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Volumn 86, Issue 4, 2010, Pages 1089-1097

An L-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: Cloning, expression, purification, and characterization

Author keywords

Acidothermus cellulolytics; Characterization; D Tagatose; L Arabinose isomerase; Purification

Indexed keywords

ACIDIC PH; AMINO ACID RESIDUES; CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; CONVERSION YIELD; D-GALACTOSE; D-TAGATOSE; DIVALENT METAL ION; ENZYMATIC ACTIVITIES; GEL FILTRATION; HIGH ACTIVITY; HIGHER TEMPERATURES; ION-EXCHANGE CHROMATOGRAPHY; L-ARABINOSE ISOMERASE; OPEN READING FRAME; OPTIMAL CONDITIONS; PURIFIED ENZYME; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; THERMOPHILIC BACTERIA;

EID: 77950629696     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2322-z     Document Type: Article
Times cited : (54)

References (35)
  • 1
    • 66449135412 scopus 로고    scopus 로고
    • Complete genome of the cellulolytic thermophile Acidothermus cellulolyticus 11B provides insights into its ecophysiological and evolutionary adaptations
    • doi:10.1101/gr.084848.108
    • Barabote RD, Xie G, Leu DH et al (2009) Complete genome of the cellulolytic thermophile Acidothermus cellulolyticus 11B provides insights into its ecophysiological and evolutionary adaptations. Genome Res. doi:10.1101/gr.084848.108
    • (2009) Genome Res.
    • Barabote, R.D.1    Xie, G.2    Leu, D.H.3
  • 3
    • 0027551680 scopus 로고
    • Bioconversion of D-galactose into otagatose
    • Cheetham P, Wootton A (1993) Bioconversion of D-galactose into Dtagatose. Enzyme Microb Technol 15:105-108
    • (1993) Enzyme Microb Technol , vol.15 , pp. 105-108
    • Cheetham, P.1    Wootton, A.2
  • 4
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • DOI 10.1111/j.1574-6968.2007.00961.x
    • Chouayekh H, Bejar W, Rhimi M, Jelleli K, Mseddi M, Bejar S (2007) Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH. FEMS Microbiol Lett 277:260-267 (Pubitemid 350145580)
    • (2007) FEMS Microbiology Letters , vol.277 , Issue.2 , pp. 260-267
    • Chouayekh, H.1    Bejar, W.2    Rhimi, M.3    Jelleli, K.4    Mseddi, M.5    Bejar, S.6
  • 5
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection of keto sugars and trioses
    • Dishe Z, Broenfreund E (1951) A new spectrophotometric method for the detection of keto sugars and trioses. J Biol Chem 192:583-587
    • (1951) J Biol Chem , vol.192 , pp. 583-587
    • Dishe, Z.1    Broenfreund, E.2
  • 6
    • 0033188539 scopus 로고    scopus 로고
    • D-Tagatose, a novel hexose: Acute effects on carbohydrate tolerance in subjects with and without type 2 diabetes
    • Donner TW, Wilber JF, Ostrowski D (1999) D-Tagatose, a novel hexose: acute effects on carbohydrate tolerance in subjects with and without type 2 diabetes. Diabetes Obes Metab 1:285-291
    • (1999) Diabetes Obes Metab , vol.1 , pp. 285-291
    • Donner, T.W.1    Wilber, J.F.2    Ostrowski, D.3
  • 7
    • 0002592987 scopus 로고    scopus 로고
    • Stability of biocatalysts process biotechnology
    • Illanes A (1999) Stability of biocatalysts process biotechnology. Electronic J Biotechnol 2:7-15
    • (1999) Electronic J Biotechnol , vol.2 , pp. 7-15
    • Illanes, A.1
  • 9
    • 3142713057 scopus 로고    scopus 로고
    • Enzymatic conversion of D-galactose to D-tagatose: Heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii
    • DOI 10.1007/s00253-004-1578-6
    • Jørgensen F, Hansen O, Stougaard P (2004) Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii. Appl Microbiol Biotechnol 64:816-822 (Pubitemid 38918145)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.6 , pp. 816-822
    • Jorgensen, F.1    Hansen, O.C.2    Stougaard, P.3
  • 10
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using L-arabinose isomerase: A review and future perspective
    • DOI 10.1007/s00253-004-1665-8
    • Kim P (2004) Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective. Appl Microbiol Biotechnol 65:243-249 (Pubitemid 39222466)
    • (2004) Applied Microbiology and Biotechnology , vol.65 , Issue.3 , pp. 243-249
    • Kim, P.1
  • 11
    • 26444526645 scopus 로고    scopus 로고
    • Purification and characterization of an larabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing d-tagatose
    • Kim HJ, Oh DK (2005) Purification and characterization of an larabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing d-tagatose. J Biotechnol 120:162-173
    • (2005) J Biotechnol , vol.120 , pp. 162-173
    • Kim, H.J.1    Oh, D.K.2
  • 12
    • 0037129833 scopus 로고    scopus 로고
    • Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: Bioconversion of D-galactose to D-tagatose using the enzyme
    • Kim BC, Lee YH, Lee HS, Lee DW, Choe EA, Pyun YR (2002) Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: bioconversion of D-galactose to D-tagatose using the enzyme. FEMS Microbiol Lett 212:121-126
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 121-126
    • Kim, B.C.1    Lee, Y.H.2    Lee, H.S.3    Lee, D.W.4    Choe, E.A.5    Pyun, Y.R.6
  • 13
    • 0037357583 scopus 로고    scopus 로고
    • A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor
    • DOI 10.1021/bp025675f
    • Kim HJ, Ryu SA, Kim P, Oh DK (2003a) A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol Prog 19:400-404 (Pubitemid 36420989)
    • (2003) Biotechnology Progress , vol.19 , Issue.2 , pp. 400-404
    • Kim, H.-J.1    Ryu, S.-A.2    Kim, P.3    Oh, D.-K.4
  • 14
    • 0037742418 scopus 로고    scopus 로고
    • Production of tagatose by a recombinant thermostable Larabinose isomerase from Thermus sp. IM6501
    • Kim JW, Kim YW, Roh HJ, Kim HY, Cha JH, Park KH, Park CS (2003b) Production of tagatose by a recombinant thermostable Larabinose isomerase from Thermus sp. IM6501. Biotechnol Lett 25:963-967
    • (2003) Biotechnol Lett , vol.25 , pp. 963-967
    • Kim, J.W.1    Kim, Y.W.2    Roh, H.J.3    Kim, H.Y.4    Cha, J.H.5    Park, K.H.6    Park, C.S.7
  • 15
    • 33144484509 scopus 로고    scopus 로고
    • Characterization of an Agrobacterium tumefaciens D-psicose-3-epimerase that converts D-fructose to D-psicose
    • Kim HJ, Hyun EK, Kim YS, Lee YJ, Oh DK (2006) Characterization of an Agrobacterium tumefaciens D-psicose-3-epimerase that converts D-fructose to D-psicose. Appl Environ Microbiol 72:981-985
    • (2006) Appl Environ Microbiol , vol.72 , pp. 981-985
    • Kim, H.J.1    Hyun, E.K.2    Kim, Y.S.3    Lee, Y.J.4    Oh, D.K.5
  • 16
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima
    • Lee DW, Jang HJ, Choe EA (2004) Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima. Appl Environ Microbiol 70:1397-1404
    • (2004) Appl Environ Microbiol , vol.70 , pp. 1397-1404
    • Lee, D.W.1    Jang, H.J.2    Choe, E.A.3
  • 17
    • 11444258321 scopus 로고    scopus 로고
    • Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerase from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
    • Lee DW, Choe EA, Kim SB, Eom SH, Hong YH, Lee SJ, Lee HS, Lee DY, Pyun YR (2005a) Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerase from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus. Arch Biochem Biophys 434:333-343
    • (2005) Arch Biochem Biophys , vol.434 , pp. 333-343
    • Lee, D.W.1    Choe, E.A.2    Kim, S.B.3    Eom, S.H.4    Hong, Y.H.5    Lee, S.J.6    Lee, H.S.7    Lee, D.Y.8    Pyun, Y.R.9
  • 18
    • 29144453887 scopus 로고    scopus 로고
    • Characterization of a thermoacidophilic Larabinose isomerase from Alicyclobacillus acidocaldarius: Role of Lys-269 in pH optimum
    • Lee SJ, Lee DW, Choe EA, Hong YH, Kim SB, Kim BC, Pyun YR (2005b) Characterization of a thermoacidophilic Larabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum. Appl Environ Microbiol 71:7888-7896
    • (2005) Appl Environ Microbiol , vol.71 , pp. 7888-7896
    • Lee, S.J.1    Lee, D.W.2    Choe, E.A.3    Hong, Y.H.4    Kim, S.B.5    Kim, B.C.6    Pyun, Y.R.7
  • 19
    • 0036011228 scopus 로고    scopus 로고
    • Tagatose, the new GRAS sweetener and health product
    • Levin GV (2002) Tagatose, the new GRAS sweetener and health product. J Med Food 5:23-36
    • (2002) J Med Food , vol.5 , pp. 23-36
    • Levin, G.V.1
  • 21
    • 38049186809 scopus 로고    scopus 로고
    • Tagatose, a new antidiabetic and obesity control drug
    • Lu Y, Levin GV, Donner TW (2008) Tagatose, a new antidiabetic and obesity control drug. Diabetes Obes Metab 10:109-134
    • (2008) Diabetes Obes Metab , vol.10 , pp. 109-134
    • Lu, Y.1    Levin, G.V.2    Donner, T.W.3
  • 22
    • 33745287171 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production
    • Manjasetty BA, Chance MR (2006) Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production. J Mol Biol 360:297-309
    • (2006) J Mol Biol , vol.360 , pp. 297-309
    • Manjasetty, B.A.1    Chance, M.R.2
  • 24
    • 0022445093 scopus 로고
    • Isolation and characterization of Acidothermus cellulolyticus gen. nov., sp. nov., a new genus of thermophilic, acidophilic, cellulolytic bacteria
    • Mohagheghi A, Grohmann K, Himmel M, Updegraff DM (1986) Isolation and characterization of Acidothermus cellulolytics gen. nov., sp. nov., a new genus of thermophilic, acidophilic, cellulolytic bacteria. Int J Syst Bacteriol 36:435-443 (Pubitemid 16057136)
    • (1986) International Journal of Systematic Bacteriology , vol.36 , Issue.3 , pp. 435-443
    • Mohagheghi, A.1    Grohmann, K.2    Himmel, M.3
  • 25
    • 0014682971 scopus 로고
    • Crystallization and properties of Larabinose isomerase from Lactobacillus gayonii
    • Nakamatu T, Yamanaka K (1969) Crystallization and properties of Larabinose isomerase from Lactobacillus gayonii. Biochim Biophys Acta 178:156-165
    • (1969) Biochim Biophys Acta , vol.178 , pp. 156-165
    • Nakamatu, T.1    Yamanaka, K.2
  • 26
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: Properties, applications, and biotechnological processes
    • Oh DK (2007) Tagatose: properties, applications, and biotechnological processes. Appl Microbiol Biotechnol 76:1-8
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 1-8
    • Oh, D.K.1
  • 27
    • 0014429922 scopus 로고
    • Purification and properties of an L-arabinose isomerase from Escherichia coli
    • Patrick JW, Lee N (1968) Purification and properties of an L-arabinose isomerase from Escherichia coli. J Biol Chem 243:4312-4318
    • (1968) J Biol Chem , vol.243 , pp. 4312-4318
    • Patrick, J.W.1    Lee, N.2
  • 28
    • 34648819320 scopus 로고    scopus 로고
    • Cloning, sequencing, overexpression and characterization of L-rhamnose isomerase from Bacillus pallidus Y25 for rare sugar production
    • DOI 10.1007/s00253-007-1109-3
    • Poonperm W, Takata G, Okada H, Morimoto K, Granström TB, Izumori K (2007) Cloning, sequencing, overexpression and characterization of L-rhamnose isomerase from Bacillus pallidus Y25 for rare sugar production. Appl Microbiol Biotechnol 76:1297-1307 (Pubitemid 47459780)
    • (2007) Applied Microbiology and Biotechnology , vol.76 , Issue.6 , pp. 1297-1307
    • Poonperm, W.1    Takata, G.2    Okada, H.3    Morimoto, K.4    Granstrom, T.B.5    Izumori, K.6
  • 30
    • 33644629689 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain
    • DOI 10.1016/j.bbagen.2005.11.007, PII S0304416505003582
    • Rhimi M, Bejar S (2006) Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive L-arabinose isomerase from the Bacillus stearothermophilus US100 strain. Biochim Biophys Acta 1760:191-199 (Pubitemid 43320507)
    • (2006) Biochimica et Biophysica Acta - General Subjects , vol.1760 , Issue.2 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 31
    • 4444333616 scopus 로고    scopus 로고
    • Bioconversion of D-galactitol to tagatose and dehydrogenase activity induction in Gluconobacter oxydans
    • DOI 10.1016/j.procbio.2004.01.028, PII S0032959204000494
    • Rollini M, Manzoni M (2005) Bioconversion of D-galactitol to tagatose and dehydrogenase activity induction in Gluconobacter oxydans. Process Biochem 40:437-444 (Pubitemid 39197440)
    • (2005) Process Biochemistry , vol.40 , Issue.1 , pp. 437-444
    • Rollini, M.1    Manzoni, M.2
  • 33
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito H, Miura K (1963) Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72:619-629
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 34
    • 0026728552 scopus 로고
    • Kinetics of galactose and tagatose formation during heat-treatment of milk
    • Troyono E, Martinez-Castro I, Olano A (1992) Kinetics of galactose and tagatose formation during heat-treatment of milk. Food Chem 45:41-43
    • (1992) Food Chem , vol.45 , pp. 41-43
    • Troyono, E.1    Martinez-Castro, I.2    Olano, A.3
  • 35
    • 0037299866 scopus 로고    scopus 로고
    • Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production
    • DOI 10.1023/A:1022575601492
    • Yoon SH, Kim P, Oh DK (2003) Properties of L-arabinose isomerase from Escherichia coli as biocatalysis for tagatose production. World J Microbiol Biotechnol 19:47-51 (Pubitemid 36357487)
    • (2003) World Journal of Microbiology and Biotechnology , vol.19 , Issue.1 , pp. 47-51
    • Yoon, S.-H.1    Kim, P.2    Oh, D.-K.3


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