메뉴 건너뛰기




Volumn 98, Issue 21, 2014, Pages 8869-8878

L-Arabinose isomerase and its use for biotechnological production of rare sugars

Author keywords

Biological catalysis; D Tagatose; L Arabinose isomerase; L Ribose; Rare sugar

Indexed keywords

CATALYSIS; ENZYMES; QUANTUM CHEMISTRY;

EID: 84925463294     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6073-0     Document Type: Review
Times cited : (67)

References (89)
  • 1
    • 0032719080 scopus 로고    scopus 로고
    • Biochemical preparation of L-ribose and L-arabinose from ribitol: a new approach
    • PID: 16232643, COI: 1:CAS:528:DyaK1MXnvFyjt7k%3D
    • Ahmed Z, Shimonishi T, Bhuiyan SH, Utamura M, Takada G, Izumori K (1999) Biochemical preparation of L-ribose and L-arabinose from ribitol: a new approach. J Biosci Bioeng 88(4):444–448
    • (1999) J Biosci Bioeng , vol.88 , Issue.4 , pp. 444-448
    • Ahmed, Z.1    Shimonishi, T.2    Bhuiyan, S.H.3    Utamura, M.4    Takada, G.5    Izumori, K.6
  • 3
    • 84863445834 scopus 로고    scopus 로고
    • Enzymes for the biocatalytic production of rare sugars
    • PID: 22350065, COI: 1:CAS:528:DC%2BC38XntlOntLo%3D
    • Beerens K, Desmet T, Soetaert W (2012) Enzymes for the biocatalytic production of rare sugars. J Ind Microbiol Biotechnol 39(6):823–834
    • (2012) J Ind Microbiol Biotechnol , vol.39 , Issue.6 , pp. 823-834
    • Beerens, K.1    Desmet, T.2    Soetaert, W.3
  • 4
    • 0033897686 scopus 로고    scopus 로고
    • D-Tagatose, a stereoisomer of D-fructose, increases blood uric acid concentration
    • PID: 10954012, COI: 1:CAS:528:DC%2BD3cXmtFShtrk%3D
    • Buemann B, Toubro S, Holst JJ, Rehfeld JF, Bibby BM, Astrup A (2000) D-Tagatose, a stereoisomer of D-fructose, increases blood uric acid concentration. Metabolism 49(8):969–976
    • (2000) Metabolism , vol.49 , Issue.8 , pp. 969-976
    • Buemann, B.1    Toubro, S.2    Holst, J.J.3    Rehfeld, J.F.4    Bibby, B.M.5    Astrup, A.6
  • 5
    • 1842531785 scopus 로고    scopus 로고
    • Generally recognized as safe (GRAS): history and description
    • PID: 15068820, COI: 1:CAS:528:DC%2BD2cXivVWms7k%3D
    • Burdock GA, Carabin IG (2004) Generally recognized as safe (GRAS): history and description. Toxicol Lett 150(1):3–18
    • (2004) Toxicol Lett , vol.150 , Issue.1 , pp. 3-18
    • Burdock, G.A.1    Carabin, I.G.2
  • 6
    • 0027551680 scopus 로고
    • Bioconversion of D-galactose into D-tagatose
    • COI: 1:CAS:528:DyaK3sXhtVSntrs%3D
    • Cheetham PSJ, Wootton AN (1993) Bioconversion of D-galactose into D-tagatose. Enzyme Microb Technol 15:105–108
    • (1993) Enzyme Microb Technol , vol.15 , pp. 105-108
    • Cheetham, P.S.J.1    Wootton, A.N.2
  • 7
    • 77950629696 scopus 로고    scopus 로고
    • An L-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: cloning, expression, purification, and characterization
    • PID: 19921180, COI: 1:CAS:528:DC%2BC3cXjvVehs78%3D
    • Cheng L, Mu W, Zhang T, Jiang B (2010a) An L-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: cloning, expression, purification, and characterization. Appl Microbiol Biotechnol 86(4):1089–1097
    • (2010) Appl Microbiol Biotechnol , vol.86 , Issue.4 , pp. 1089-1097
    • Cheng, L.1    Mu, W.2    Zhang, T.3    Jiang, B.4
  • 8
    • 77952501933 scopus 로고    scopus 로고
    • Thermostable L-arabinose isomerase from Bacillus stearothermophilus IAM11001 for D-tagatose production: gene cloning, purification and characterisation
    • PID: 20474051, COI: 1:CAS:528:DC%2BC3cXmtV2jsLY%3D
    • Cheng L, Mu W, Jiang B (2010b) Thermostable L-arabinose isomerase from Bacillus stearothermophilus IAM11001 for D-tagatose production: gene cloning, purification and characterisation. J Sci Food Agric 90(8):1327–1333
    • (2010) J Sci Food Agric , vol.90 , Issue.8 , pp. 1327-1333
    • Cheng, L.1    Mu, W.2    Jiang, B.3
  • 9
    • 79957941383 scopus 로고    scopus 로고
    • A novel method to prepare L-arabinose from xylose mother liquor by yeast-mediated biopurification
    • PID: 21649890, COI: 1:CAS:528:DC%2BC3MXnvVOhu7c%3D
    • Cheng H, Wang H, Lv J, Jiang M, Lin S, Deng Z (2011) A novel method to prepare L-arabinose from xylose mother liquor by yeast-mediated biopurification. Microb cell fact 10(1):43
    • (2011) Microb cell fact , vol.10 , Issue.1 , pp. 43
    • Cheng, H.1    Wang, H.2    Lv, J.3    Jiang, M.4    Lin, S.5    Deng, Z.6
  • 10
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • PID: 18031349, COI: 1:CAS:528:DC%2BD2sXhsVersLzI
    • 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
    • (2007) FEMS Microbiol Lett , vol.277 , pp. 260-267
    • Chouayekh, H.1    Bejar, W.2    Rhimi, M.3    Jelleli, K.4    Mseddi, M.5    Bejar, S.6
  • 11
    • 62549090557 scopus 로고    scopus 로고
    • Highly efficient production of the staphylococcal nuclease reporter in Lactobacillus bulgaricus governed by the promoter of the hlbA gene
    • PID: 19243442, COI: 1:CAS:528:DC%2BD1MXktlaku7o%3D
    • Chouayekh H, Serror P, Boudebbouze S, Maguin E (2009) Highly efficient production of the staphylococcal nuclease reporter in Lactobacillus bulgaricus governed by the promoter of the hlbA gene. FEMS Microbiol Lett 293(2):232–239
    • (2009) FEMS Microbiol Lett , vol.293 , Issue.2 , pp. 232-239
    • Chouayekh, H.1    Serror, P.2    Boudebbouze, S.3    Maguin, E.4
  • 12
    • 28944434107 scopus 로고    scopus 로고
    • Boric acid as a mobile phase additive for high performance liquid chromatography separation of ribose, arabinose and ribulose
    • PID: 16253266
    • De Muynck C, Beauprez J, Soetaert W, Vandamme EJ (2006) Boric acid as a mobile phase additive for high performance liquid chromatography separation of ribose, arabinose and ribulose. J Chromatogr A 1101(1):115–121
    • (2006) J Chromatogr A , vol.1101 , Issue.1 , pp. 115-121
    • De Muynck, C.1    Beauprez, J.2    Soetaert, W.3    Vandamme, E.J.4
  • 13
    • 0033188539 scopus 로고    scopus 로고
    • D-Tagatose, a novel hexose: acute effects on carbohydrate tolerance in subjects with and without type 2 diabetes
    • PID: 11225640, COI: 1:CAS:528:DC%2BD3cXmtFClsQ%3D%3D
    • 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
  • 14
    • 84895532582 scopus 로고    scopus 로고
    • Biochemical characterization of a thermostable L-arabinose isomerase from a thermoacidophilic bacterium Alicyclobacillus hesperidum URH17-3-68
    • COI: 1:CAS:528:DC%2BC2cXlvFCitb0%3D
    • Fan C, Liu K, Zhang T, Zhou L, Xue D, Jia B, Mu W (2014) Biochemical characterization of a thermostable L-arabinose isomerase from a thermoacidophilic bacterium Alicyclobacillus hesperidum URH17-3-68. J Mol Catal B Enzym 102:120–126
    • (2014) J Mol Catal B Enzym , vol.102 , pp. 120-126
    • Fan, C.1    Liu, K.2    Zhang, T.3    Zhou, L.4    Xue, D.5    Jia, B.6    Mu, W.7
  • 15
    • 1542297643 scopus 로고    scopus 로고
    • Izumoring: a novel and complete strategy for bioproduction of rare sugars
    • PID: 16233597
    • Granström TB, Takata G, Tokuda M, Izumori K (2004) Izumoring: a novel and complete strategy for bioproduction of rare sugars. J Biosci Bioeng 97(2):89–94
    • (2004) J Biosci Bioeng , vol.97 , Issue.2 , pp. 89-94
    • Granström, T.B.1    Takata, G.2    Tokuda, M.3    Izumori, K.4
  • 16
    • 3142662891 scopus 로고
    • Pentose fermentation by Lactobacillus plantarum II. L-arabinose isomerase
    • PID: 13539034, COI: 1:CAS:528:DyaG1cXhtFOkur4%3D
    • Heath EC, Horecker BL, Smyrniotis PZ, Takagi Y (1958) Pentose fermentation by Lactobacillus plantarum II. L-arabinose isomerase. J Biol Chem 231(2):1031–1037
    • (1958) J Biol Chem , vol.231 , Issue.2 , pp. 1031-1037
    • Heath, E.C.1    Horecker, B.L.2    Smyrniotis, P.Z.3    Takagi, Y.4
  • 17
    • 35948946147 scopus 로고    scopus 로고
    • Metabolic engineering of Lactobacillus plantarum for production of L-ribulose
    • PID: 17873078, COI: 1:CAS:528:DC%2BD2sXhtlSksLfE
    • Helanto M, Kiviharju K, Leisola M, Nyyssölä A (2007) Metabolic engineering of Lactobacillus plantarum for production of L-ribulose. Appl Environ Microbiol 73(21):7083–7091
    • (2007) Appl Environ Microbiol , vol.73 , Issue.21 , pp. 7083-7091
    • Helanto, M.1    Kiviharju, K.2    Leisola, M.3    Nyyssölä, A.4
  • 19
    • 33847723004 scopus 로고    scopus 로고
    • Production of D-tagatose at high temperatures using immobilized Escherichia coli cells expressing L-arabinose isomerase from Thermotoga neapolitana
    • PID: 17206372, COI: 1:CAS:528:DC%2BD2sXis1ektbc%3D
    • Hong YH, Lee DW, Lee SJ, Choe EA, Kim SB, Lee YH, Cheigh CI, Pyun YR (2007) Production of D-tagatose at high temperatures using immobilized Escherichia coli cells expressing L-arabinose isomerase from Thermotoga neapolitana. Biotechnol Lett 29(4):569–574
    • (2007) Biotechnol Lett , vol.29 , Issue.4 , pp. 569-574
    • Hong, Y.H.1    Lee, D.W.2    Lee, S.J.3    Choe, E.A.4    Kim, S.B.5    Lee, Y.H.6    Cheigh, C.I.7    Pyun, Y.R.8
  • 20
    • 84255160731 scopus 로고    scopus 로고
    • Creation of metal-independent hyper thermophilic L-arabinose isomerase by homologous recombination
    • PID: 22103589, COI: 1:CAS:528:DC%2BC3MXhsV2nu7%2FM
    • Hong YH, Lee DW, Pyun YR, Lee SH (2011) Creation of metal-independent hyper thermophilic L-arabinose isomerase by homologous recombination. J Agric Food Chem 59(24):12939–12947
    • (2011) J Agric Food Chem , vol.59 , Issue.24 , pp. 12939-12947
    • Hong, Y.H.1    Lee, D.W.2    Pyun, Y.R.3    Lee, S.H.4
  • 21
    • 82355173285 scopus 로고    scopus 로고
    • Perspectives of biotechnological production of L-ribose and its purification
    • PID: 21874275, COI: 1:CAS:528:DC%2BC3MXht1yhur3J
    • Hu C, Li L, Zheng Y, Rui L, Hu C (2011) Perspectives of biotechnological production of L-ribose and its purification. Appl Microbiol Biotechnol 92:449–455
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 449-455
    • Hu, C.1    Li, L.2    Zheng, Y.3    Rui, L.4    Hu, C.5
  • 22
    • 84892959225 scopus 로고    scopus 로고
    • Characterization of a thermophilic L-arabinose isomerase from Thermoanaerobacterium saccharolyticum NTOU1
    • COI: 1:CAS:528:DC%2BC3sXptFClurg%3D
    • Hung XG, Tseng WC, Liu SM, Tzou WS, Fang TY (2014) Characterization of a thermophilic L-arabinose isomerase from Thermoanaerobacterium saccharolyticum NTOU1. Biochem Eng J 83:121–128
    • (2014) Biochem Eng J , vol.83 , pp. 121-128
    • Hung, X.G.1    Tseng, W.C.2    Liu, S.M.3    Tzou, W.S.4    Fang, T.Y.5
  • 23
    • 33847706656 scopus 로고    scopus 로고
    • Process for manufacturing D-tagatose
    • Ibrahim OO, Spradlin JE (2000) Process for manufacturing D-tagatose. US Patent 6:057,135
    • (2000) US Patent , vol.6 , pp. 057,135
    • Ibrahim, O.O.1    Spradlin, J.E.2
  • 24
    • 38249030954 scopus 로고
    • Production of D-tagatose from D-galactitol by Mycobacterium smegmatis
    • COI: 1:CAS:528:DyaL1cXktVGhtrg%3D
    • Izumori K, Tsuzaki K (1988) Production of D-tagatose from D-galactitol by Mycobacterium smegmatis. J Ferment Technol 66(2):225–227
    • (1988) J Ferment Technol , vol.66 , Issue.2 , pp. 225-227
    • Izumori, K.1    Tsuzaki, K.2
  • 25
    • 80755176655 scopus 로고    scopus 로고
    • Supramolecular stabilization of acid tolerant L-arabinose isomerase from Lactobacillus sakei
    • COI: 1:CAS:528:DC%2BC3MXhsVaqsb7I
    • Jebors S, Tauran Y, Aghajari N, Boudebbouze S, Maguin E, Haser R, Coleman AW, Rhimi M (2011) Supramolecular stabilization of acid tolerant L-arabinose isomerase from Lactobacillus sakei. Chem Commun 47(45):12307–12309
    • (2011) Chem Commun , vol.47 , Issue.45 , pp. 12307-12309
    • Jebors, S.1    Tauran, Y.2    Aghajari, N.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Coleman, A.W.7    Rhimi, M.8
  • 26
    • 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
    • PID: 15168095
    • JØrgensen F, Hansen OC, 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(6):816–822
    • (2004) Appl Microbiol Biotechnol , vol.64 , Issue.6 , pp. 816-822
    • JØrgensen, F.1    Hansen, O.C.2    Stougaard, P.3
  • 27
    • 23244444982 scopus 로고    scopus 로고
    • Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus L-arabinose isomerase mutant in a packed-bed bioreactor
    • PID: 16080720, COI: 1:CAS:528:DC%2BD2MXls1SjtL0%3D
    • Jung ES, Kim HJ, Oh DK (2005) Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus L-arabinose isomerase mutant in a packed-bed bioreactor. Biotechnol Prog 21(4):1335–1340
    • (2005) Biotechnol Prog , vol.21 , Issue.4 , pp. 1335-1340
    • Jung, E.S.1    Kim, H.J.2    Oh, D.K.3
  • 28
    • 85018150620 scopus 로고    scopus 로고
    • L-Ribose isomerase, its preparation and uses
    • Kagawa KI, Okayama KT (2001) L-Ribose isomerase, its preparation and uses. US patent 6,294,369 B1
    • (2001) US patent 6,294 , vol.369 , pp. B1
    • Kagawa, K.I.1    Okayama, K.T.2
  • 29
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective
    • COI: 1:CAS:528:DC%2BD2cXmsVCgurg%3D
    • Kim P (2004) Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective. Appl Microb Biotechnol 65(3):243–249
    • (2004) Appl Microb Biotechnol , vol.65 , Issue.3 , pp. 243-249
    • Kim, P.1
  • 30
    • 26444526645 scopus 로고    scopus 로고
    • Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose
    • PID: 16084621, COI: 1:CAS:528:DC%2BD2MXhtFSisLrL
    • Kim HJ, Oh DK (2005) Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose. J Biotechnol 120(2):162–173
    • (2005) J Biotechnol , vol.120 , Issue.2 , pp. 162-173
    • Kim, H.J.1    Oh, D.K.2
  • 31
    • 0035121730 scopus 로고    scopus 로고
    • High production of D-tagatose, a potential sugar substitute, using immobilized L-arabinose isomerase
    • PID: 11170501, COI: 1:CAS:528:DC%2BD3MXivVamug%3D%3D
    • Kim P, Yoon SH, Roh HJ, Choi JH (2001a) High production of D-tagatose, a potential sugar substitute, using immobilized L-arabinose isomerase. Biotechnol Prog 17(1):208–210
    • (2001) Biotechnol Prog , vol.17 , Issue.1 , pp. 208-210
    • Kim, P.1    Yoon, S.H.2    Roh, H.J.3    Choi, J.H.4
  • 32
    • 0034775246 scopus 로고    scopus 로고
    • Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase
    • PID: 11592915, COI: 1:CAS:528:DC%2BD3MXotFWqtbw%3D
    • Kim P, Yoon S, Seo M, Oh DK, Choi JH (2001b) Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase. Biotechnol Appl Biochem 34:99–102
    • (2001) Biotechnol Appl Biochem , vol.34 , pp. 99-102
    • Kim, P.1    Yoon, S.2    Seo, M.3    Oh, D.K.4    Choi, J.H.5
  • 33
    • 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
    • PID: 12076797, COI: 1:CAS:528:DC%2BD38XksF2jsrY%3D
    • 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(1):121–126
    • (2002) FEMS Microbiol Lett , vol.212 , Issue.1 , 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
  • 34
    • 0037742418 scopus 로고    scopus 로고
    • Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp. IM6501
    • PID: 12889832, COI: 1:CAS:528:DC%2BD3sXktlagurY%3D
    • Kim JW, Kim YW, Roh HJ, Kim HY, Cha JH, Park KH, Park CS (2003a) Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp. IM6501. Biotechnol Lett 25(12):963–967
    • (2003) Biotechnol Lett , vol.25 , Issue.12 , 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
  • 35
    • 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
    • PID: 12675579, COI: 1:CAS:528:DC%2BD38XpvVantr8%3D
    • Kim HJ, Ryu SA, Kim P, Oh DK (2003b) A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol Prog 19(2):400–404
    • (2003) Biotechnol Prog , vol.19 , Issue.2 , pp. 400-404
    • Kim, H.J.1    Ryu, S.A.2    Kim, P.3    Oh, D.K.4
  • 36
    • 33745454160 scopus 로고    scopus 로고
    • Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose
    • PID: 16834609, COI: 1:CAS:528:DC%2BD28XotFKgtb4%3D
    • Kim HJ, Kim JH, Oh HJ, Oh DK (2006) Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose. J Appl Microbiol 101(1):213–221
    • (2006) J Appl Microbiol , vol.101 , Issue.1 , pp. 213-221
    • Kim, H.J.1    Kim, J.H.2    Oh, H.J.3    Oh, D.K.4
  • 37
    • 84925538959 scopus 로고    scopus 로고
    • Recombinant GRAS strains expressing thermophilic arabinose isomerase as an active form and method of preparing food grade tagatose by using the same
    • B2
    • Kim SB, Lee YM, Park SW, Kim JH, Song SH, Lee KP (2009) Recombinant GRAS strains expressing thermophilic arabinose isomerase as an active form and method of preparing food grade tagatose by using the same. US Patent 8:137–946, B2
    • (2009) US Patent , vol.8 , pp. 137-946
    • Kim, S.B.1    Lee, Y.M.2    Park, S.W.3    Kim, J.H.4    Song, S.H.5    Lee, K.P.6
  • 39
    • 84920251559 scopus 로고    scopus 로고
    • Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase
    • Kim BJ, Hong SH, Shin KC, Jo YS, Oh DK (2014a) Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase. Appl Microbiol Biotechnol 1–11
    • (2014) Appl Microbiol Biotechnol , pp. 1-11
    • Kim, B.J.1    Hong, S.H.2    Shin, K.C.3    Jo, Y.S.4    Oh, D.K.5
  • 40
    • 84894422899 scopus 로고    scopus 로고
    • L-Ribose production from L-arabinose by immobilized recombinant Escherichia coli co-expressing the L-arabinose isomerase and mannose-6-phosphate isomerase genes from Geobacillus thermodenitrificans
    • PID: 24078190, COI: 1:CAS:528:DC%2BC3sXhsFCjtLzP
    • Kim KR, Seo ES, Oh DK (2014b) L-Ribose production from L-arabinose by immobilized recombinant Escherichia coli co-expressing the L-arabinose isomerase and mannose-6-phosphate isomerase genes from Geobacillus thermodenitrificans. Appl Biochem Biotechnol 172(1):275–288
    • (2014) Appl Biochem Biotechnol , vol.172 , Issue.1 , pp. 275-288
    • Kim, K.R.1    Seo, E.S.2    Oh, D.K.3
  • 41
    • 0023021760 scopus 로고
    • The organization of the araBAD operon of Escherichia coli
    • PID: 3549454, COI: 1:CAS:528:DyaL2sXktFymu70%3D
    • Lee N, Gielow W, Martin R, Hamilton E, Fowler A (1986) The organization of the araBAD operon of Escherichia coli. Gene 47(2):231–244
    • (1986) Gene , vol.47 , Issue.2 , pp. 231-244
    • Lee, N.1    Gielow, W.2    Martin, R.3    Hamilton, E.4    Fowler, A.5
  • 42
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyper thermophilic eubacterium Thermotoga maritima
    • PID: 15006759, COI: 1:CAS:528:DC%2BD2cXisVKjuro%3D
    • Lee DW, Jang HJ, Choe EA, Kim BC, Lee SJ, Kim SB, Hong YH, Pyun YR (2004) Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyper thermophilic 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    Kim, B.C.4    Lee, S.J.5    Kim, S.B.6    Hong, Y.H.7    Pyun, Y.R.8
  • 43
    • 11444258321 scopus 로고    scopus 로고
    • Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
    • PID: 15639234, COI: 1:CAS:528:DC%2BD2MXhvFyktw%3D%3D
    • Lee DW, Choe EA, Kim SB, Eom SH, Hong YH, Lee SJ, Lee HS, Lee DY, Ryun YR (2005a) Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus. Arch Biochem Biophys 434(2):333–343
    • (2005) Arch Biochem Biophys , vol.434 , Issue.2 , 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    Ryun, Y.R.9
  • 44
    • 29144453887 scopus 로고    scopus 로고
    • Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum
    • PID: 16332764, COI: 1:CAS:528:DC%2BD2MXhtlehtLjO
    • Lee SJ, Lee DW, Choe EA, Hong YH, Kim SB, Kim BC, Pyun YR (2005b) Characterization of a thermoacidophilic L-arabinose 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
  • 45
    • 80052362567 scopus 로고    scopus 로고
    • Isomaltulose production via yeast surface display of sucrose isomerase from Enterobacter sp. FMB-1 on Saccharomyces cerevisiae
    • PID: 21803574, COI: 1:CAS:528:DC%2BC3MXhtV2qtLvM
    • Lee GY, Jung JH, Seo DH, Hansin J, Ha SJ, Cha J, Kim YS, Park CS (2011) Isomaltulose production via yeast surface display of sucrose isomerase from Enterobacter sp. FMB-1 on Saccharomyces cerevisiae. Bioresour Technol 102(19):9179–9184
    • (2011) Bioresour Technol , vol.102 , Issue.19 , pp. 9179-9184
    • Lee, G.Y.1    Jung, J.H.2    Seo, D.H.3    Hansin, J.4    Ha, S.J.5    Cha, J.6    Kim, Y.S.7    Park, C.S.8
  • 46
    • 84870979267 scopus 로고    scopus 로고
    • Homologous alkalophilic and acidophilic L-arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability
    • PID: 23001647, COI: 1:CAS:528:DC%2BC38XhslyjsrrP
    • Lee SJ, Lee SJ, Lee YJ, Kim SB, Kim SK, Lee DW (2012) Homologous alkalophilic and acidophilic L-arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability. Appl Environ Microbiol 78(24):8813–8816
    • (2012) Appl Environ Microbiol , vol.78 , Issue.24 , pp. 8813-8816
    • Lee, S.J.1    Lee, S.J.2    Lee, Y.J.3    Kim, S.B.4    Kim, S.K.5    Lee, D.W.6
  • 47
    • 0036011228 scopus 로고    scopus 로고
    • Tagatose, the new GRAS sweetener and health product
    • PID: 12511110, COI: 1:CAS:528:DC%2BD38XktlSjt7o%3D
    • Levin GV (2002) Tagatose, the new GRAS sweetener and health product. J Med Food 5(1):23–36
    • (2002) J Med Food , vol.5 , Issue.1 , pp. 23-36
    • Levin, G.V.1
  • 48
    • 79955525190 scopus 로고    scopus 로고
    • Identification and characterization of a novel L-arabinose isomerase from Anoxybacillus flavithermus useful in D-tagatose production
    • PID: 21516359
    • Li Y, Zhu Y, Liu A, Sun Y (2011) Identification and characterization of a novel L-arabinose isomerase from Anoxybacillus flavithermus useful in D-tagatose production. Extremophiles 15:441–450
    • (2011) Extremophiles , vol.15 , pp. 441-450
    • Li, Y.1    Zhu, Y.2    Liu, A.3    Sun, Y.4
  • 49
    • 84869136375 scopus 로고    scopus 로고
    • Probing the essential catalytic residues and substrate affinity in thermophilic L-arabinose isomerase by homology modeling and site-directed mutagenesis
    • COI: 1:CAS:528:DC%2BC38Xhsl2iurrL
    • Li G, Xu Z, Li S, Xu H (2012) Probing the essential catalytic residues and substrate affinity in thermophilic L-arabinose isomerase by homology modeling and site-directed mutagenesis. Chin J Catal 33:1717–1723
    • (2012) Chin J Catal , vol.33 , pp. 1717-1723
    • Li, G.1    Xu, Z.2    Li, S.3    Xu, H.4
  • 50
    • 84857916775 scopus 로고    scopus 로고
    • Bioconversion of D-galactose to D-tagatose: continuous packed bed reaction with an immobilized thermostable L-arabinose isomerase and efficient purification by selective microbial degradation
    • PID: 22038246, COI: 1:CAS:528:DC%2BC38XitVGnsrc%3D
    • Liang M, Chen M, Liu X, Zhai Y, Liu X, Zhang H, Xiao M, Wang P (2012) Bioconversion of D-galactose to D-tagatose: continuous packed bed reaction with an immobilized thermostable L-arabinose isomerase and efficient purification by selective microbial degradation. Appl Microbiol Biotechnol 93(4):1469–1474
    • (2012) Appl Microbiol Biotechnol , vol.93 , Issue.4 , pp. 1469-1474
    • Liang, M.1    Chen, M.2    Liu, X.3    Zhai, Y.4    Liu, X.5    Zhang, H.6    Xiao, M.7    Wang, P.8
  • 51
    • 34547920744 scopus 로고    scopus 로고
    • High production of D-tagatose by the addition of boric acid
    • PID: 17583351, COI: 1:CAS:528:DC%2BD2sXms1eqtbo%3D
    • Lim BC, Kim HJ, Oh DK (2007) High production of D-tagatose by the addition of boric acid. Biotechnol Prog 23:824–828
    • (2007) Biotechnol Prog , vol.23 , pp. 824-828
    • Lim, B.C.1    Kim, H.J.2    Oh, D.K.3
  • 52
    • 50649091654 scopus 로고    scopus 로고
    • Tagatose production with pH control in a stirred tank reactor containing immobilized L-arabinose isomerase from Thermotoga neapolitana
    • PID: 18500585, COI: 1:CAS:528:DC%2BD1cXnsVGltrg%3D
    • Lim BC, Kim HJ, Oh DK (2008) Tagatose production with pH control in a stirred tank reactor containing immobilized L-arabinose isomerase from Thermotoga neapolitana. Appl Biochem Biotechnol 149(3):245–253
    • (2008) Appl Biochem Biotechnol , vol.149 , Issue.3 , pp. 245-253
    • Lim, B.C.1    Kim, H.J.2    Oh, D.K.3
  • 53
    • 84864105970 scopus 로고    scopus 로고
    • Production of L-ribose from L-ribulose by a triple-site variant of mannose-6-phosphate isomerase from Geobacillus thermodenitrificans
    • PID: 22447612, COI: 1:CAS:528:DC%2BC38XnsVSqu7g%3D
    • Lim YR, Yeom SJ, Oh DK (2012) Production of L-ribose from L-ribulose by a triple-site variant of mannose-6-phosphate isomerase from Geobacillus thermodenitrificans. Appl Environ Microbiol 78(11):3880–3884
    • (2012) Appl Environ Microbiol , vol.78 , Issue.11 , pp. 3880-3884
    • Lim, Y.R.1    Yeom, S.J.2    Oh, D.K.3
  • 55
    • 33745287171 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production
    • PID: 16756997, COI: 1:CAS:528:DC%2BD28Xmt1yrs7Y%3D
    • 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
  • 56
    • 84891624116 scopus 로고    scopus 로고
    • Enzymatic conversion of D-galactose to D-tagatose: cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5
    • PID: 23948501, COI: 1:CAS:528:DC%2BC3sXht1Kgt7zF
    • Men Y, Zhu Y, Zhang L, Kang Z, Izumori K, Sun Y, Ma Y (2014) Enzymatic conversion of D-galactose to D-tagatose: cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5. Microbiol Res 169(2):171–178
    • (2014) Microbiol Res , vol.169 , Issue.2 , pp. 171-178
    • Men, Y.1    Zhu, Y.2    Zhang, L.3    Kang, Z.4    Izumori, K.5    Sun, Y.6    Ma, Y.7
  • 57
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: properties, applications, and biotechnological processes
    • PID: 17492284, COI: 1:CAS:528:DC%2BD2sXosVSksrk%3D
    • 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
  • 58
    • 32944473444 scopus 로고    scopus 로고
    • Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans
    • PID: 16489490, COI: 1:CAS:528:DC%2BD28XhsFCrsrY%3D
    • Oh HJ, Kim HJ, Oh DK (2006a) Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans. Biotechnol Lett 28(3):145–149
    • (2006) Biotechnol Lett , vol.28 , Issue.3 , pp. 145-149
    • Oh, H.J.1    Kim, H.J.2    Oh, D.K.3
  • 59
    • 33750616739 scopus 로고    scopus 로고
    • Modification of optimal pH in L-arabinose isomerase from Geobacillus stearothermophilus for D-galactose isomerization
    • COI: 1:CAS:528:DC%2BD28Xht1Sgsb7K
    • Oh DK, Oh HJ, Kim HJ, Cheon J, Kim P (2006b) Modification of optimal pH in L-arabinose isomerase from Geobacillus stearothermophilus for D-galactose isomerization. J Mol Catal B Enzym 43:108–112
    • (2006) J Mol Catal B Enzym , vol.43 , pp. 108-112
    • Oh, D.K.1    Oh, H.J.2    Kim, H.J.3    Cheon, J.4    Kim, P.5
  • 60
    • 59349098795 scopus 로고    scopus 로고
    • Synthesis and pharmaceutical application of L-ribose
    • COI: 1:CAS:528:DC%2BD1MXhs1Oiur8%3D
    • Okano K (2009) Synthesis and pharmaceutical application of L-ribose. Tetrahedron 65(10):1937–1949
    • (2009) Tetrahedron , vol.65 , Issue.10 , pp. 1937-1949
    • Okano, K.1
  • 61
    • 55649100728 scopus 로고    scopus 로고
    • Cloning and characterization of a novel L-arabinose isomerase from Bacillus licheniformis
    • PID: 18716768, COI: 1:CAS:528:DC%2BD1cXhtlaqsbnN
    • Prabhu P, Tiwari MK, Jeya M, Gunasekaran P, Kim IW, Lee JK (2008) Cloning and characterization of a novel L-arabinose isomerase from Bacillus licheniformis. Appl Microbiol Biotechnol 81(2):283–290
    • (2008) Appl Microbiol Biotechnol , vol.81 , Issue.2 , pp. 283-290
    • Prabhu, P.1    Tiwari, M.K.2    Jeya, M.3    Gunasekaran, P.4    Kim, I.W.5    Lee, J.K.6
  • 62
    • 77649217237 scopus 로고    scopus 로고
    • Probing the molecular determinant for the catalytic efficiency of L-arabinose isomerase from Bacillus licheniformis
    • PID: 20048061, COI: 1:CAS:528:DC%2BC3cXjsFams7s%3D
    • Prabhu P, Jeya M, Lee JK (2010) Probing the molecular determinant for the catalytic efficiency of L-arabinose isomerase from Bacillus licheniformis. Appl Environ Microbiol 76(5):1653–1660
    • (2010) Appl Environ Microbiol , vol.76 , Issue.5 , pp. 1653-1660
    • Prabhu, P.1    Jeya, M.2    Lee, J.K.3
  • 63
    • 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
    • PID: 16386851, COI: 1:CAS:528:DC%2BD28XitVarsLw%3D
    • 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
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 64
    • 34247644456 scopus 로고    scopus 로고
    • Probing the essential catalytic residues and substrate affinity in the thermoactive Bacillus stearothermophilus US100 L-arabinose isomerase by site-directed mutagenesis
    • PID: 17337581, COI: 1:CAS:528:DC%2BD2sXltVaqsrc%3D
    • Rhimi M, Juy M, Aghajari N, Haser R, Bejar S (2007) Probing the essential catalytic residues and substrate affinity in the thermoactive Bacillus stearothermophilus US100 L-arabinose isomerase by site-directed mutagenesis. J Bacteriol 189(9):3556–3563
    • (2007) J Bacteriol , vol.189 , Issue.9 , pp. 3556-3563
    • Rhimi, M.1    Juy, M.2    Aghajari, N.3    Haser, R.4    Bejar, S.5
  • 65
    • 64449084435 scopus 로고    scopus 로고
    • Rational design of Bacillus stearothermophilus US100 L-arabinose isomerase: potential applications for D-tagatose production
    • PID: 19278622, COI: 1:CAS:528:DC%2BD1MXksVCntLc%3D
    • Rhimi M, Aghajari N, Juy M, Chouayekh H, Maguin E, Haser R, Bejar S (2009) Rational design of Bacillus stearothermophilus US100 L-arabinose isomerase: potential applications for D-tagatose production. Biochimie 91(5):650–653
    • (2009) Biochimie , vol.91 , Issue.5 , pp. 650-653
    • Rhimi, M.1    Aghajari, N.2    Juy, M.3    Chouayekh, H.4    Maguin, E.5    Haser, R.6    Bejar, S.7
  • 66
    • 77955665578 scopus 로고    scopus 로고
    • The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer
    • PID: 20688514, COI: 1:CAS:528:DC%2BC3cXhtVert77I
    • Rhimi M, lhammami R, Bajic G, Boudebbouze S, Maguin E, Haser R, Aghajari N (2010) The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer. Bioresour Technol 101:9171–9177
    • (2010) Bioresour Technol , vol.101 , pp. 9171-9177
    • Rhimi, M.1    Lhammami, R.2    Bajic, G.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Aghajari, N.7
  • 67
    • 80755143049 scopus 로고    scopus 로고
    • The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures
    • PID: 22074172, COI: 1:CAS:528:DC%2BC38XhtFOqsLk%3D
    • Rhimi M, Bajic G, Ilhammami R, Boudebbouze S, Maguin E, Haser R, Aghajari N (2011a) The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp. ANA-3 is highly active at low temperatures. Microb Cell Fact 10:96
    • (2011) Microb Cell Fact , vol.10 , pp. 96
    • Rhimi, M.1    Bajic, G.2    Ilhammami, R.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Aghajari, N.7
  • 68
    • 78650802091 scopus 로고    scopus 로고
    • Production of D-tagatose, a low caloric sweetener during milk fermentation using L-arabinose isomerase
    • PID: 21111612, COI: 1:CAS:528:DC%2BC3MXks1ClsQ%3D%3D
    • Rhimi M, Chouayekh H, Gouillouard I, Maguin E, Bejar S (2011b) Production of D-tagatose, a low caloric sweetener during milk fermentation using L-arabinose isomerase. Bioresour Technol 102:3309–3315
    • (2011) Bioresour Technol , vol.102 , pp. 3309-3315
    • Rhimi, M.1    Chouayekh, H.2    Gouillouard, I.3    Maguin, E.4    Bejar, S.5
  • 69
    • 4444333616 scopus 로고    scopus 로고
    • Bioconversion of D-galactitol to tagatose and dehydrogenase activity induction in Gluconobacter oxydans
    • COI: 1:CAS:528:DC%2BD2cXntlGmtL4%3D
    • Rollini M, Manzoni M (2005) Bioconversion of D-galactitol to tagatose and dehydrogenase activity induction in Gluconobacter oxydans. Process Biochem 40(1):437–444
    • (2005) Process Biochem , vol.40 , Issue.1 , pp. 437-444
    • Rollini, M.1    Manzoni, M.2
  • 70
    • 0346783288 scopus 로고    scopus 로고
    • Continuous D-tagatose production by immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor
    • PID: 14656135, COI: 1:CAS:528:DC%2BD3sXltF2rsLY%3D
    • Ryu SA, Kim CS, Kim HJ, Baek DH, Oh DK (2003) Continuous D-tagatose production by immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol Prog 19:1643–1647
    • (2003) Biotechnol Prog , vol.19 , pp. 1643-1647
    • Ryu, S.A.1    Kim, C.S.2    Kim, H.J.3    Baek, D.H.4    Oh, D.K.5
  • 71
    • 84866740969 scopus 로고    scopus 로고
    • Bifidobacterium longum L-arabinose isomerase—overexpression in Lactococcus lactis, purification, and characterization
    • PID: 22763951, COI: 1:CAS:528:DC%2BC38XhsVWntr7O
    • Salonen N, Nyyssölä A, Salonen K, Turunen O (2012) Bifidobacterium longum L-arabinose isomerase—overexpression in Lactococcus lactis, purification, and characterization. Appl Biochem Biotechnol 168(2):392–405
    • (2012) Appl Biochem Biotechnol , vol.168 , Issue.2 , pp. 392-405
    • Salonen, N.1    Nyyssölä, A.2    Salonen, K.3    Turunen, O.4
  • 72
    • 84880136941 scopus 로고    scopus 로고
    • D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase
    • Salonen N, Salonen K, Leisola M, Nyyssölä A (2013) D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase. Bioproc Biosyst Eng 1–9
    • (2013) Bioproc Biosyst Eng , pp. 1-9
    • Salonen, N.1    Salonen, K.2    Leisola, M.3    Nyyssölä, A.4
  • 73
    • 46549087961 scopus 로고    scopus 로고
    • A new and efficient phosphate starvation inducible expression system for Lactococcus lactis
    • PID: 18431568
    • Sirén N, Salonen K, Leisola M, Nyyssola A (2008) A new and efficient phosphate starvation inducible expression system for Lactococcus lactis. Appl Microbiol Biotechnol 79(5):803–810
    • (2008) Appl Microbiol Biotechnol , vol.79 , Issue.5 , pp. 803-810
    • Sirén, N.1    Salonen, K.2    Leisola, M.3    Nyyssola, A.4
  • 74
    • 84894473593 scopus 로고    scopus 로고
    • L-Arabinose isomerase and D-xylose isomerase from Lactobacillus reuteri: characterization, coexpression in the food grade host Lactobacillus plantarum, and application in the conversion of D-galactose and D-glucose
    • PID: 24443973, COI: 1:CAS:528:DC%2BC2cXpt12rsg%3D%3D
    • Staudigl P, Haltrich D, Peterbauer CK (2014) L-Arabinose isomerase and D-xylose isomerase from Lactobacillus reuteri: characterization, coexpression in the food grade host Lactobacillus plantarum, and application in the conversion of D-galactose and D-glucose. J Agric Food Chem 62(7):1617–1624
    • (2014) J Agric Food Chem , vol.62 , Issue.7 , pp. 1617-1624
    • Staudigl, P.1    Haltrich, D.2    Peterbauer, C.K.3
  • 75
    • 0017815877 scopus 로고
    • The shape of L-arabinose isomerase from Escherichia coli
    • PID: 348696, COI: 1:CAS:528:DyaE1cXktlyksb4%3D
    • Wallace LJ, Eiserling FA, Wilcox G (1978) The shape of L-arabinose isomerase from Escherichia coli. J Biol Chem 253(10):3717–3720
    • (1978) J Biol Chem , vol.253 , Issue.10 , pp. 3717-3720
    • Wallace, L.J.1    Eiserling, F.A.2    Wilcox, G.3
  • 76
    • 84865272522 scopus 로고    scopus 로고
    • A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c
    • PID: 22917022, COI: 1:CAS:528:DC%2BC3sXhsFyitrk%3D
    • Wanarska M, Kur J (2012) A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c. Microb Cell Fact 11(1):113
    • (2012) Microb Cell Fact , vol.11 , Issue.1 , pp. 113
    • Wanarska, M.1    Kur, J.2
  • 77
    • 79952814999 scopus 로고    scopus 로고
    • A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: gene cloning, purification and characterization
    • COI: 1:CAS:528:DC%2BC3MXjsV2itb8%3D
    • Xu Z, Qing YJ, Li S, Feng XH, Xu H, Ouyang PK (2011) A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: gene cloning, purification and characterization. J Mol Catal B Enzym 70:1–7
    • (2011) J Mol Catal B Enzym , vol.70 , pp. 1-7
    • Xu, Z.1    Qing, Y.J.2    Li, S.3    Feng, X.H.4    Xu, H.5    Ouyang, P.K.6
  • 78
    • 84858749628 scopus 로고    scopus 로고
    • Production of D-tagatose, a functional sweetener, utilizing alginate immobilized Lactobacillus fermentum CGMCC2921 cells
    • PID: 22203394, COI: 1:CAS:528:DC%2BC38XhvVWktL0%3D
    • Xu Z, Li S, Fu FG, Li GX, Feng X, Xu H, Ouyang PK (2012) Production of D-tagatose, a functional sweetener, utilizing alginate immobilized Lactobacillus fermentum CGMCC2921 cells. Appl Biochem Biotechnol 166:961–973
    • (2012) Appl Biochem Biotechnol , vol.166 , pp. 961-973
    • Xu, Z.1    Li, S.2    Fu, F.G.3    Li, G.X.4    Feng, X.5    Xu, H.6    Ouyang, P.K.7
  • 79
    • 84899980900 scopus 로고    scopus 로고
    • Function of aspartic acid residues in optimum pH control of L-arabinose isomerase from Lactobacillus fermentum
    • Xu Z, Li S, Feng X, Zhan Y, Xu H (2014) Function of aspartic acid residues in optimum pH control of L-arabinose isomerase from Lactobacillus fermentum. Appl Microbiol Biotechnol 1–10
    • (2014) Appl Microbiol Biotechnol , pp. 1-10
    • Xu, Z.1    Li, S.2    Feng, X.3    Zhan, Y.4    Xu, H.5
  • 80
    • 67650488869 scopus 로고    scopus 로고
    • Substrate specificity of a mannose-6-phosphate isomerase from Bacillus subtilis and its application in the production of L-ribose
    • PID: 19447949, COI: 1:CAS:528:DC%2BD1MXptV2gs7w%3D
    • Yeom SJ, Ji JH, Kim NH, Park CS, Oh DK (2009a) Substrate specificity of a mannose-6-phosphate isomerase from Bacillus subtilis and its application in the production of L-ribose. Appl Environ Microbiol 75(14):4705–4710
    • (2009) Appl Environ Microbiol , vol.75 , Issue.14 , pp. 4705-4710
    • Yeom, S.J.1    Ji, J.H.2    Kim, N.H.3    Park, C.S.4    Oh, D.K.5
  • 81
    • 70350515953 scopus 로고    scopus 로고
    • L-Ribose production from L-arabinose by using purified L-arabinose isomerase and mannose-6-phosphate isomerase from Geobacillus thermodenitrificans
    • PID: 19749063, COI: 1:CAS:528:DC%2BD1MXhsVGrs7%2FL
    • Yeom SJ, Kim NH, Park CS, Oh DK (2009b) L-Ribose production from L-arabinose by using purified L-arabinose isomerase and mannose-6-phosphate isomerase from Geobacillus thermodenitrificans. Appl Environ Microbiol 75(21):6941–6943
    • (2009) Appl Environ Microbiol , vol.75 , Issue.21 , pp. 6941-6943
    • Yeom, S.J.1    Kim, N.H.2    Park, C.S.3    Oh, D.K.4
  • 82
    • 79551472833 scopus 로고    scopus 로고
    • Characterization of a mannose-6-phosphate isomerase from Thermus thermophilus and increased L-ribose production by its R142N mutant
    • PID: 21115698, COI: 1:CAS:528:DC%2BC3MXisVOrtLs%3D
    • Yeom SJ, Seo ES, Kim BN, Kim YS, Oh DK (2011) Characterization of a mannose-6-phosphate isomerase from Thermus thermophilus and increased L-ribose production by its R142N mutant. Appl Environ Microbiol 77(3):762–767
    • (2011) Appl Environ Microbiol , vol.77 , Issue.3 , pp. 762-767
    • Yeom, S.J.1    Seo, E.S.2    Kim, B.N.3    Kim, Y.S.4    Oh, D.K.5
  • 83
    • 0037299866 scopus 로고    scopus 로고
    • Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production
    • COI: 1:CAS:528:DC%2BD3sXhsFKkurY%3D
    • Yoon SH, Kim P, Oh DK (2003) Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production. World J Microbiol Biotechnol 19(1):47–51
    • (2003) World J Microbiol Biotechnol , vol.19 , Issue.1 , pp. 47-51
    • Yoon, S.H.1    Kim, P.2    Oh, D.K.3
  • 84
    • 0003419057 scopus 로고
    • D-tagatose as a low-calorie carbohydrate sweetener and bulking agent
    • Zehner LR (1988) D-tagatose as a low-calorie carbohydrate sweetener and bulking agent. US Patent 4:786,722
    • (1988) US Patent , vol.4 , pp. 786,722
    • Zehner, L.R.1
  • 85
    • 84896511457 scopus 로고    scopus 로고
    • Coexpression of β-D-galactosidase and L-arabinose isomerase in the production of D-tagatose: a functional sweetener
    • PID: 24568679, COI: 1:CAS:528:DC%2BC2cXjt1yls7c%3D
    • Zhan Y, Xu Z, Li S, Liu X, Xu L, Feng X, Xu H (2014) Coexpression of β-D-galactosidase and L-arabinose isomerase in the production of D-tagatose: a functional sweetener. J Agric Food Chem 62(11):2412–2417
    • (2014) J Agric Food Chem , vol.62 , Issue.11 , pp. 2412-2417
    • Zhan, Y.1    Xu, Z.2    Li, S.3    Liu, X.4    Xu, L.5    Feng, X.6    Xu, H.7
  • 86
    • 77955519658 scopus 로고    scopus 로고
    • Alginate immobilization of recombinant Escherichia coli whole cells harboring L-arabinose isomerase for L-ribulose production
    • COI: 1:CAS:528:DC%2BC3cXos1yrtrY%3D
    • Zhang YW, Prabhu P, Lee JK (2010a) Alginate immobilization of recombinant Escherichia coli whole cells harboring L-arabinose isomerase for L-ribulose production. Bioproc Biosyst Eng 33(6):741–748
    • (2010) Bioproc Biosyst Eng , vol.33 , Issue.6 , pp. 741-748
    • Zhang, Y.W.1    Prabhu, P.2    Lee, J.K.3
  • 87
    • 77955528014 scopus 로고    scopus 로고
    • L-Ribulose production by an Escherichia coli harboring L-arabinose isomerase from Bacillus licheniformis
    • PID: 20495916, COI: 1:CAS:528:DC%2BC3cXptlWqsb4%3D
    • Zhang YW, Jeya M, Lee JK (2010b) L-Ribulose production by an Escherichia coli harboring L-arabinose isomerase from Bacillus licheniformis. Appl Microbiol Biotechnol 87(6):1993–1999
    • (2010) Appl Microbiol Biotechnol , vol.87 , Issue.6 , pp. 1993-1999
    • Zhang, Y.W.1    Jeya, M.2    Lee, J.K.3
  • 88
    • 79952574164 scopus 로고    scopus 로고
    • Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass
    • PID: 21038097, COI: 1:CAS:528:DC%2BC3MXhslWltrw%3D
    • Zhang YW, Jeya M, Lee JK (2011) Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass. Appl Microbiol Biotechnol 89(5):1435–1442
    • (2011) Appl Microbiol Biotechnol , vol.89 , Issue.5 , pp. 1435-1442
    • Zhang, Y.W.1    Jeya, M.2    Lee, J.K.3
  • 89
    • 84862810508 scopus 로고    scopus 로고
    • Heterologous expression and characterization of Bacillus coagulans L-arabinose isomerase
    • PID: 22806043, COI: 1:CAS:528:DC%2BC38XmtFWgtbc%3D
    • Zhou X, Wu JC (2012) Heterologous expression and characterization of Bacillus coagulans L-arabinose isomerase. World J Microbiol Biotechnol 28(5):2205–2212
    • (2012) World J Microbiol Biotechnol , vol.28 , Issue.5 , pp. 2205-2212
    • Zhou, X.1    Wu, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.