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Volumn 87, Issue 2, 2004, Pages 161-169

Synergistic activity of Paenibacillus sp. BP-23 cellobiohydrolase Cel48C in association with the contiguous endoglucanase Cel9B and with endoor exo-acting glucanases from Thermobifida fusca

Author keywords

Cellobiohydrolase; Cellulase; Cellulose degradation; Synergism

Indexed keywords

BACTERIA; BIOASSAY; CLONING; ENZYMES;

EID: 3042787960     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20099     Document Type: Article
Times cited : (15)

References (37)
  • 2
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Barr BK, Hsieh YL, Ganem B, Wilson DB. 1996. Identification of two functionally different classes of exocellulases. Biochemistry 35: 586-592.
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.L.2    Ganem, B.3    Wilson, D.B.4
  • 3
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • Béguin P, Aubert J-P. 1994. The biological degradation of cellulose. FEMS Microbiol Rev 13:25-58.
    • (1994) FEMS Microbiol Rev , vol.13 , pp. 25-58
    • Béguin, P.1    Aubert, J.-P.2
  • 4
    • 0027739839 scopus 로고
    • Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. Strain BP-23
    • Blanco A, Pastor FIJ. 1993. Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. Strain BP-23. Can J Microbiol 39:1162-1166.
    • (1993) Can J Microbiol , vol.39 , pp. 1162-1166
    • Blanco, A.1    Pastor, F.I.J.2
  • 5
    • 0028790376 scopus 로고
    • Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23
    • Blanco A, Vidal T, Colom JF, Pastor FIJ. 1995. Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23. Appl Environ Microbiol 61:4468-4470.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4468-4470
    • Blanco, A.1    Vidal, T.2    Colom, J.F.3    Pastor, F.I.J.4
  • 6
    • 0031823404 scopus 로고    scopus 로고
    • Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterization of the enzyme. Performance in paper manufacture from cereal straw
    • Blanco A, Diaz P, Martínez J, Vidal T, Torres AL, Pastor FIJ. 1998. Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterization of the enzyme. Performance in paper manufacture from cereal straw. Appl Microbiol Biotechnol 50:48-54.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 48-54
    • Blanco, A.1    Diaz, P.2    Martínez, J.3    Vidal, T.4    Torres, A.L.5    Pastor, F.I.J.6
  • 7
    • 0041541782 scopus 로고    scopus 로고
    • A multidomain xylanase from Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes
    • Blanco A, Diaz P, Zueco J, Parascandola P, Pastor FIJ. 1999. A multidomain xylanase from Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes. Microbiology 145:2163-2170.
    • (1999) Microbiology , vol.145 , pp. 2163-2170
    • Blanco, A.1    Diaz, P.2    Zueco, J.3    Parascandola, P.4    Pastor, F.I.J.5
  • 8
    • 0035809069 scopus 로고    scopus 로고
    • Optimized mixtures of recombinant Humicola insolens cellulases for the biodegradation of crystalline cellulose
    • Boisset C, Pétrequin C, Chanzy H, Henrissat B, Schülein M. 2001. Optimized mixtures of recombinant Humicola insolens cellulases for the biodegradation of crystalline cellulose. Biotechnol Bioeng 72: 339-345.
    • (2001) Biotechnol Bioeng , vol.72 , pp. 339-345
    • Boisset, C.1    Pétrequin, C.2    Chanzy, H.3    Henrissat, B.4    Schülein, M.5
  • 10
    • 0034641715 scopus 로고    scopus 로고
    • Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose
    • Carrad G, Koivula A, Söderlund H, Béguin P. 2000. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc Natl Acad Sci USA 97:10342-10347.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10342-10347
    • Carrad, G.1    Koivula, A.2    Söderlund, H.3    Béguin, P.4
  • 13
    • 0036623620 scopus 로고    scopus 로고
    • Effect of cellulase-assisted refining on the properties of dried and never-dried eucalyptus pulp
    • García O, Torres AL, Colom JF, Pastor FIJ, Diaz P, Vidal T. 2002. Effect of cellulase-assisted refining on the properties of dried and never-dried eucalyptus pulp. Cellulose 9:115-125.
    • (2002) Cellulose , vol.9 , pp. 115-125
    • García, O.1    Torres, A.L.2    Colom, J.F.3    Pastor, F.I.J.4    Diaz, P.5    Vidal, T.6
  • 14
    • 0036310985 scopus 로고    scopus 로고
    • The crystal structure and catalytic mechanism of cellobiohydrolase CelS the major enzymatic component of the Clostridium thermocellum cellulosome
    • Guimarães BG, Souchon H, Lytle BL, Wu JHD, Alzari PM. 2002. The crystal structure and catalytic mechanism of cellobiohydrolase CelS the major enzymatic component of the Clostridium thermocellum cellulosome. J Mol Biol 320:587-596.
    • (2002) J Mol Biol , vol.320 , pp. 587-596
    • Guimarães, B.G.1    Souchon, H.2    Lytle, B.L.3    Wu, J.H.D.4    Alzari, P.M.5
  • 15
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat B, Driguez H, Viet C, Schülein M. 1985. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Biotechnology 3:722-726.
    • (1985) Biotechnology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schülein, M.4
  • 16
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin DC, Spezio M, Walker LP, Wilson DB. 1993. Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects. Biotechnol Bioeng 42:1002-1013.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 17
    • 0033869510 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of a family 48 exocellulase, Cel48A, from Thermobifida fusca
    • Irwin DC, Zhang S, Wilson DB. 2000. Cloning, expression and characterisation of a family 48 exocellulase, Cel48A, from Thermobifida fusca. Eur J Biochem 267:4988-4997.
    • (2000) Eur J Biochem , vol.267 , pp. 4988-4997
    • Irwin, D.C.1    Zhang, S.2    Wilson, D.B.3
  • 18
    • 0036022022 scopus 로고    scopus 로고
    • Cooperative and competitive binding in synergistic mixtures of Thermobifida fusca cellulases Cel5A, Cel6B, and Cel9A
    • Jeoh T, Wilson DB, Walker LP. 2002. Cooperative and competitive binding in synergistic mixtures of Thermobifida fusca cellulases Cel5A, Cel6B, and Cel9A. Biotechnol Prog 18:760-769.
    • (2002) Biotechnol Prog , vol.18 , pp. 760-769
    • Jeoh, T.1    Wilson, D.B.2    Walker, L.P.3
  • 19
    • 0036727254 scopus 로고    scopus 로고
    • The fibronectin type 3-like repeat from Clostridium thermocellum cellobiohydrolase CbhA promotes hydrolysis of cellulose by modifying its surface
    • Kataeva IA, Seidel RD, Shah A, West LT, Li XL, Ljungdahl LG. 2002. The fibronectin type 3-like repeat from Clostridium thermocellum cellobiohydrolase CbhA promotes hydrolysis of cellulose by modifying its surface. Appl Environ Microbiol 68:4292-4300.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4292-4300
    • Kataeva, I.A.1    Seidel, R.D.2    Shah, A.3    West, L.T.4    Li, X.L.5    Ljungdahl, L.G.6
  • 21
    • 0033199811 scopus 로고    scopus 로고
    • Substrate and enzyme characteristics that limit cellulose hydrolysis
    • Mansfield SD, Mooney C, Saddler JN. 1999. Substrate and enzyme characteristics that limit cellulose hydrolysis. Biotechnol Prog 15: 804-816.
    • (1999) Biotechnol Prog , vol.15 , pp. 804-816
    • Mansfield, S.D.1    Mooney, C.2    Saddler, J.N.3
  • 22
    • 0036723835 scopus 로고    scopus 로고
    • Synergistic effects on crystalline cellulose degradation between cellulosomal cellulases from Clostridium cellulovorans
    • Murashima K, Kosugi A, Doi RH. 2002. Synergistic effects on crystalline cellulose degradation between cellulosomal cellulases from Clostridium cellulovorans. J Bacteriol 184:5088-5095.
    • (2002) J Bacteriol , vol.184 , pp. 5088-5095
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 23
    • 0037371574 scopus 로고    scopus 로고
    • Synergistic effects of cellulosomal xylanase and cellulases from Clostridium cellulovorans on plant cell wall degradation
    • Murashima K, Kosugi A, Doi RH. 2003. Synergistic effects of cellulosomal xylanase and cellulases from Clostridium cellulovorans on plant cell wall degradation. J Bacteriol 185:1518-1524.
    • (2003) J Bacteriol , vol.185 , pp. 1518-1524
    • Murashima, K.1    Kosugi, A.2    Doi, R.H.3
  • 24
    • 0032190381 scopus 로고    scopus 로고
    • The crystal structure of processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 20 Å resolution
    • Parsiegla G, Juy M, Reverbel LC, Tardif C, Bélaich J-P, Driguez H, Haser R. 1998. The crystal structure of processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 20 Å resolution. EMBO J 17:5551-5562.
    • (1998) EMBO J , vol.17 , pp. 5551-5562
    • Parsiegla, G.1    Juy, M.2    Reverbel, L.C.3    Tardif, C.4    Bélaich, J.-P.5    Driguez, H.6    Haser, R.7
  • 25
    • 0035102159 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a multidomain endoglucanase from Paenibacillus sp. BP-23: Evaluation of its performance in pulp refining
    • Pastor FIJ, Pujol X, Blanco A, Vidal T, Torres AL, Diaz P. 2001. Molecular cloning and characterization of a multidomain endoglucanase from Paenibacillus sp. BP-23: evaluation of its performance in pulp refining. Appl Microbiol Biotechnol 55:61-68.
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 61-68
    • Pastor, F.I.J.1    Pujol, X.2    Blanco, A.3    Vidal, T.4    Torres, A.L.5    Diaz, P.6
  • 26
    • 0031057162 scopus 로고    scopus 로고
    • Synergistic interaction of the Clostridium stercorarium cellulases Avicelase I (CelZ) and Avicelase II (CelY) in the degradation of microcrystalline cellulose
    • Riedel K, Ritter J, Bronnenmeier K. 1997. Synergistic interaction of the Clostridium stercorarium cellulases Avicelase I (CelZ) and Avicelase II (CelY) in the degradation of microcrystalline cellulose. FEMS Microbiol Lett 147:239-243.
    • (1997) FEMS Microbiol Lett , vol.147 , pp. 239-243
    • Riedel, K.1    Ritter, J.2    Bronnenmeier, K.3
  • 28
    • 0038045561 scopus 로고    scopus 로고
    • Exo-mode of action of cellobiohydrolase Cel48C from Paenibacillus sp. BP-23, a unique type of cellulase among Bacillales
    • Sánchez M, Pastor FIJ, Diaz P. 2003. Exo-mode of action of cellobiohydrolase Cel48C from Paenibacillus sp. BP-23, a unique type of cellulase among Bacillales. Eur J Biochem 270:2913-2919.
    • (2003) Eur J Biochem , vol.270 , pp. 2913-2919
    • Sánchez, M.1    Pastor, F.I.J.2    Diaz, P.3
  • 29
    • 0034840478 scopus 로고    scopus 로고
    • The cellulosome and cellulose degradation by anaerobic bacteria
    • Schwarz WH. 2001. The cellulosome and cellulose degradation by anaerobic bacteria. Appl Microbiol Biotechnol 56:634-649.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 634-649
    • Schwarz, W.H.1
  • 30
    • 0033972605 scopus 로고    scopus 로고
    • An unusual pectate lyase from a Bacillus sp. with high activity on pectin: Cloning and characterization
    • Soriano M, Blanco A, Diaz P, Pastor FIJ. 2000. An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization. Microbiology 146:89-95.
    • (2000) Microbiology , vol.146 , pp. 89-95
    • Soriano, M.1    Blanco, A.2    Diaz, P.3    Pastor, F.I.J.4
  • 31
    • 77956994971 scopus 로고
    • The Nelson-Somogyi copper reduction method. Analysis of sugars found in glycoprotein
    • Spiro RG. 1966. The Nelson-Somogyi copper reduction method. Analysis of sugars found in glycoprotein. Methods Enzymol 8:3-26.
    • (1966) Methods Enzymol , vol.8 , pp. 3-26
    • Spiro, R.G.1
  • 32
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • Teeri TT. 1997. Crystalline cellulose degradation: new insight into the function of cellobiohydrolases. TIBTECH 15:160-167.
    • (1997) TIBTECH , vol.15 , pp. 160-167
    • Teeri, T.T.1
  • 35
    • 0036092426 scopus 로고    scopus 로고
    • Synergism in binary mixtures of Thermobifidafusca cellulases Cel6B, Cel9A, and Cel5A on BMCC and Avicel
    • Watson DL, Wilson DB, Walker LP. 2002. Synergism in binary mixtures of Thermobifidafusca cellulases Cel6B, Cel9A, and Cel5A on BMCC and Avicel. Appl Biochem Biotechnol 101:97-111.
    • (2002) Appl Biochem Biotechnol , vol.101 , pp. 97-111
    • Watson, D.L.1    Wilson, D.B.2    Walker, L.P.3
  • 36
    • 77957061124 scopus 로고
    • Preparation of crystalline, amorphous, and dyed cellulase substrates
    • Wood TM. 1988. Preparation of crystalline, amorphous, and dyed cellulase substrates. Methods Enzymol 160:19-25.
    • (1988) Methods Enzymol , vol.160 , pp. 19-25
    • Wood, T.M.1
  • 37
    • 0034043589 scopus 로고    scopus 로고
    • Site-directed mutation of non-catalytic residues of Thermobifida fusca exocellulase Cel6B
    • Zhang S, Irwin DC, Wilson DB. 2000. Site-directed mutation of non-catalytic residues of Thermobifida fusca exocellulase Cel6B. Eur J Biochem 267:3101-3115.
    • (2000) Eur J Biochem , vol.267 , pp. 3101-3115
    • Zhang, S.1    Irwin, D.C.2    Wilson, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.