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Volumn 155, Issue 3, 2011, Pages 338-349

Levansucrases from Pseudomonas syringae pv. tomato and P. chlororaphis subsp. aurantiaca: Substrate specificity, polymerizing properties and usage of different acceptors for fructosylation

Author keywords

Directed mutagenesis; Fructooligosaccharides; Heterooligofructans; Lsc3; Random mutagenesis

Indexed keywords

DIRECTED MUTAGENESIS; FRUCTO-OLIGOSACCHARIDES; HETEROOLIGOFRUCTANS; LSC3; RANDOM MUTAGENESIS;

EID: 80052356113     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.07.026     Document Type: Article
Times cited : (57)

References (62)
  • 1
    • 43849102032 scopus 로고    scopus 로고
    • Coupling of fully automated chip-based electrospray ionization to high-capacity ion trap mass spectrometer for ganglioside analysis
    • Almeida R., Mosoarca C., Chirita M., Udrescu V., Dinca N., Vukelić Z., Allen M., Zamfir A.D. Coupling of fully automated chip-based electrospray ionization to high-capacity ion trap mass spectrometer for ganglioside analysis. Anal. Biochem. 2008, 378:43-52.
    • (2008) Anal. Biochem. , vol.378 , pp. 43-52
    • Almeida, R.1    Mosoarca, C.2    Chirita, M.3    Udrescu, V.4    Dinca, N.5    Vukelić, Z.6    Allen, M.7    Zamfir, A.D.8
  • 3
    • 0039848317 scopus 로고    scopus 로고
    • Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity
    • Batista F.R., Hernandez L., Fernandez J.R., Arrieta J., Menendez C., Gomez R., Tambara Y., Pons T. Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity. Biochem. J. 1999, 337:503-506.
    • (1999) Biochem. J. , vol.337 , pp. 503-506
    • Batista, F.R.1    Hernandez, L.2    Fernandez, J.R.3    Arrieta, J.4    Menendez, C.5    Gomez, R.6    Tambara, Y.7    Pons, T.8
  • 5
    • 33646341761 scopus 로고    scopus 로고
    • The capacity of short-chain fructo-oligosaccharides to stimulate faecal bifidobacteria: a dose-response relationship study in healthy humans
    • Bouhnik Y., Raskine L., Simoneau G., Paineau D., Bornet F. The capacity of short-chain fructo-oligosaccharides to stimulate faecal bifidobacteria: a dose-response relationship study in healthy humans. Nutr. J. 2006, 5:8.
    • (2006) Nutr. J. , vol.5 , pp. 8
    • Bouhnik, Y.1    Raskine, L.2    Simoneau, G.3    Paineau, D.4    Bornet, F.5
  • 6
    • 80052378824 scopus 로고    scopus 로고
    • Production of fructo-oligosaccharides from sucrose by two levansucrases from Pseudomonas aurantiaca and Zymomonas mobilis
    • Byun S.H., Han W.C., Kang S.A., Kim C.H., Jang K.H. Production of fructo-oligosaccharides from sucrose by two levansucrases from Pseudomonas aurantiaca and Zymomonas mobilis. J. Biotechnol. 2007, 131:S112.
    • (2007) J. Biotechnol. , vol.131
    • Byun, S.H.1    Han, W.C.2    Kang, S.A.3    Kim, C.H.4    Jang, K.H.5
  • 10
    • 0025861055 scopus 로고
    • Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis
    • Chambert R., Petit-Glatron M.F. Polymerase and hydrolase activities of Bacillus subtilis levansucrase can be separately modulated by site-directed mutagenesis. Biochem. J. 1991, 279:35-41.
    • (1991) Biochem. J. , vol.279 , pp. 35-41
    • Chambert, R.1    Petit-Glatron, M.F.2
  • 11
    • 0027368002 scopus 로고
    • Structural identification of oligosaccharides produced by Zymomonas mobilis levansucrase
    • Crittenden R.G., Doelle H.W. Structural identification of oligosaccharides produced by Zymomonas mobilis levansucrase. Biotechnol. Lett. 1993, 15:1055-1060.
    • (1993) Biotechnol. Lett. , vol.15 , pp. 1055-1060
    • Crittenden, R.G.1    Doelle, H.W.2
  • 12
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase
    • Geiser M., Cebe R., Drewello D., Schmitz R. Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase. BioTechniques 2001, 31:88-92.
    • (2001) BioTechniques , vol.31 , pp. 88-92
    • Geiser, M.1    Cebe, R.2    Drewello, D.3    Schmitz, R.4
  • 13
    • 57749108291 scopus 로고    scopus 로고
    • Two active forms of Zymomonas mobilis levansucrase: an ordered microfibril structure of the enzyme promotes levan polymerization
    • Goldman D., Lavid N., Schwartz A., Shoham G., Danino D., Shoham Y. Two active forms of Zymomonas mobilis levansucrase: an ordered microfibril structure of the enzyme promotes levan polymerization. J. Biol. Chem. 2008, 283:32209-32217.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32209-32217
    • Goldman, D.1    Lavid, N.2    Schwartz, A.3    Shoham, G.4    Danino, D.5    Shoham, Y.6
  • 17
    • 0029070512 scopus 로고
    • Purification and properties of an extracellular levansucrase from Pseudomonas syringae pv phaseolicola
    • Hettwer U., Gross M., Rudolph K. Purification and properties of an extracellular levansucrase from Pseudomonas syringae pv phaseolicola. J. Bacteriol. 1995, 177:2834-2839.
    • (1995) J. Bacteriol. , vol.177 , pp. 2834-2839
    • Hettwer, U.1    Gross, M.2    Rudolph, K.3
  • 18
    • 0036694992 scopus 로고    scopus 로고
    • Molecular characterization of the levansucrase gene from Pseudomonas aurantiaca S-4380 and its expression in Escherchia coli
    • Jang E.K., Jang K.H., Koh I., Kim I.H., Kim S.H., Kang S.A., Kim C.H., Ha S.D., Rhee S.K. Molecular characterization of the levansucrase gene from Pseudomonas aurantiaca S-4380 and its expression in Escherchia coli. J. Microbiol. Biotechnol. 2002, 12:603-609.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 603-609
    • Jang, E.K.1    Jang, K.H.2    Koh, I.3    Kim, I.H.4    Kim, S.H.5    Kang, S.A.6    Kim, C.H.7    Ha, S.D.8    Rhee, S.K.9
  • 20
    • 33646192925 scopus 로고    scopus 로고
    • Mutagenesis of Xanthomonas campestris and selection of strains with enhanced xanthan production
    • Kamal F., Mehrgan H., Assadi M.M., Mortazavi S.A. Mutagenesis of Xanthomonas campestris and selection of strains with enhanced xanthan production. Iran Biomed. J. 2003, 7:91-98.
    • (2003) Iran Biomed. J. , vol.7 , pp. 91-98
    • Kamal, F.1    Mehrgan, H.2    Assadi, M.M.3    Mortazavi, S.A.4
  • 21
    • 0035135534 scopus 로고    scopus 로고
    • Acceptor reactions of a novel transfructosylating enzyme from Bacillus sp
    • Kim Y.M., Park J.P., Sinha J., Lim K.H., Yun J.W. Acceptor reactions of a novel transfructosylating enzyme from Bacillus sp. Biotehnol. Lett. 2001, 23:13-16.
    • (2001) Biotehnol. Lett. , vol.23 , pp. 13-16
    • Kim, Y.M.1    Park, J.P.2    Sinha, J.3    Lim, K.H.4    Yun, J.W.5
  • 22
    • 62349102392 scopus 로고    scopus 로고
    • Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications
    • Lammens W., Le Roy K., Schroeven L., Van Laere A., Rabijns A., Van den Ende W. Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications. J. Exp. Bot. 2009, 60:727-740.
    • (2009) J. Exp. Bot. , vol.60 , pp. 727-740
    • Lammens, W.1    Le Roy, K.2    Schroeven, L.3    Van Laere, A.4    Rabijns, A.5    Van den Ende, W.6
  • 23
    • 41549112339 scopus 로고    scopus 로고
    • Amino acid substitutions of His296 alter the catalytic properties of Zymomonas mobilis 10232 levansucrase
    • Li S.Y., Chen M., Li G., Yan Y.L., Yu H.Y., Zhan Y.H., Peng Z.X., Wang J., Lin M. Amino acid substitutions of His296 alter the catalytic properties of Zymomonas mobilis 10232 levansucrase. Acta Biochim. Pol. 2008, 55:201-206.
    • (2008) Acta Biochim. Pol. , vol.55 , pp. 201-206
    • Li, S.Y.1    Chen, M.2    Li, G.3    Yan, Y.L.4    Yu, H.Y.5    Zhan, Y.H.6    Peng, Z.X.7    Wang, J.8    Lin, M.9
  • 25
    • 0033989881 scopus 로고    scopus 로고
    • Metabolization of β-(2,6)-linked fructose-oligosaccharides by different bifidobacteria
    • Marx S.P., Winkler S., Hartmeier W. Metabolization of β-(2,6)-linked fructose-oligosaccharides by different bifidobacteria. FEMS Microbiol. Lett. 2000, 182:163-169.
    • (2000) FEMS Microbiol. Lett. , vol.182 , pp. 163-169
    • Marx, S.P.1    Winkler, S.2    Hartmeier, W.3
  • 26
    • 0001369336 scopus 로고
    • A buffer solution for colorimetric comparison
    • McIlvaine T.C. A buffer solution for colorimetric comparison. J. Biol. Chem. 1921, 49:183-186.
    • (1921) J. Biol. Chem. , vol.49 , pp. 183-186
    • McIlvaine, T.C.1
  • 27
    • 0242490546 scopus 로고    scopus 로고
    • Structural framework of fructosyl transfer in Bacillus subtilis levansucrase
    • Meng G., Fütterer K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat. Struct. Biol. 2003, 10:935-941.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 935-941
    • Meng, G.1    Fütterer, K.2
  • 28
    • 41549120638 scopus 로고    scopus 로고
    • Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucrase
    • Meng G., Fütterer K. Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucrase. BMC Struct. Biol. 2008, 88:16.
    • (2008) BMC Struct. Biol. , vol.88 , pp. 16
    • Meng, G.1    Fütterer, K.2
  • 29
    • 0033823457 scopus 로고    scopus 로고
    • Production of fructosylxyloside by the new fructosyltransferase from Bacillus macerans EG-6
    • Nam S.W., Yun H.J., Ahn J.H., Kim K.H., Kim B.W. Production of fructosylxyloside by the new fructosyltransferase from Bacillus macerans EG-6. Biotechnol. Lett. 2000, 22:1243-1246.
    • (2000) Biotechnol. Lett. , vol.22 , pp. 1243-1246
    • Nam, S.W.1    Yun, H.J.2    Ahn, J.H.3    Kim, K.H.4    Kim, B.W.5
  • 30
    • 0022690946 scopus 로고
    • Difference in mode of inhibition between α-D-xylosyl β-D-fructoside and α-isomaltosyl β-D-fructoside in synthesis of glucan by Streptococcus mutans D-glucosyltransferase
    • Nisizawa T., Takeuchi K., Imai S., Kitahata S., Okada S. Difference in mode of inhibition between α-D-xylosyl β-D-fructoside and α-isomaltosyl β-D-fructoside in synthesis of glucan by Streptococcus mutans D-glucosyltransferase. Carbohydr. Res. 1986, 147:135-144.
    • (1986) Carbohydr. Res. , vol.147 , pp. 135-144
    • Nisizawa, T.1    Takeuchi, K.2    Imai, S.3    Kitahata, S.4    Okada, S.5
  • 31
    • 68849100746 scopus 로고    scopus 로고
    • Evaluation of cross-linked aggregates from purified Bacillus subtilis levansucrase mutants for transfructosylation reactions
    • Ortiz-Soto M.E., Rudiño-Piñera E., Rodriguez-Alegria M.E., Lopez Munguia A. Evaluation of cross-linked aggregates from purified Bacillus subtilis levansucrase mutants for transfructosylation reactions. BMC Biotechnol. 2009, 9:68.
    • (2009) BMC Biotechnol. , vol.9 , pp. 68
    • Ortiz-Soto, M.E.1    Rudiño-Piñera, E.2    Rodriguez-Alegria, M.E.3    Lopez Munguia, A.4
  • 32
    • 33645546180 scopus 로고    scopus 로고
    • The levansucrase and inulosucrase enzymes of Lactobacillus reuteri 121 catalyse processive and non-processive transglycosylation reactions
    • Ozimek L.K., Kralj S., van der Maarel M.J.E.C., Dijkhuizen L. The levansucrase and inulosucrase enzymes of Lactobacillus reuteri 121 catalyse processive and non-processive transglycosylation reactions. Microbiology 2006, 152:1187-1196.
    • (2006) Microbiology , vol.152 , pp. 1187-1196
    • Ozimek, L.K.1    Kralj, S.2    van der Maarel, M.J.E.C.3    Dijkhuizen, L.4
  • 33
    • 0038397303 scopus 로고    scopus 로고
    • Enzymatic synthesis of fructosyl oligosaccharides by levansucrase from Microbacterium laevaniformans ATCC 15953
    • Park H.E., Park N.H., Kim M.J., Lee T.H., Lee H.G., Yang J.Y., Cha J. Enzymatic synthesis of fructosyl oligosaccharides by levansucrase from Microbacterium laevaniformans ATCC 15953. Enzyme Microb. Technol. 2003, 32:820-827.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 820-827
    • Park, H.E.1    Park, N.H.2    Kim, M.J.3    Lee, T.H.4    Lee, H.G.5    Yang, J.Y.6    Cha, J.7
  • 34
    • 21144451878 scopus 로고    scopus 로고
    • Lactosucrose production by various microorganisms harboring levansucrase activity
    • Park N.-H., Choi H.-J., Oh D.-K. Lactosucrose production by various microorganisms harboring levansucrase activity. Biotechnol. Lett. 2005, 27:495-497.
    • (2005) Biotechnol. Lett. , vol.27 , pp. 495-497
    • Park, N.-H.1    Choi, H.-J.2    Oh, D.-K.3
  • 37
    • 34250329984 scopus 로고    scopus 로고
    • Expression vectors for enzyme restriction- and ligation-independent cloning for producing recombinant His-fusion proteins
    • Rivas B.d.l., Curiel J.A., Mancheño J.M., Muñoz R. Expression vectors for enzyme restriction- and ligation-independent cloning for producing recombinant His-fusion proteins. Biotechnol. Prog. 2007, 23:680-686.
    • (2007) Biotechnol. Prog. , vol.23 , pp. 680-686
    • Rivas, B.1    Curiel, J.A.2    Mancheño, J.M.3    Muñoz, R.4
  • 38
    • 34249719483 scopus 로고    scopus 로고
    • Overexpression, purification, crystallization and preliminary structural studies of p-coumaric acid decarboxylase from Lactobacillus plantarum
    • Rodríguez H., Rivas B.d.l., Muñoz R., Mancheño J.M. Overexpression, purification, crystallization and preliminary structural studies of p-coumaric acid decarboxylase from Lactobacillus plantarum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2007, 63:300-303.
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.63 , pp. 300-303
    • Rodríguez, H.1    Rivas, B.2    Muñoz, R.3    Mancheño, J.M.4
  • 39
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 40
    • 0032899645 scopus 로고    scopus 로고
    • Elevated temperature and chemical modification selectively abolishes levan forming activity of levansucrase of Zymomonas mobilis
    • Sangiliyandi G., Ray K.C., Gunasekaran P. Elevated temperature and chemical modification selectively abolishes levan forming activity of levansucrase of Zymomonas mobilis. Biotechnol. Lett. 1999, 21:179-182.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 179-182
    • Sangiliyandi, G.1    Ray, K.C.2    Gunasekaran, P.3
  • 41
    • 20544433205 scopus 로고    scopus 로고
    • Biocatalytic and chemical investigations in the synthesis of sucrose analogues
    • Seibel J., Moraru R., Götze S. Biocatalytic and chemical investigations in the synthesis of sucrose analogues. Tetrahedron 2005, 61:7081-7086.
    • (2005) Tetrahedron , vol.61 , pp. 7081-7086
    • Seibel, J.1    Moraru, R.2    Götze, S.3
  • 42
    • 33747772729 scopus 로고    scopus 로고
    • Synthesis of sucrose analogues and the mechanism of action of Bacillus subtilis fructosyltransferase (levansucrase)
    • Seibel J., Moraru R., Götze S., Buchholz K., Na'amnieh S., Pawlowski A., Hecht H.J. Synthesis of sucrose analogues and the mechanism of action of Bacillus subtilis fructosyltransferase (levansucrase). Carbohydr. Res. 2006, 41:2335-2349.
    • (2006) Carbohydr. Res. , vol.41 , pp. 2335-2349
    • Seibel, J.1    Moraru, R.2    Götze, S.3    Buchholz, K.4    Na'amnieh, S.5    Pawlowski, A.6    Hecht, H.J.7
  • 43
    • 7944222517 scopus 로고    scopus 로고
    • Development of Bifidobacterium lactis Bb 12 on β-(2,6)-linked fructan-containing substrate
    • Semjonovs S., Marauska M., Linde R., Grube M., Zikmanis P., Bekers M. Development of Bifidobacterium lactis Bb 12 on β-(2,6)-linked fructan-containing substrate. Eng. Life Sci. 2004, 4:433-437.
    • (2004) Eng. Life Sci. , vol.4 , pp. 433-437
    • Semjonovs, S.1    Marauska, M.2    Linde, R.3    Grube, M.4    Zikmanis, P.5    Bekers, M.6
  • 44
    • 0029665023 scopus 로고    scopus 로고
    • Preparation of electro-competent E. coli using saltfree growth medium
    • Sharma R.C., Schimke R.T. Preparation of electro-competent E. coli using saltfree growth medium. BioTechniques 1996, 20:42-44.
    • (1996) BioTechniques , vol.20 , pp. 42-44
    • Sharma, R.C.1    Schimke, R.T.2
  • 45
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H. Tricine-SDS-PAGE. Nat. Protoc. 2006, 1:16-22.
    • (2006) Nat. Protoc. , vol.1 , pp. 16-22
    • Schägger, H.1
  • 46
    • 79955961857 scopus 로고    scopus 로고
    • Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs
    • Strube C.P., Homann A., Gamer M., Jahn D., Seibel J., Heinz D.W. Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs. J. Biol. Chem. 2011, 286:17593-17600.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17593-17600
    • Strube, C.P.1    Homann, A.2    Gamer, M.3    Jahn, D.4    Seibel, J.5    Heinz, D.W.6
  • 47
    • 0037761896 scopus 로고    scopus 로고
    • A method for rapid quantification of sucrose and fructan oligosaccharides suitable for enzyme and physiological studies
    • St.John J.A., Bonnett G.D., Simpson R.J. A method for rapid quantification of sucrose and fructan oligosaccharides suitable for enzyme and physiological studies. New Phytol. 1996, 134:197-203.
    • (1996) New Phytol. , vol.134 , pp. 197-203
    • St John, J.A.1    Bonnett, G.D.2    Simpson, R.J.3
  • 48
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 1986, 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 49
    • 66449113450 scopus 로고    scopus 로고
    • Superiority of 1-kestose, the smallest fructo-oligosaccharide, to a synthetic mixture of fructo-oligosaccharides in the selective stimulating sctivity on bifidobacteria
    • Suzuki N., Aiba Y., Takeda H., Fukumori Y., Koga Y. Superiority of 1-kestose, the smallest fructo-oligosaccharide, to a synthetic mixture of fructo-oligosaccharides in the selective stimulating sctivity on bifidobacteria. Biosci. Microflora 2006, 25:109-116.
    • (2006) Biosci. Microflora , vol.25 , pp. 109-116
    • Suzuki, N.1    Aiba, Y.2    Takeda, H.3    Fukumori, Y.4    Koga, Y.5
  • 50
    • 0344937993 scopus 로고    scopus 로고
    • Structural analysis and optimised production of fructo-oligosaccharides by levansucrase from Acetobacter diazotrophicus SRT4
    • Tambara Y., Hormaza J.V., Perez C., Leon A., Arrieta J., Hernandez L. Structural analysis and optimised production of fructo-oligosaccharides by levansucrase from Acetobacter diazotrophicus SRT4. Biotechnol. Lett. 1999, 21:117-121.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 117-121
    • Tambara, Y.1    Hormaza, J.V.2    Perez, C.3    Leon, A.4    Arrieta, J.5    Hernandez, L.6
  • 51
    • 0027968068 scopus 로고
    • Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 15244342938 scopus 로고    scopus 로고
    • Molecular and functional characterization of a levansucrase from the sourdough isolate Lactobacillus sanfranciscensis TMW 1.392
    • Tieking M., Ehrmann M.A., Vogel R.F., Gänzle M.G. Molecular and functional characterization of a levansucrase from the sourdough isolate Lactobacillus sanfranciscensis TMW 1.392. Appl. Microbiol. Biotechnol. 2005, 66:655-663.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 655-663
    • Tieking, M.1    Ehrmann, M.A.2    Vogel, R.F.3    Gänzle, M.G.4
  • 53
    • 0035910182 scopus 로고    scopus 로고
    • Purification of a novel fructosyltransferase from Lactobacillus reuteri strain 121 and characterization of the levan produced
    • van Hijum S.A.F.T., Bonting K., van der Maarel M.J.E.C., Dijkhuizen L. Purification of a novel fructosyltransferase from Lactobacillus reuteri strain 121 and characterization of the levan produced. FEMS Microbiol. Lett. 2001, 205:323-328.
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 323-328
    • van Hijum, S.A.F.T.1    Bonting, K.2    van der Maarel, M.J.E.C.3    Dijkhuizen, L.4
  • 54
  • 55
    • 40649099520 scopus 로고    scopus 로고
    • Hansenula polymorpha maltase gene promoter with sigma 70-like elements is feasible for Escherichia coli-based biotechnological applications: expression of three genomic levansucrase genes of Pseudomonas syringae pv tomato
    • Visnapuu T., Mäe A., Alamäe T. Hansenula polymorpha maltase gene promoter with sigma 70-like elements is feasible for Escherichia coli-based biotechnological applications: expression of three genomic levansucrase genes of Pseudomonas syringae pv tomato. Process Biochem. 2008, 43:414-422.
    • (2008) Process Biochem. , vol.43 , pp. 414-422
    • Visnapuu, T.1    Mäe, A.2    Alamäe, T.3
  • 56
    • 66449092059 scopus 로고    scopus 로고
    • Fully automated chip-based negative mode nanoelectrospray mass spectrometry of fructooligosaccharides produced by heterologously expressed levansucrase from Pseudomonas syringae pv. tomato DC3000
    • Visnapuu T., Zamfir A.D., Mosoarca C., Stanescu M.D., Alamäe T. Fully automated chip-based negative mode nanoelectrospray mass spectrometry of fructooligosaccharides produced by heterologously expressed levansucrase from Pseudomonas syringae pv. tomato DC3000. Rapid Commun. Mass Spectrom. 2009, 23:1337-1346.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 1337-1346
    • Visnapuu, T.1    Zamfir, A.D.2    Mosoarca, C.3    Stanescu, M.D.4    Alamäe, T.5
  • 57
    • 52449128012 scopus 로고    scopus 로고
    • Genetic and functional characterization of Lactobacillus panis levansucrase
    • Waldherr F.W., Meissner D., Vogel R.F. Genetic and functional characterization of Lactobacillus panis levansucrase. Arch. Microbiol. 2008, 190:497-505.
    • (2008) Arch. Microbiol. , vol.190 , pp. 497-505
    • Waldherr, F.W.1    Meissner, D.2    Vogel, R.F.3
  • 58
    • 3242707573 scopus 로고    scopus 로고
    • An improvement of the site-directed mutagenesis method by combination of megaprimer, one-side PCR and DpnI treatment
    • Wei D., Li M., Zhang X., Xing L. An improvement of the site-directed mutagenesis method by combination of megaprimer, one-side PCR and DpnI treatment. Anal. Biochem. 2004, 331:401-403.
    • (2004) Anal. Biochem. , vol.331 , pp. 401-403
    • Wei, D.1    Li, M.2    Zhang, X.3    Xing, L.4
  • 60
    • 0036775911 scopus 로고    scopus 로고
    • Identification of functionally important aminoacid residues in Zymomonas mobilis levansucrase
    • Yanase H., Maeda M., Hagiwara E., Yagi H., Taniguchi K., Okamato K. Identification of functionally important aminoacid residues in Zymomonas mobilis levansucrase. J. Biochem. 2002, 132:565-572.
    • (2002) J. Biochem. , vol.132 , pp. 565-572
    • Yanase, H.1    Maeda, M.2    Hagiwara, E.3    Yagi, H.4    Taniguchi, K.5    Okamato, K.6
  • 61
    • 2642522774 scopus 로고    scopus 로고
    • Antitumor activity of levan polysaccharides from selected microorganisms
    • Yoo S.H., Yoon E.J., Cha J., Lee H.G. Antitumor activity of levan polysaccharides from selected microorganisms. Int. J. Biol. Macromol. 2004, 34:37-41.
    • (2004) Int. J. Biol. Macromol. , vol.34 , pp. 37-41
    • Yoo, S.H.1    Yoon, E.J.2    Cha, J.3    Lee, H.G.4
  • 62
    • 38149093213 scopus 로고    scopus 로고
    • Tailor-made fructooligosaccharides by a combination of substrate and genetic engineering
    • Zuccaro A., Götze S., Kneip S., Dersch P., Seibel J. Tailor-made fructooligosaccharides by a combination of substrate and genetic engineering. Chembiochem 2008, 9:143-149.
    • (2008) Chembiochem , vol.9 , pp. 143-149
    • Zuccaro, A.1    Götze, S.2    Kneip, S.3    Dersch, P.4    Seibel, J.5


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