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Volumn 3, Issue 1, 2014, Pages 1-7

Identification of novel glycosyl hydrolases with cellulolytic activity against crystalline cellulose from metagenomic libraries constructed from bacterial enrichment cultures

Author keywords

Cellulase; Glycosyl hydrolase; Metagenome; Xylanase

Indexed keywords


EID: 84940347025     PISSN: None     EISSN: 21931801     Source Type: Journal    
DOI: 10.1186/2193-1801-3-365     Document Type: Article
Times cited : (32)

References (24)
  • 1
    • 0027193209 scopus 로고
    • An adhesive domain detected in functionally diverse receptors
    • 10.1016/0968-0004(93)90049-S
    • Beckmann G, Bork P: An adhesive domain detected in functionally diverse receptors. Trends Biochem Sci 1993, 18: 40-41. 10. 1016/0968-0004(93)90049-S.
    • (1993) Trends Biochem Sci , vol.18 , pp. 40-41
    • Beckmann, G.1    Bork, P.2
  • 2
    • 78149406841 scopus 로고    scopus 로고
    • Mining metagenomes for novel cellulase genes
    • 10.1007/s10529-010-0356-z
    • Duan CJ, Feng JX: Mining metagenomes for novel cellulase genes. Biotechnol Lett 2010, 32: 1765-1775. 10. 1007/s10529-010-0356-z.
    • (2010) Biotechnol Lett , vol.32 , pp. 1765-1775
    • Duan, C.J.1    Feng, J.X.2
  • 3
  • 4
    • 2442681858 scopus 로고    scopus 로고
    • The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities
    • 10.1074/jbc.M401620200
    • Henshaw JL, Bolam DN, Pires VM, Czjzek M, Henrissat B, Ferreira LM, Fontes CM, Gilbert HJ: The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities. J Biol Chem 2004, 279: 21552-21559. 10. 1074/jbc. M401620200.
    • (2004) J Biol Chem , vol.279 , pp. 21552-21559
    • Henshaw, J.L.1    Bolam, D.N.2    Pires, V.M.3    Czjzek, M.4    Henrissat, B.5    Ferreira, L.M.6    Fontes, C.M.7    Gilbert, H.J.8
  • 5
    • 84859627968 scopus 로고    scopus 로고
    • Biocatalyst and their small molecule products from metagenomic studies
    • 10.1016/j.cbpa.2012.02.015
    • Iqbal HA, Feng Z, Brady SF: Biocatalyst and their small molecule products from metagenomic studies. Curr Opin Chem Biol 2012, 16: 109-116. 10. 1016/j. cbpa. 2012. 02. 015.
    • (2012) Curr Opin Chem Biol , vol.16 , pp. 109-116
    • Iqbal, H.A.1    Feng, Z.2    Brady, S.F.3
  • 6
    • 32044439116 scopus 로고    scopus 로고
    • Stable coexistence of five bacterial strains as a cellulose-degrading community
    • 10.1128/AEM.71.11.7099-7106.2005
    • Kato S, Haruta S, Cui ZJ, Ishii M, Igarashi Y: Stable coexistence of five bacterial strains as a cellulose-degrading community. Appl Environ Microbiol 2005, 71: 7099-7106. 10. 1128/AEM. 71. 11. 7099-7106. 2005.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7099-7106
    • Kato, S.1    Haruta, S.2    Cui, Z.J.3    Ishii, M.4    Igarashi, Y.5
  • 7
    • 33746351766 scopus 로고    scopus 로고
    • Molecular cloning of the gene encoding beta-1,3(4)-glucanase A from a marine bacterium, Pseudomonas sp. PE2, an essential enzyme for the degradation of Pythium porphyrae cell walls
    • 10.1007/s00253-005-0200-x
    • Kitamura E, Kamei Y: Molecular cloning of the gene encoding beta-1, 3(4)-glucanase A from a marine bacterium, Pseudomonassp. PE2, an essential enzyme for the degradation ofPythium porphyraecell walls. Appl Microbiol Biotechnol 2006, 71: 630-637. 10. 1007/s00253-005-0200-x.
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 630-637
    • Kitamura, E.1    Kamei, Y.2
  • 8
    • 0026378943 scopus 로고
    • The influence of selected water quality parameters on the decay rated and exoenzymatic activity of detritus of Nymphaea alba L. floating leaf blades in laboratory experiments
    • 10.1007/BF00317572
    • Kok CJ, van der Velde G: The influence of selected water quality parameters on the decay rated and exoenzymatic activity of detritus ofNymphaea albaL. floating leaf blades in laboratory experiments. Oecologia 1991, 88: 311-316. 10. 1007/BF00317572.
    • (1991) Oecologia , vol.88 , pp. 311-316
    • Kok, C.J.1    van der Velde, G.2
  • 9
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives
    • 10.1007/s10295-008-0327-8
    • Kumar R, Singh S, Singh OV: Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol 2008, 35: 377-391. 10. 1007/s10295-008-0327-8.
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 11
    • 84873790809 scopus 로고
    • Replica plating and indirect selection of bacterial mutants
    • Lederberg J, Lederberg EM: Replica plating and indirect selection of bacterial mutants. J Bacteriol 1952, 63: 399-406.
    • (1952) J Bacteriol , vol.63 , pp. 399-406
    • Lederberg, J.1    Lederberg, E.M.2
  • 12
    • 67449124798 scopus 로고    scopus 로고
    • Bioprospecting metagenomes: glycosyl hydrolases for converting biomass
    • 10.1186/1754-6834-2-10
    • Li LL, McCorkle SR, Monchy S, Taghavi S, van der Lelie D: Bioprospecting metagenomes: glycosyl hydrolases for converting biomass. Biotechnol Biofuel 2009, 2: 10. 10. 1186/1754-6834-2-10.
    • (2009) Biotechnol Biofuel , vol.2 , pp. 10
    • Li, L.L.1    McCorkle, S.R.2    Monchy, S.3    Taghavi, S.4    van der Lelie, D.5
  • 13
    • 3042596766 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller LG: Use of dinitrosalicylic acid reagent for determination of reducing sugar. Biotechnol Bioeng 1959, 5: 193-219.
    • (1959) Biotechnol Bioeng , vol.5 , pp. 193-219
    • Miller, L.G.1
  • 14
    • 2442709187 scopus 로고    scopus 로고
    • The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5A in complex with oligosaccharaides reveals two distinct binding site with different ligand specificities
    • 10.1074/jbc.M401599200
    • Pires VM, Henshaw JL, Prates JA, Bolam DN, Ferreira LM, Fontes CM, Henrissat B, Planas A, Gilbert HJ, Czjzek M: The crystal structure of the family 6 carbohydrate binding module fromCellvibrio mixtusendoglucanase 5A in complex with oligosaccharaides reveals two distinct binding site with different ligand specificities. J Biol Chem 2004, 279: 21560-21568. 10. 1074/jbc. M401599200.
    • (2004) J Biol Chem , vol.279 , pp. 21560-21568
    • Pires, V.M.1    Henshaw, J.L.2    Prates, J.A.3    Bolam, D.N.4    Ferreira, L.M.5    Fontes, C.M.6    Henrissat, B.7    Planas, A.8    Gilbert, H.J.9    Czjzek, M.10
  • 15
    • 80054037883 scopus 로고    scopus 로고
    • Inhibition of enzymatic hydrolysis by residual lignins from softwood - study of enzyme binding and inactivation on liginin-rich surface
    • 10.1002/bit.23242
    • Rahikainen JL, Mikander S, Marjamaa K, Tamminen T, Lappas A, Viikari L, Kruus K: Inhibition of enzymatic hydrolysis by residual lignins from softwood - study of enzyme binding and inactivation on liginin-rich surface. Biotechnol Bioeng 2011, 108: 2823-2834. 10. 1002/bit. 23242.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2823-2834
    • Rahikainen, J.L.1    Mikander, S.2    Marjamaa, K.3    Tamminen, T.4    Lappas, A.5    Viikari, L.6    Kruus, K.7
  • 18
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M: The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4: 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 19
    • 0036159062 scopus 로고    scopus 로고
    • Hydrolysis of lignocellulosic materials for ethanol production: a review
    • 10.1016/S0960-8524(01)00212-7
    • Sun Y, Cheng J: Hydrolysis of lignocellulosic materials for ethanol production: a review. Biores Technol 2002, 83: 1-11. 10. 1016/S0960-8524(01)00212-7.
    • (2002) Biores Technol , vol.83 , pp. 1-11
    • Sun, Y.1    Cheng, J.2
  • 21
    • 0028533339 scopus 로고
    • Cellulose pretreatments of lignocellulosic substrates
    • 10.1016/0141-0229(94)90012-4
    • Weil J, Westgate P, Kohlmann K, Ladisch MR: Cellulose pretreatments of lignocellulosic substrates. Enzyme Microb Technol 1994, 16: 1002-1004. 10. 1016/0141-0229(94)90012-4.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 1002-1004
    • Weil, J.1    Westgate, P.2    Kohlmann, K.3    Ladisch, M.R.4
  • 22
    • 0002438403 scopus 로고
    • A comparision of the thermostability of cellulose from various thermophilic fungi
    • Wojtczak G, Breuil C, Yamuda J, Saddler JN: A comparision of the thermostability of cellulose from various thermophilic fungi. Appl Miocrobiol Biotechnol 1987, 27: 82-87.
    • (1987) Appl Miocrobiol Biotechnol , vol.27 , pp. 82-87
    • Wojtczak, G.1    Breuil, C.2    Yamuda, J.3    Saddler, J.N.4
  • 23
    • 84864406375 scopus 로고    scopus 로고
    • Xylans inhibit enzymatic hydrolysis of lignocellulosic materials by cellulases
    • Zhang J, Tang M, Viikari L: Xylans inhibit enzymatic hydrolysis of lignocellulosic materials by cellulases. Bioresour Technol 2012, 121: 8-12.
    • (2012) Bioresour Technol , vol.121 , pp. 8-12
    • Zhang, J.1    Tang, M.2    Viikari, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.