메뉴 건너뛰기




Volumn 107, Issue 6, 2009, Pages 610-614

Isolation and characterization of a multienzyme complex (cellulosome) of the Paenibacillus curdlanolyticus B-6 grown on Avicel under aerobic conditions

Author keywords

Carboxymethyl cellulose; Cellulolytic enzyme; Cellulosome; Facultatively anaerobic bacterium; Lignocellulosic substance; Multienzyme complex; Paenibacillus curdlanolyticus; Xylanase; Xylanolytic enzyme

Indexed keywords

CARBOXYMETHYL CELLULOSE; CELLULOLYTIC ENZYME; CELLULOSOME; FACULTATIVELY ANAEROBIC BACTERIUM; LIGNOCELLULOSIC SUBSTANCE; MULTIENZYME COMPLEX; PAENIBACILLUS CURDLANOLYTICUS; XYLANASE; XYLANOLYTIC ENZYME;

EID: 65549138472     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2009.01.010     Document Type: Article
Times cited : (45)

References (34)
  • 1
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer E.A., Belaich J.-P., Shoham Y., and Lamed R. The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides. Annu. Rev. Microbiol. 58 (2004) 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
  • 2
    • 0027984011 scopus 로고
    • The cellulosome: a treasure-trove for biotechnology
    • Bayer E.A., Morag E., and Lamed R. The cellulosome: a treasure-trove for biotechnology. Trends Biotech. 12 (1994) 379-386
    • (1994) Trends Biotech. , vol.12 , pp. 379-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 3
    • 0031799314 scopus 로고    scopus 로고
    • The cellulosome of Clostridium thermocellum
    • Béguin P., and Alzari P. The cellulosome of Clostridium thermocellum. Biochem. Soc. Trans. 26 (1998) 178-185
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 178-185
    • Béguin, P.1    Alzari, P.2
  • 5
    • 0033996436 scopus 로고    scopus 로고
    • Isolation and properties of a cellulosome type multienzyme complex of the thermophilic Bacteroides sp. strain P-1
    • Ponpium P., Ratanakhanokchai K., and Kyu K.L. Isolation and properties of a cellulosome type multienzyme complex of the thermophilic Bacteroides sp. strain P-1. Enzyme Microb. Technol. 26 (2000) 459-465
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 459-465
    • Ponpium, P.1    Ratanakhanokchai, K.2    Kyu, K.L.3
  • 6
    • 0022512490 scopus 로고
    • Ultrastructure of the cell surface cellulosome in Clostridium thermocellum
    • Bayer E.A., and Lamed R. Ultrastructure of the cell surface cellulosome in Clostridium thermocellum. J. Bacteriol. 167 (1986) 828-836
    • (1986) J. Bacteriol. , vol.167 , pp. 828-836
    • Bayer, E.A.1    Lamed, R.2
  • 7
    • 0033167973 scopus 로고    scopus 로고
    • The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides
    • Shoham Y., Lamed R., and Bayer E.A. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol. 7 (1999) 275-281
    • (1999) Trends Microbiol. , vol.7 , pp. 275-281
    • Shoham, Y.1    Lamed, R.2    Bayer, E.A.3
  • 8
    • 0037137211 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum
    • Sabathé F., Bélaïch A., and Soucaille P. Characterization of the cellulolytic complex (cellulosome) of Clostridium acetobutylicum. FEMS Microbiol. Lett. 217 (2002) 15-22
    • (2002) FEMS Microbiol. Lett. , vol.217 , pp. 15-22
    • Sabathé, F.1    Bélaïch, A.2    Soucaille, P.3
  • 10
    • 0031857381 scopus 로고    scopus 로고
    • Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome
    • Kakiuchi M., Isui A., Suzuki K., Fujino T., Fujino E., Kimura T., Karita S., Sakka K., and Ohmiya K. Cloning and DNA sequencing of the genes encoding Clostridium josui scaffolding protein CipA and cellulase CelD and identification of their gene products as major components of the cellulosome. J. Bacteriol. 180 (1998) 4303-4308
    • (1998) J. Bacteriol. , vol.180 , pp. 4303-4308
    • Kakiuchi, M.1    Isui, A.2    Suzuki, K.3    Fujino, T.4    Fujino, E.5    Kimura, T.6    Karita, S.7    Sakka, K.8    Ohmiya, K.9
  • 11
    • 0027976505 scopus 로고
    • Mulicomplex cellulase-xylanase system of Clostridium papyrosolvens C7
    • Pohlschröder M., Leschine S.B., and Canale-Parola E. Mulicomplex cellulase-xylanase system of Clostridium papyrosolvens C7. J. Bacteriol. 176 (1994) 70-76
    • (1994) J. Bacteriol. , vol.176 , pp. 70-76
    • Pohlschröder, M.1    Leschine, S.B.2    Canale-Parola, E.3
  • 13
    • 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. Paenibacillus curdlanolyticus strain B-6 xylanolytic-cellulolytic enzyme system that degrades insoluble polysaccharides. Appl. Environ. Microbiol. 72 (2006) 2483-2490
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2483-2490
    • Pason, P.1    Kyu, K.L.2    Ratanakhanokchai, K.3
  • 14
    • 0015358796 scopus 로고
    • Growth and cellulase formation by Cellvibrio fulvus
    • Berg B., Hofstan B.V., and Petterson B. Growth and cellulase formation by Cellvibrio fulvus. J. Appl. Bacteriol. 35 (1972) 201-214
    • (1972) J. Appl. Bacteriol. , vol.35 , pp. 201-214
    • Berg, B.1    Hofstan, B.V.2    Petterson, B.3
  • 15
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • Nelson N. A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153 (1944) 375-380
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.1
  • 16
    • 0345490830 scopus 로고    scopus 로고
    • Purification and properties of a xylan-binding endoxylanase from alkaliphilic Bacillus sp. strain K-1
    • Ratanakhanokchai K., Kyu K.L., and Tanticharoen M. Purification and properties of a xylan-binding endoxylanase from alkaliphilic Bacillus sp. strain K-1. Appl. Environ. Microbiol. 65 (1999) 694-697
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 694-697
    • Ratanakhanokchai, K.1    Kyu, K.L.2    Tanticharoen, M.3
  • 17
    • 0025690514 scopus 로고
    • Subunit composition and glycosidic activities of the cellulose complex from Clostridium thermocellum JW20
    • Kohring S., Wiegel J., and Mayer F. Subunit composition and glycosidic activities of the cellulose complex from Clostridium thermocellum JW20. Appl. Environ. Microbiol. 56 (1990) 3798-3804
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3798-3804
    • Kohring, S.1    Wiegel, J.2    Mayer, F.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0028294637 scopus 로고
    • Characterization and sequence of a Thermomonospora fusca xylanase
    • Irwin D., Jung E.D., and Wilson D.B. Characterization and sequence of a Thermomonospora fusca xylanase. Appl. Environ. Microbiol. 60 (1994) 763-770
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 763-770
    • Irwin, D.1    Jung, E.D.2    Wilson, D.B.3
  • 21
    • 0023629497 scopus 로고
    • Specialized cell surface structures in cellulolytic bacteria
    • Lamed R., Naimark J., Morgenstern E., and Bayer E.A. Specialized cell surface structures in cellulolytic bacteria. J. Biotechnol. 169 (1987) 3792-3800
    • (1987) J. Biotechnol. , vol.169 , pp. 3792-3800
    • Lamed, R.1    Naimark, J.2    Morgenstern, E.3    Bayer, E.A.4
  • 22
    • 0001728210 scopus 로고
    • Macromolecule organization of the cellulolytic enzyme complex of Clostridium thermocellum as revealed by electron microscopy
    • Mayer F., Coughlan M.P., Mori Y., and Ljungdahl L.G. Macromolecule organization of the cellulolytic enzyme complex of Clostridium thermocellum as revealed by electron microscopy. Appl. Environ. Microbiol. 53 (1987) 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
  • 23
    • 0030002212 scopus 로고    scopus 로고
    • The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation
    • Béguin P., and Lemaire M. The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation. Crit. Rev. Biochem. Molec. Biol. 31 (1996) 201-236
    • (1996) Crit. Rev. Biochem. Molec. Biol. , vol.31 , pp. 201-236
    • Béguin, P.1    Lemaire, M.2
  • 24
    • 0021016163 scopus 로고
    • Characterization of a cellulose binding, cellulose-containing complex in Clostridium thermocellum
    • Lamed R., Setter L.E., and Bayer E.A. Characterization of a cellulose binding, cellulose-containing complex in Clostridium thermocellum. J. Bacteriol. 156 (1983) 828-836
    • (1983) J. Bacteriol. , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, L.E.2    Bayer, E.A.3
  • 25
    • 0034132054 scopus 로고    scopus 로고
    • Characterization of the cellulolytic complex (cellulosome) from Ruminococcus albus
    • Ohara H., Karita S., Kimura T., Sakka K., and Ohmiya K. Characterization of the cellulolytic complex (cellulosome) from Ruminococcus albus. Biosci. Biotechnol. Biochem. 64 (2000) 254-260
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 254-260
    • Ohara, H.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmiya, K.5
  • 26
    • 0035209025 scopus 로고    scopus 로고
    • Characterization of xylanolytic enzymes in Clostridium cellulovorans: expression of xylanase activity dependent on growth substrates
    • Kosugi A., Murashima K., and Doi R.H. Characterization of xylanolytic enzymes in Clostridium cellulovorans: expression of xylanase activity dependent on growth substrates. J. Bacteriol. 183 (2001) 7037-7043
    • (2001) J. Bacteriol. , vol.183 , pp. 7037-7043
    • Kosugi, A.1    Murashima, K.2    Doi, R.H.3
  • 27
    • 0033056902 scopus 로고    scopus 로고
    • The extracellular xylan degradative system in Clostridium cellulolyticum cultivated on xylan: evidence for cell-free cellulosome production
    • Mohand-Oussaid O., Payot S., Guedon E., Gelhaye E., Youyou A., and Petitdemange H. The extracellular xylan degradative system in Clostridium cellulolyticum cultivated on xylan: evidence for cell-free cellulosome production. J. Bacteriol. 181 (1999) 4035-4040
    • (1999) J. Bacteriol. , vol.181 , pp. 4035-4040
    • Mohand-Oussaid, O.1    Payot, S.2    Guedon, E.3    Gelhaye, E.4    Youyou, A.5    Petitdemange, H.6
  • 28
    • 1642330045 scopus 로고    scopus 로고
    • A novel, ultra-large xylanolytic complex (xylanosome) secreted by Streptomyces olivaceoviridis
    • Jiang Z.-Q., Deng W., Li L.-T., Ding C.-H., Kusakabe I., and Tan S.-S. A novel, ultra-large xylanolytic complex (xylanosome) secreted by Streptomyces olivaceoviridis. Biotechnol. Lett. 26 (2004) 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
  • 29
    • 0002390753 scopus 로고
    • Substrate factors limiting enzymatic hydrolysis
    • Saddler J.N. (Ed), C.A.B. International, Wallingford
    • Converse A.O. Substrate factors limiting enzymatic hydrolysis. In: Saddler J.N. (Ed). Bioconversion of forest and agricultural plant residues (1993), C.A.B. International, Wallingford 93-106
    • (1993) Bioconversion of forest and agricultural plant residues , pp. 93-106
    • Converse, A.O.1
  • 30
    • 0034840478 scopus 로고    scopus 로고
    • The cellulosome and cellulose degradation by anaerobic bacteria
    • Schwarz W.H. The cellulosome and cellulose degradation by anaerobic bacteria. Appl Microbiol. Biotechnol. 56 (2001) 634-649
    • (2001) Appl Microbiol. Biotechnol. , vol.56 , pp. 634-649
    • Schwarz, W.H.1
  • 31
    • 0021855251 scopus 로고
    • Organization and distribution of the cellulosome in Clostridium thermocellum
    • Bayer E.A., Setter E., and Lamed R. Organization and distribution of the cellulosome in Clostridium thermocellum. J. Bacteriol. 163 (1985) 552-559
    • (1985) J. Bacteriol. , vol.163 , pp. 552-559
    • Bayer, E.A.1    Setter, E.2    Lamed, R.3
  • 32
    • 0025886996 scopus 로고
    • Purification and cooperative activity of enzymes constituting the xylan-degrading system of Thermomonospora fusca
    • Bachmann S.L., and McCarthy A.J. Purification and cooperative activity of enzymes constituting the xylan-degrading system of Thermomonospora fusca. Appl. Environ. Microbiol. 57 (1991) 2121-2130
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2121-2130
    • Bachmann, S.L.1    McCarthy, A.J.2
  • 33
    • 0033199811 scopus 로고    scopus 로고
    • Substrate and enzyme characteristics that limit cellulose hydrolysis
    • Mansfield S.D., Mooney C., and Saddler J.N. Substrate and enzyme characteristics that limit cellulose hydrolysis. Biotechnol. Prog. 15 (1999) 804-816
    • (1999) Biotechnol. Prog. , vol.15 , pp. 804-816
    • Mansfield, S.D.1    Mooney, C.2    Saddler, J.N.3
  • 34
    • 33750195557 scopus 로고    scopus 로고
    • Purification of xylanase from alkaliphilic Bacillus sp. K-8 by using corn husk column
    • Tachaapaikoon C., Kyu K.L., and Ratanakhanokchai K. Purification of xylanase from alkaliphilic Bacillus sp. K-8 by using corn husk column. Proc. Biochem. 41 (2006) 2441-2445
    • (2006) Proc. Biochem. , vol.41 , pp. 2441-2445
    • Tachaapaikoon, C.1    Kyu, K.L.2    Ratanakhanokchai, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.