메뉴 건너뛰기




Volumn 13, Issue 2, 2009, Pages 345-354

Purification and biochemical characterization of a native invertase from the hydrogen-producing Thermotoga neapolitana (DSM 4359)

Author keywords

Invertase; Solute binding protein; Thermophilic; Thermotoga neapolitana; Thermotogales

Indexed keywords

BETA FRUCTOFURANOSIDASE; INULIN; ION; METAL; POLYMER;

EID: 61449083524     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-008-0222-2     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 2442458877 scopus 로고    scopus 로고
    • The three-dimensional structure of invertase (β-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an inverting glycosidases
    • F Alberto C Bignon G Sulzenbacher B Henrissat M Czjzek 2004 The three-dimensional structure of invertase (β-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an inverting glycosidases J Biol Chem 279 18903 18910
    • (2004) J Biol Chem , vol.279 , pp. 18903-18910
    • Alberto, F.1    Bignon, C.2    Sulzenbacher, G.3    Henrissat, B.4    Czjzek, M.5
  • 2
    • 33646253657 scopus 로고    scopus 로고
    • Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose
    • F Alberto E Jordi B Henrissat M Czjzek 2006 Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose Biochem J 395 457 462
    • (2006) Biochem J , vol.395 , pp. 457-462
    • Alberto, F.1    Jordi, E.2    Henrissat, B.3    Czjzek, M.4
  • 4
    • 0028357521 scopus 로고
    • Purification and characterization of sucrose α-glucohydrolase (invertase) from the hyperthermophilic archaeon Pyrococcus furiosus
    • HR Badr KA Sims MWW Adams 1994 Purification and characterization of sucrose α-glucohydrolase (invertase) from the hyperthermophilic archaeon Pyrococcus furiosus System Appl Microbiol 17 1 6
    • (1994) System Appl Microbiol , vol.17 , pp. 1-6
    • Badr, H.R.1    Sims, K.A.2    Adams, M.W.W.3
  • 5
    • 0017030513 scopus 로고
    • New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere
    • WE Balch RS Wolfe 1976 New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere Appl Environ Microbiol 32 781 791
    • (1976) Appl Environ Microbiol , vol.32 , pp. 781-791
    • Balch, W.E.1    Wolfe, R.S.2
  • 6
    • 33748037939 scopus 로고
    • Amylases α and β
    • P Bernfeld 1955 Amylases α and β Methods Enzymol 1 149 158
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 7
    • 0027155829 scopus 로고
    • Molecular characterization of a fructanase produced by Bacteroides fragilis BF-1
    • GL Blatch DR Woods 1993 Molecular characterization of a fructanase produced by Bacteroides fragilis BF-1 J Bacteriol 175 3058 3066
    • (1993) J Bacteriol , vol.175 , pp. 3058-3066
    • Blatch, G.L.1    Woods, D.R.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • MM Bradford 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding Anal Biochem 72 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 27144509128 scopus 로고    scopus 로고
    • An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima
    • SB Conners CI Montero DA Comfort KR Shockley MR Johnson SR Chhabra RM Kelly 2005 An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima J Bacteriol 187 7267 7282
    • (2005) J Bacteriol , vol.187 , pp. 7267-7282
    • Conners, S.B.1    Montero, C.I.2    Comfort, D.A.3    Shockley, K.R.4    Johnson, M.R.5    Chhabra, S.R.6    Kelly, R.M.7
  • 10
    • 78651153791 scopus 로고
    • Disc electrophoresis II. Method and application to human serum proteins
    • BJ Davis 1964 Disc electrophoresis II. Method and application to human serum proteins Ann NY Acad Sci 121 404 427
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 11
    • 0027253969 scopus 로고
    • Cloning and characterization of β-galactoside and β-glucoside hydrolysing enzymes of Thermotoga maritima
    • J Gabelsberger W Liebl KH Schleifer 1993 Cloning and characterization of β-galactoside and β-glucoside hydrolysing enzymes of Thermotoga maritima FEMS Microbiol Lett 109 131 138
    • (1993) FEMS Microbiol Lett , vol.109 , pp. 131-138
    • Gabelsberger, J.1    Liebl, W.2    Schleifer, K.H.3
  • 12
    • 0029778801 scopus 로고    scopus 로고
    • The glucose transport system of the hyperthermophilic anaerobic bacterium Thermotoga neapolitana
    • MY Galperin KM Noll AH Romano 1996 The glucose transport system of the hyperthermophilic anaerobic bacterium Thermotoga neapolitana Appl Environ Microbiol 62 2915 2918
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2915-2918
    • Galperin, M.Y.1    Noll, K.M.2    Romano, A.H.3
  • 13
    • 0031030475 scopus 로고    scopus 로고
    • Coregulation of β-galactoside uptake and hydrolysis by the hyperthermophilic bacterium Thermotoga neapolitana
    • MY Galperin KM Noll AH Romano 1997 Coregulation of β-galactoside uptake and hydrolysis by the hyperthermophilic bacterium Thermotoga neapolitana Appl Environ Microbiol 63 969 972
    • (1997) Appl Environ Microbiol , vol.63 , pp. 969-972
    • Galperin, M.Y.1    Noll, K.M.2    Romano, A.H.3
  • 15
    • 0035145163 scopus 로고    scopus 로고
    • Classification of glycoside hydrolases and glycosyltransferases from hyperthermophiles
    • B Henrissat PM Coutinho 2001 Classification of glycoside hydrolases and glycosyltransferases from hyperthermophiles Methods Enzymol Part A 330 183 201
    • (2001) Methods Enzymol Part A , vol.330 , pp. 183-201
    • Henrissat, B.1    Coutinho, P.M.2
  • 16
    • 77956868541 scopus 로고
    • A roll-tube method for the cultivation of strict anaerobes
    • RE Hungate 1969 A roll-tube method for the cultivation of strict anaerobes Methods Microbiol 3B 117 132
    • (1969) Methods Microbiol , vol.3 , pp. 117-132
    • Hungate, R.E.1
  • 17
    • 0015979809 scopus 로고
    • Purification and some properties of an endocellular sucrase from a constitutive mutant of Bacillus subtilis Marburg 168
    • F Kunst M Pascal J-A Lepesant J Walle R Dedonder 1974 Purification and some properties of an endocellular sucrase from a constitutive mutant of Bacillus subtilis Marburg 168 Eur J Biochem 42 611 620
    • (1974) Eur J Biochem , vol.42 , pp. 611-620
    • Kunst, F.1    Pascal, M.2    Lepesant, J.-A.3    Walle, J.4    Dedonder, R.5
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • UK Laemmli 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.K.1
  • 19
    • 0030468569 scopus 로고    scopus 로고
    • Purification and characterization of neutral and alkaline invertase from carrot
    • H-S Lee A Sturm 1996 Purification and characterization of neutral and alkaline invertase from carrot Plant Physiol 112 1513 1522
    • (1996) Plant Physiol , vol.112 , pp. 1513-1522
    • Lee, H.-S.1    Sturm, A.2
  • 20
    • 0028123353 scopus 로고
    • Comparative amino acid sequence analysis of Thermotoga maritima β-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between β-glucosidases of the BGA family and other families of β-1, 4-glycosyl hydrolases
    • W Liebl J Gabelsberger KH Schleifer 1994 Comparative amino acid sequence analysis of Thermotoga maritima β-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between β-glucosidases of the BGA family and other families of β-1, 4-glycosyl hydrolases Mol Gen Genet 242 111 115
    • (1994) Mol Gen Genet , vol.242 , pp. 111-115
    • Liebl, W.1    Gabelsberger, J.2    Schleifer, K.H.3
  • 21
    • 0031855806 scopus 로고    scopus 로고
    • Analysis of the gene for the β-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima and characterisation of the enzyme expressed in Escherichia coli
    • W Liebl D Bren A Gotschlich 1998 Analysis of the gene for the β-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima and characterisation of the enzyme expressed in Escherichia coli Appl Microbiol Biotechnol 50 55 64
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 55-64
    • Liebl, W.1    Bren, D.2    Gotschlich, A.3
  • 22
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • P Matsudaira 1987 Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes J Biol Chem 262 10035 10038
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 23
    • 0036856399 scopus 로고    scopus 로고
    • Periplasmic maltose- and glucose-binding protein activities in cell-free extracts of Thermotoga maritima
    • D Nanavati KM Noll AH Romano 2002 Periplasmic maltose- and glucose-binding protein activities in cell-free extracts of Thermotoga maritima Microbiology 148 3531 3537
    • (2002) Microbiology , vol.148 , pp. 3531-3537
    • Nanavati, D.1    Noll, K.M.2    Romano, A.H.3
  • 26
    • 39549103079 scopus 로고    scopus 로고
    • Evolution of mal ABC transporter operons in the Thermococcales and Thermotogales
    • KM Noll P Lapierre JP Gogarten DM Nanavati 2008 Evolution of mal ABC transporter operons in the Thermococcales and Thermotogales BMC Evol Biol 8 7
    • (2008) BMC Evol Biol , vol.8 , pp. 7
    • Noll, K.M.1    Lapierre, P.2    Gogarten, J.P.3    Nanavati, D.M.4
  • 27
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • DJ Pappin P Hojrup AJ Bleasby 1993 Rapid identification of proteins by peptide-mass fingerprinting Curr Biol 3 327 332
    • (1993) Curr Biol , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 29
    • 0034604396 scopus 로고    scopus 로고
    • Microbial genome analyses: Comparative transport capabilities in eighteen prokaryotes
    • IT Paulsen L Nguyen MK Sliwinski R Rabus MH Saier Jr 2000 Microbial genome analyses: comparative transport capabilities in eighteen prokaryotes J Mol Biol 301 75 100
    • (2000) J Mol Biol , vol.301 , pp. 75-100
    • Paulsen, I.T.1    Nguyen, L.2    Sliwinski, M.K.3    Rabus, R.4    Saier Jr, M.H.5
  • 31
    • 0020317258 scopus 로고
    • Plasmid-mediated uptake and metabolism of sucrose by Escherichia coli K12
    • K Schmid M Schupfner R Schmitt 1982 Plasmid-mediated uptake and metabolism of sucrose by Escherichia coli K12 J Bacteriol 151 68 76
    • (1982) J Bacteriol , vol.151 , pp. 68-76
    • Schmid, K.1    Schupfner, M.2    Schmitt, R.3
  • 33
    • 34249333446 scopus 로고    scopus 로고
    • Transglycosylation reactions using glycosyl hydrolases from Thermotoga neapolitana, a marine hydrogen-producing bacterium
    • A Tramice E Pagnotta I Romano A Gambacorta A Trincone 2007 Transglycosylation reactions using glycosyl hydrolases from Thermotoga neapolitana, a marine hydrogen-producing bacterium J Mol Cat 47 21 27
    • (2007) J Mol Cat , vol.47 , pp. 21-27
    • Tramice, A.1    Pagnotta, E.2    Romano, I.3    Gambacorta, A.4    Trincone, A.5
  • 34
    • 34247375264 scopus 로고    scopus 로고
    • A novel variant of Thermotoga neapolitana β-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation
    • P Turner D Svensson P Adlercreutz E Nodberg Karlsson 2007 A novel variant of Thermotoga neapolitana β-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation J Biotech 130 67 74
    • (2007) J Biotech , vol.130 , pp. 67-74
    • Turner, P.1    Svensson, D.2    Adlercreutz, P.3    Nodberg Karlsson, E.4
  • 35
    • 61449094966 scopus 로고    scopus 로고
    • United States Patent 6942998
    • Van Ooteghem SA (2005) United States Patent 6942998
    • (2005)
    • Van Ooteghem, S.A.1
  • 36
    • 0020987603 scopus 로고
    • Microbial inulinases: Fermentation process, properties and applications
    • EJ Vandamme DG Derycke 1983 Microbial inulinases: fermentation process, properties and applications Adv Appl Microbiol 29 139 176
    • (1983) Adv Appl Microbiol , vol.29 , pp. 139-176
    • Vandamme, E.J.1    Derycke, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.