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Volumn 93, Issue 5, 2012, Pages 1947-1956

A novel thermostable and glucose-tolerant β-glucosidase from Fervidobacterium islandicum

Author keywords

Glucosidase; Fervidobacterium islandicum; Glycoside hydrolase family 1; Thermoactive enzyme

Indexed keywords

AMINO ACID RESIDUES; BROAD TEMPERATURE RANGES; DITHIOTHREITOL; DIVALENT CATION; FERVIDOBACTERIUM ISLANDICUM; GLUCOSIDASE; GLYCOSIDE HYDROLASE FAMILY 1; HIGH LEVEL EXPRESSION; OPEN READING FRAME; OPTIMUM ACTIVITY; THERMOACTIVITY; THERMOPHILIC BACTERIA;

EID: 84857914120     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3406-0     Document Type: Article
Times cited : (52)

References (46)
  • 1
    • 0018736520 scopus 로고
    • Characterization and purification of thermostable β-glucosidase from Clostridium thermocellum
    • DOI 10.1016/0006-291X(79)91269-5
    • Ait N, Creuzet N, Cattaneo J (1979) Characterization and purification of a thermostable β-glucosidase from Clostridium thermocellum. Biochem Biophys Res Commun 90:537-546 (Pubitemid 10245944)
    • (1979) Biochemical and Biophysical Research Communications , vol.90 , Issue.2 , pp. 537-546
    • Ait, N.1    Creuzet, N.2    Cattaneo, J.3
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISSMODEL Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T, Suresh CG, Tolley SP, Dodson EJ, Hughes MA (1995) The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 3:951-960
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 5
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • Béguin P (1990) Molecular biology of cellulose degradation. Annu Rev Microbiol 44:219-248
    • (1990) Annu Rev Microbiol , vol.44 , pp. 219-248
    • Béguin, P.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0001590330 scopus 로고
    • The TIM barrel-the most frequently occurring folding motif in proteins
    • Branden C (1991) The TIM barrel-the most frequently occurring folding motif in proteins. Curr Opin Struct Biol 1:978-983
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 978-983
    • Branden, C.1
  • 9
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • DOI 10.1038/nprot.2007.131, PII NPROT.2007.131
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2:953-971 (Pubitemid 46745592)
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von, H.G.3    Nielsen, H.4
  • 11
    • 2442670433 scopus 로고    scopus 로고
    • Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors
    • DOI 10.1021/bi049666m
    • Gloster TM, Roberts S, Ducros VM, Perugino G, Rossi M, Hoos R, Moracci M,VasellaA, Davies GJ (2004) Structural studies of the betaglycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors. Biochemistry 43:6101-6109 (Pubitemid 38669478)
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 6101-6109
    • Gloster, T.M.1    Roberts, S.2    Ducros, V.M.-A.3    Perugino, G.4    Rossi, M.5    Hoos, R.6    Moracci, M.7    Vasella, A.8    Davies, G.J.9
  • 13
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon J, Davies G (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA 92:7090-7094
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.5    Davies, G.6
  • 14
    • 84941885978 scopus 로고
    • Combined product and substrate inhibition equation for cellobiase
    • Hong J, Ladisch M, Gong C, Wankat P, Tsao G (1981) Combined product and substrate inhibition equation for cellobiase. Biotechnol Bioeng 23:2779-2788
    • (1981) Biotechnol Bioeng , vol.23 , pp. 2779-2788
    • Hong, J.1    Ladisch, M.2    Gong, C.3    Wankat, P.4    Tsao, G.5
  • 15
    • 0025282531 scopus 로고
    • Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the 'Thermotogales'
    • DOI 10.1007/BF00423318
    • Huber R, Woese C, Langworthy T, Kristjansson J, Stetter K (1990) Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the "Thermotogales". Arch Microbiol 154:105-111 (Pubitemid 20239454)
    • (1990) Archives of Microbiology , vol.154 , Issue.2 , pp. 105-111
    • Huber, R.1    Woese, C.R.2    Langworthy, T.A.3    Kristjansson, J.K.4    Stetter, K.O.5
  • 16
    • 0028956984 scopus 로고
    • β-Glucosidase, β- galactosidase, family A cellulases, family F xylanases and two barley glycanases from a superfamily of enzymes with 8-fold β/αarchitecture and with two conserved glutamates near the carboxyterminal ends of β-strands four and seven
    • Jenkins J, Lo Leggio L, Harris G, Pickersgill R (1995) β-Glucosidase, β- galactosidase, family A cellulases, family F xylanases and two barley glycanases from a superfamily of enzymes with 8-fold β/αarchitecture and with two conserved glutamates near the carboxyterminal ends of β-strands four and seven. FEBS Lett 362:281-285
    • (1995) FEBS Lett , vol.362 , pp. 281-285
    • Jenkins, J.1    Lo Leggio, L.2    Harris, G.3    Pickersgill, R.4
  • 17
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292:195-202
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.1
  • 18
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen S, Luesink E, Stams A, Zehnder A (1993) Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur J Biochem 213:305-312 (Pubitemid 23106059)
    • (1993) European Journal of Biochemistry , vol.213 , Issue.1 , pp. 305-312
    • Kengen, S.W.M.1    Luesink, E.J.2    Stams, A.J.M.3    Zehnder, A.J.B.4
  • 19
    • 84857923962 scopus 로고    scopus 로고
    • Lignocellulose converting enzymes from thermophiles
    • Horikoshi K (ed) Springer, New York
    • Klippel B, and Antranikian G (2011) Lignocellulose converting enzymes from thermophiles. In Horikoshi K (ed) Extremophiles handbook. Springer, New York, pp 444-474
    • (2011) Extremophiles Handbook , pp. 444-474
    • Klippel, B.1    Antranikian, G.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U (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.1
  • 22
    • 69949142859 scopus 로고    scopus 로고
    • Screening and identification of new isolate: Thermostable Escherichia coli with novel thermoalkalotolerant cellulases
    • Li X, Bhaskar R, Yang H, Wang D, Miao Y (2009) Screening and identification of new isolate: thermostable Escherichia coli with novel thermoalkalotolerant cellulases. Curr Microbiol 59:393-399
    • (2009) Curr Microbiol , vol.59 , pp. 393-399
    • Li, X.1    Bhaskar, R.2    Yang, H.3    Wang, D.4    Miao, Y.5
  • 23
    • 80855139035 scopus 로고    scopus 로고
    • Strategies to enhance enzymatic hydrolysis of cellulose in lignocellulosic biomass
    • MacLellan J (2010) Strategies to enhance enzymatic hydrolysis of cellulose in lignocellulosic biomass. MMG 445 Basic Biotech 6:31-35
    • (2010) MMG 445 Basic Biotech , vol.6 , pp. 31-35
    • MacLellan, J.1
  • 24
    • 0030459862 scopus 로고    scopus 로고
    • Identification of two glutamic acid residues essential for catalysis in the β-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • Moracci M, Capalbo L, Ciaramella M, Rossi M (1996) Identification of two glutamic acid residues essential for catalysis in the β-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus. Protein Eng 9:1191-1195
    • (1996) Protein Eng , vol.9 , pp. 1191-1195
    • Moracci, M.1    Capalbo, L.2    Ciaramella, M.3    Rossi, M.4
  • 25
    • 70350710163 scopus 로고    scopus 로고
    • Production of the rare ginsenosides compound K, compound Y and compound Mc by a thermostable β-glycosidase from Sulfolobus acidocaldarius
    • Noh K, Oh DK (2009) Production of the rare ginsenosides compound K, compound Y and compound Mc by a thermostable β- glycosidase from Sulfolobus acidocaldarius. Biol Pharm Bull 32:1830-1835
    • (2009) Biol Pharm Bull , vol.32 , pp. 1830-1835
    • Noh, K.1    Oh, D.K.2
  • 26
    • 0005812912 scopus 로고
    • Isolation of Streptomyces sp. producing glucose-tolerant beta-glucosidases and properties of the enzymes
    • Ozaki H, Yamada K (1991) Isolation of Streptomyces sp. producing glucose-tolerant beta-glucosidases and properties of the enzymes. Agric Biol Chem 55:979-987
    • (1991) Agric Biol Chem , vol.55 , pp. 979-987
    • Ozaki, H.1    Yamada, K.2
  • 27
    • 0023257746 scopus 로고
    • Purification and properties of a stable β-glucosidase from an extremely thermophilic anaerobic bacterium
    • Patchett M, Daniel R, Morgan H (1987) Purification and properties of a stable β-glucosidase from an extremely thermophilic anaerobic bacterium. Biochem J 243:779-787 (Pubitemid 17073716)
    • (1987) Biochemical Journal , vol.243 , Issue.3 , pp. 779-787
    • Patchett, M.L.1    Daniel, R.M.2    Morgan, H.W.3
  • 28
    • 0029100735 scopus 로고
    • Properties of a novel glucose enhanced β-glucosidase purified from Streptomyces sp. ATCC11238
    • Perez-Pons JA, Robordosa X, Querol E (1995) Properties of a novel glucose enhanced β-glucosidase purified from Streptomyces sp. ATCC11238. Biochim Biophys Acta 1251:145-153
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 145-153
    • Perez-Pons, J.A.1    Robordosa, X.2    Querol, E.3
  • 29
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae
    • Riou C, Salmon J, Vallierl M, Gunata Z, Barre P (1998) Purification, characterization and substrate specificity of a novel highly glucose-tolerant β-glucosidase from Aspergillus oryzae. Appl Environ Microbiol 64:3607-3614 (Pubitemid 28462947)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.10 , pp. 3607-3614
    • Riou, C.1    Salmon, J.-M.2    Vallier, M.-J.3    Gunata, Z.4    Barre, P.5
  • 30
    • 0027594752 scopus 로고
    • Purification and properties of the Clostridium thermocellum bglB gene product expressed in Escherichia coli
    • DOI 10.1016/0141-0229(93)90125-L
    • Romaniec M, Huskisson N, Barker P, Demain A (1993) Purification and properties of the Clostridium thermocellum bgl gene product expressed in Escherichia coli. Enzyme Microb Technol 15:393-400 (Pubitemid 23124093)
    • (1993) Enzyme and Microbial Technology , vol.15 , Issue.5 , pp. 393-400
    • Romaniec, M.P.M.1    Huskisson, N.2    Barker, P.3    Demain, A.L.4
  • 31
    • 0002792701 scopus 로고
    • Cellulases: Biosynthesis and applications
    • Ryu D, Mandels M (1980) Cellulases: biosynthesis and applications. Enzyme Microb Technol 2:91-102
    • (1980) Enzyme Microb Technol , vol.2 , pp. 91-102
    • Ryu, D.1    Mandels, M.2
  • 32
    • 0029786225 scopus 로고    scopus 로고
    • Production, purification, and characterization of a highly glucose- tolerant novel β-glucosidase from Candida peltata
    • Saha B, Bothast R (1996) Production, purification and characterization of a highly glucose-tolerant novel β-glucosidase from Candida peltata. Appl Environ Microbiol 62:3165-3170 (Pubitemid 26304096)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.9 , pp. 3165-3170
    • Saha, B.C.1    Bothast, R.J.2
  • 33
    • 0028982269 scopus 로고
    • Construction of chimeric β-glucosidases with improved enzymatic properties
    • Singh A, Hayashi K (1995) Construction of chimeric β-glucosidases with improved enzymatic properties. J Biol Chem 270:21928-21933
    • (1995) J Biol Chem , vol.270 , pp. 21928-21933
    • Singh, A.1    Hayashi, K.2
  • 34
    • 0026731191 scopus 로고
    • Region-directed mutagenesis of residues surrounding the active site nucleophile in β- Glucosidase from Agrobacterium faecalis
    • Trimbur D, Warren R, Withers S (1992) Region-directed mutagenesis of residues surrounding the active site nucleophile in β- glucosidase from Agrobacterium faecalis. J Biol Chem 267:10248-10251
    • (1992) J Biol Chem , vol.267 , pp. 10248-10251
    • Trimbur, D.1    Warren, R.2    Withers, S.3
  • 36
    • 0025375657 scopus 로고
    • Crystallization of alcohol oxidase from Pichia pastoris. Secondary structure predictions indicate a domain with the eightfold beta/alpha-barrel fold
    • DOI 10.1007/BF01024988
    • Tykarska E, Lebioda L, Marchut E, Steczko J, Stec B (1990) Crystallization of alcohol oxidase from Pichia pastoris. Secondary structure predictions indicate a domain with the eightfold beta/ alpha-barrel fold. J Protein Chem 9:83-86 (Pubitemid 20221380)
    • (1990) Journal of Protein Chemistry , vol.9 , Issue.1 , pp. 83-86
    • Tykarska, E.1    Lebioda, L.2    Marchut, E.3    Steczko, J.4    Stec, B.5
  • 38
    • 0028876332 scopus 로고
    • Characterization of the celB gene coding for β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli
    • VoorhorstW, Eggen R, Luesink E, De VosW(1995) Characterization of the celB gene coding for β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli. J Bacteriol 177:7105-7111
    • (1995) J Bacteriol , vol.177 , pp. 7105-7111
    • Voorhorst, W.1    Eggen, R.2    Luesink, E.3    De Vos, W.4
  • 39
    • 0028848613 scopus 로고
    • Identification of the acid/base catalyst in Agrobacterium faecalis beta-glucosidase by kinetic analysis of mutants
    • Wang Q, Trimbur D, Graham R, Warren R, Withers S (1995) Identification of the acid/base catalyst in Agrobacterium faecalis beta-glucosidase by kinetic analysis of mutants. Biochem 34:14554-14562
    • (1995) Biochem , vol.34 , pp. 14554-14562
    • Wang, Q.1    Trimbur, D.2    Graham, R.3    Warren, R.4    Withers, S.5
  • 40
    • 0035896377 scopus 로고    scopus 로고
    • The TIM-barrel fold: A versatile framework for efficient enzymes
    • Wierenga R (2001) The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett 492:193-198
    • (2001) FEBS Lett , vol.492 , pp. 193-198
    • Wierenga, R.1
  • 41
    • 0022049674 scopus 로고
    • Properties of cellulolytic enzyme systems
    • Wood T (1985) Properties of cellulolytic enzyme systems. Biochem Soc Trans 13:407-410
    • (1985) Biochem Soc Trans , vol.13 , pp. 407-410
    • Wood, T.1
  • 42
    • 0024334731 scopus 로고
    • The mechanism of fungal cellulase action. Synergism between enzyme components of Penicillium pinophilum cellulase in solubilizing hydrogen bound-ordered cellulose
    • Wood T, McCrae S, Bhat K (1989) The mechanism of fungal cellulase action: synergism between components of Penicillum pinophilum cellulase in solubilizing hydrogen bond ordered cellulose. Biochem J 260:37-43 (Pubitemid 19139896)
    • (1989) Biochemical Journal , vol.260 , Issue.1 , pp. 37-43
    • Wood, T.M.1    McCrae, S.I.2    Bhat, K.M.3
  • 43
    • 0026443120 scopus 로고
    • Cloning, characterization and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable betaglucosidase expressed in Escherichia coli
    • Wright R, Yablonsky M, Shalita Z, Goyal A, Eveleigh D (1992) Cloning, characterization and nucleotide sequence of a gene encoding Microbispora bispora BglB, a thermostable betaglucosidase expressed in Escherichia coli. Appl Environ Microbiol 58:3455-3465
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3455-3465
    • Wright, R.1    Yablonsky, M.2    Shalita, Z.3    Goyal, A.4    Eveleigh, D.5
  • 44
    • 0027470938 scopus 로고
    • Acceleration of ethanol production from paper mill waste fiber by supplementation with β-glucosidase
    • DOI 10.1016/0141-0229(93)90117-K
    • Xin Z, Yinbo Q, Peiji G (1993) Acceleration of ethanol production from paper mill waster fiber by supplementation with β- glucosidases. Enzyme Microb Technol 15:62-65 (Pubitemid 23015847)
    • (1993) Enzyme and Microbial Technology , vol.15 , Issue.1 , pp. 62-65
    • Xin, Z.1    Yinbo, Q.2    Peiji, G.3
  • 45
    • 0000822014 scopus 로고    scopus 로고
    • Purification and characterization of a glucose-tolerant β-glucosidase from Aspergillus niger CCRC 31494
    • Yan T, Lin C (1997) Purification and characterization of a glucosetolerant β-glucosidase from Aspergillus niger CCRC 31494. Biosci Biotechnol Biochem 61:965-970 (Pubitemid 27369474)
    • (1997) Bioscience, Biotechnology and Biochemistry , vol.61 , Issue.6 , pp. 965-970
    • Yan, T.-R.1    Lin, C.-L.2
  • 46
    • 49349101730 scopus 로고    scopus 로고
    • Non-ionic surfactants and non-catalytic protein treatment on enzymatic hydrolysis of pretreated creeping wild ryegrass
    • Zheng Y, Pan Z, Zhang R, Wang D, Jenkins B (2008) Non-ionic surfactants and non-catalytic protein treatment on enzymatic hydrolysis of pretreated creeping wild ryegrass. Appl Biochem Biotechnol 146:231-248
    • (2008) Appl Biochem Biotechnol , vol.146 , pp. 231-248
    • Zheng, Y.1    Pan, Z.2    Zhang, R.3    Wang, D.4    Jenkins, B.5


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