzyme complex of Clostridium thermocellum as revealed by electron microscopy
    • Mayer, F., M. P. Coughlan, Y. Mori, and L. G. Ljungdahl. 1987. Macromolecular organization of the cellulolytic enzyme complex of Clostridium thermocellum as revealed by electron microscopy. Appl. Environ. Microbiol. 53: 2785-2792.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2785-2792
    • Mayer, F.1    Coughlan, M.P.2    Mori, Y.3    Ljungdahl, L.G.4
  • 26
    • 0026848803 scopus 로고
    • Infinity digestion for the near-total recovery of purified cellulosome from Clostridium thermocellum
    • Morag, E., E. A. Bayer, and R. Lamed. 1992. Infinity digestion for the near-total recovery of purified cellulosome from Clostridium thermocellum. Enzyme Microbial Technol. 14: 289-292.
    • (1992) Enzyme Microbial Technol. , vol.14 , pp. 289-292
    • Morag, E.1    Bayer, E.A.2    Lamed, R.3
  • 27
    • 0041036897 scopus 로고
    • Characteristics of the adhesion of Ruminococcus albus to cellulose
    • Morris, E. J. 1988. Characteristics of the adhesion of Ruminococcus albus to cellulose. FEMS Microbiol. Lett. 51: 113-118.
    • (1988) FEMS Microbiol. Lett. , vol.51 , pp. 113-118
    • Morris, E.J.1
  • 28
    • 4444263028 scopus 로고    scopus 로고
    • Purification and characterization of the fibrinolytic enzyme produced by Bacillus subtilis KCK-7 from Chungkookjang
    • Paik, H. D., S. K. Lee, S. Heo, S. Y. Kim, H. H. Lee, and T. J. Kwon. 2004. Purification and characterization of the fibrinolytic enzyme produced by Bacillus subtilis KCK-7 from Chungkookjang. J. Microbiol. Biotechnol. 14: 829-835.
    • (2004) J. Microbiol. Biotechnol. , vol.14 , pp. 829-835
    • Paik, H.D.1    Lee, S.K.2    Heo, S.3    Kim, S.Y.4    Lee, H.H.5    Kwon, T.J.6
  • 29
    • 0033996436 scopus 로고    scopus 로고
    • Isolation and properties of a cellulosome type multienzyme complex of the thermophilic Bacteroides sp. strain P-1
    • Ponpium, P., K. Ratanakhanokchai, and K. L. Kyu. 2000. Isolation and properties of a cellulosome type multienzyme complex of the thermophilic Bacteroides sp. strain P-1. Enzyme Microbial Technol. 26: 459-465.
    • (2000) Enzyme Microbial Technol. , vol.26 , pp. 459-465
    • Ponpium, P.1    Ratanakhanokchai, K.2    Kyu, K.L.3
  • 30
    • 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. Tanticharoen. 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    Tanticharoen, M.3
  • 31
    • 0025128248 scopus 로고
    • Effects of physicochemical factors on the adhesion of cellulose avicel of the ruminal bacteria Ruminococcus flavefaciens and Fibrobacter succinogenes subsp. succinogenes
    • Roger, V., G. Fonty, S. Komisarczuk-Bony, and P. Gouet. 1990. Effects of physicochemical factors on the adhesion of cellulose avicel of the ruminal bacteria Ruminococcus flavefaciens and Fibrobacter succinogenes subsp. succinogenes. Appl. Environ. Microbiol. 56: 3081-3087.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3081-3087
    • Roger, V.1    Fonty, G.2    Komisarczuk-Bony, S.3    Gouet, P.4
  • 32
    • 0030999754 scopus 로고    scopus 로고
    • Transfer of Bacillus alginolyticus, Bacillus chondroitinus, Bacillus curdlanolyticus, Bacillus glucanolyticus, Bacillus kobensis, and Bacillus thiaminolyticus to the genus Paenibacillus and emended description of the genus Paenibacillus
    • Shida, O., H. Takagi, K. Kadowaki, L. K. Nakamura, and K. Komagata. 1997. Transfer of Bacillus alginolyticus, Bacillus chondroitinus, Bacillus curdlanolyticus, Bacillus glucanolyticus, Bacillus kobensis, and Bacillus thiaminolyticus to the genus Paenibacillus and emended description of the genus Paenibacillus. Int. J. Syst. Bacteriol. 47: 289-298.
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 289-298
    • Shida, O.1    Takagi, H.2    Kadowaki, K.3    Nakamura, L.K.4    Komagata, K.5
  • 33
    • 33750423631 scopus 로고
    • Notes in sugar determination
    • Somogyi, M. 1952. Notes in sugar determination. J. Biol. Chem. 195: 19-23.
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 34
    • 27944441310 scopus 로고    scopus 로고
    • Mass-spectral identification of an extracellular protease from Bacillus subtilis KCCM 10257, a producer of antibacterial peptide subtilein
    • Song, H. H., M. J. Gill, and C. Lee. 2005. Mass-spectral identification of an extracellular protease from Bacillus subtilis KCCM 10257, a producer of antibacterial peptide subtilein. J. Microbiol. Biotechnol. 15: 1054-1059.
    • (2005) J. Microbiol. Biotechnol. , vol.15 , pp. 1054-1059
    • Song, H.H.1    Gill, M.J.2    Lee, C.3
  • 35
    • 0030642144 scopus 로고    scopus 로고
    • Xylanolytic enzymes from fungi and bacteria
    • Sunna, A. and G. Antranikian. 1997. Xylanolytic enzymes from fungi and bacteria. Crit. Rev. Biotechnol. 17: 39-67.
    • (1997) Crit. Rev. Biotechnol. , vol.17 , pp. 39-67
    • Sunna, A.1    Antranikian, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.