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Volumn 62, Issue 7, 2014, Pages 1617-1624

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

Author keywords

d fructose; d tagatose; d xylose (glucose) isomerase; food grade; l arabinose isomerase; Lactobacillus

Indexed keywords

AFFINITY CHROMATOGRAPHY; BACILLI; CLONING; ENCODING (SYMBOLS); ENZYMES; ESCHERICHIA COLI; FRUCTOSE; GENE EXPRESSION; GENES; GLUCOSE; METAL IONS; PURIFICATION;

EID: 84894473593     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf404785m     Document Type: Article
Times cited : (48)

References (50)
  • 1
    • 79952814999 scopus 로고    scopus 로고
    • A novel l -arabinose isomerase from Lactobacillus fermentum CGMCC2921 for d -tagatose production: Gene cloning, purification and characterization
    • Xu, Z.; Qing, Y.; Li, S.; Feng, X.; Xu, H.; Ouyang, P. A novel l -arabinose isomerase from Lactobacillus fermentum CGMCC2921 for d -tagatose production: gene cloning, purification and characterization J. Mol. Catal. B: Enzymatic 2011, 70 (1-2) 1-7
    • (2011) J. Mol. Catal. B: Enzymatic , vol.70 , Issue.12 , pp. 1-7
    • Xu, Z.1    Qing, Y.2    Li, S.3    Feng, X.4    Xu, H.5    Ouyang, P.6
  • 2
    • 33947632003 scopus 로고    scopus 로고
    • Co-expression of l -arabinose isomerase and d -glucose isomerase in E. Coli and development of an efficient process producing simultaneously d -tagatose and d -fructose
    • Rhimi, M.; Messaoud, E. B.; Borgi, M. A.; Khadra, K. B.; Bejar, S. Co-expression of l -arabinose isomerase and d -glucose isomerase in E. coli and development of an efficient process producing simultaneously d -tagatose and d -fructose Enzyme Microb. Technol. 2007, 40 (6) 1531-1537
    • (2007) Enzyme Microb. Technol. , vol.40 , Issue.6 , pp. 1531-1537
    • Rhimi, M.1    Messaoud, E.B.2    Borgi, M.A.3    Khadra, K.B.4    Bejar, S.5
  • 3
    • 84866740969 scopus 로고    scopus 로고
    • Bifidobacterium longum l -arabinose isomerase overexpression in Lactococcus lactis, purification, and characterization
    • Salonen, N.; Nyyssölä, A.; Salonen, K.; Turunen, O. Bifidobacterium longum l -arabinose isomerase overexpression in Lactococcus lactis, purification, and characterization Appl. Biochem. Biotechnol. 2012, 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
  • 4
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: Properties, applications, and biotechnological processes
    • Oh, D. K. Tagatose: properties, applications, and biotechnological processes Appl. Microbiol. Biotechnol. 2007, 76 (1) 1-8
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , Issue.1 , pp. 1-8
    • Oh, D.K.1
  • 5
    • 0034048991 scopus 로고    scopus 로고
    • Preparation of l -arabinose isomerase originated from Escherichia coli as a biocatalyst for d -tagatose production
    • Roh, H. J.; Yoon, S. H.; Kim, P. Preparation of l -arabinose isomerase originated from Escherichia coli as a biocatalyst for d -tagatose production Biotechnol. Lett. 2000, 22 (3) 197-199
    • (2000) Biotechnol. Lett. , vol.22 , Issue.3 , pp. 197-199
    • Roh, H.J.1    Yoon, S.H.2    Kim, P.3
  • 6
    • 0034775246 scopus 로고    scopus 로고
    • Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase
    • Kim, P.; Yoon, S. H.; Seo, M. J.; Oh, D. K.; Choi, J. H. Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase Biotechnol. Appl. Biochem. 2001, 34 (2) 99-102
    • (2001) Biotechnol. Appl. Biochem. , vol.34 , Issue.2 , pp. 99-102
    • Kim, P.1    Yoon, S.H.2    Seo, M.J.3    Oh, D.K.4    Choi, J.H.5
  • 8
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using l -arabinose isomerase: A review and future perspective
    • Kim, P. Current studies on biological tagatose production using l -arabinose isomerase: a review and future perspective Appl. Microbiol. Biotechnol. 2004, 65 (3) 243-249
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , Issue.3 , pp. 243-249
    • Kim, P.1
  • 9
    • 77955665578 scopus 로고    scopus 로고
    • The acid tolerant l -arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive d -tagatose producer
    • Rhimi, M.; Ilhammami, R.; Bajic, G.; Boudebbouze, S.; Maguin, E.; Haser, R.; Aghajari, N. The acid tolerant l -arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive d -tagatose producer Bioresour. Technol. 2010, 101 (23) 9171-9177
    • (2010) Bioresour. Technol. , vol.101 , Issue.23 , pp. 9171-9177
    • Rhimi, M.1    Ilhammami, R.2    Bajic, G.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Aghajari, N.7
  • 10
    • 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
    • Men, Y.; Zhu, Y.; Zhang, L.; Kang, Z.; Izumori, K.; Sun, Y.; Ma, Y. Enzymatic conversion of d -galactose to d -tagatose: cloning, overexpression and characterization of l -arabinose isomerase from Pediococcus pentosaceus PC-5 Microbiol. Res. 2014, 169, 171-178
    • (2014) Microbiol. Res. , vol.169 , pp. 171-178
    • Men, Y.1    Zhu, Y.2    Zhang, L.3    Kang, Z.4    Izumori, K.5    Sun, Y.6    Ma, Y.7
  • 11
    • 0029998291 scopus 로고    scopus 로고
    • Molecular and industrial aspects of glucose isomerase
    • Bhosale, S. H.; Rao, M. B.; Deshpande, V. V. Molecular and industrial aspects of glucose isomerase Microbiol. Rev. 1996, 60 (2) 280-300
    • (1996) Microbiol. Rev. , vol.60 , Issue.2 , pp. 280-300
    • Bhosale, S.H.1    Rao, M.B.2    Deshpande, V.V.3
  • 12
    • 0026548869 scopus 로고
    • One-step purification of Actinoplanes missouriensis d -sylose isomerase by high-performance immobilized copper-affinity chromatography: Functional analysis of surface histidine residues by site-directed mutagenesis
    • Mrabet, N. T.; Van Den Brande, I.; Van Den Broeck, A. One-step purification of Actinoplanes missouriensis d -sylose isomerase by high-performance immobilized copper-affinity chromatography: functional analysis of surface histidine residues by site-directed mutagenesis Biochemistry 1992, 31 (10) 2690-2702
    • (1992) Biochemistry , vol.31 , Issue.10 , pp. 2690-2702
    • Mrabet, N.T.1    Van Den Brande, I.2    Van Den Broeck, A.3
  • 14
    • 0042863130 scopus 로고    scopus 로고
    • Solubility and crystallization of xylose isomerase from Streptomyces rubiginosus
    • Vuolanto, A.; Uotila, S.; Leisola, M.; Visuri, K. Solubility and crystallization of xylose isomerase from Streptomyces rubiginosus J. Cryst. Growth 2003, 257 (3-4) 403-411
    • (2003) J. Cryst. Growth , vol.257 , Issue.34 , pp. 403-411
    • Vuolanto, A.1    Uotila, S.2    Leisola, M.3    Visuri, K.4
  • 15
    • 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
    • Jørgensen, F.; Hansen, O. C.; Stougaard, P. Enzymatic conversion of d -galactose to d -tagatose: heterologous expression and characterisation of a thermostable l -arabinose isomerase from Thermoanaerobacter mathranii Appl. Microbiol. Biotechnol. 2004, 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
  • 16
    • 80052633525 scopus 로고    scopus 로고
    • Food-grade gene expression in lactic acid bacteria
    • Peterbauer, C.; Maischberger, T.; Haltrich, D. Food-grade gene expression in lactic acid bacteria Biotechnol. J. 2011, 6 (9) 1147-1161
    • (2011) Biotechnol. J. , vol.6 , Issue.9 , pp. 1147-1161
    • Peterbauer, C.1    Maischberger, T.2    Haltrich, D.3
  • 17
    • 84864066205 scopus 로고    scopus 로고
    • Lactobacillus plantarum and Lactobacillus buchneri as expression systems: Evaluation of different origins of replication for the design of suitable shuttle vectors
    • Spath, K.; Heinl, S.; Egger, E.; Grabherr, R. Lactobacillus plantarum and Lactobacillus buchneri as expression systems: evaluation of different origins of replication for the design of suitable shuttle vectors Mol. Biotechnol. 2012, 52 (1) 40-48
    • (2012) Mol. Biotechnol. , vol.52 , Issue.1 , pp. 40-48
    • Spath, K.1    Heinl, S.2    Egger, E.3    Grabherr, R.4
  • 18
    • 77955335008 scopus 로고    scopus 로고
    • Importance of lactobacilli in food and feed biotechnology
    • Giraffa, G.; Chanishvili, N.; Widyastuti, Y. Importance of lactobacilli in food and feed biotechnology Res. Microbiol. 2010, 161 (6) 480-487
    • (2010) Res. Microbiol. , vol.161 , Issue.6 , pp. 480-487
    • Giraffa, G.1    Chanishvili, N.2    Widyastuti, Y.3
  • 19
  • 20
    • 84867743360 scopus 로고    scopus 로고
    • Direct cloning in Lactobacillus plantarum: Electroporation with non-methylated plasmid DNA enhances transformation efficiency and makes shuttle vectors obsolete
    • Spath, K.; Heinl, S.; Grabherr, R. Direct cloning in Lactobacillus plantarum: electroporation with non-methylated plasmid DNA enhances transformation efficiency and makes shuttle vectors obsolete. Microb. Cell Factories 2012, 11, 141.
    • (2012) Microb. Cell Factories , vol.11 , pp. 141
    • Spath, K.1    Heinl, S.2    Grabherr, R.3
  • 21
    • 84857433671 scopus 로고    scopus 로고
    • Homodimeric β-galactosidase from Lactobacillus delbrueckii subsp. Bulgaricus DSM 20081: Expression in Lactobacillus plantarum and biochemical characterization
    • Nguyen, T. T.; Nguyen, H. A.; Arreola, S. L.; Mlynek, G.; Djinović-Carugo, K.; Mathiesen, G.; Nguyen, T. H.; Haltrich, D. Homodimeric β-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus DSM 20081: expression in Lactobacillus plantarum and biochemical characterization J. Agric. Food Chem. 2012, 60 (7) 1713-1721
    • (2012) J. Agric. Food Chem. , vol.60 , Issue.7 , pp. 1713-1721
    • Nguyen, T.T.1    Nguyen, H.A.2    Arreola, S.L.3    Mlynek, G.4    Djinović-Carugo, K.5    Mathiesen, G.6    Nguyen, T.H.7    Haltrich, D.8
  • 22
    • 80755168874 scopus 로고    scopus 로고
    • Chitinase from Bacillus licheniformis DSM13: Expression in Lactobacillus plantarum WCFS1 and biochemical characterisation
    • Nguyen, H. A.; Nguyen, T. H.; Nguyen, T. T.; Peterbauer, C. K.; Mathiesen, G.; Haltrich, D. Chitinase from Bacillus licheniformis DSM13: expression in Lactobacillus plantarum WCFS1 and biochemical characterisation Protein Express. Purif. 2012, 81 (2) 166-174
    • (2012) Protein Express. Purif. , vol.81 , Issue.2 , pp. 166-174
    • Nguyen, H.A.1    Nguyen, T.H.2    Nguyen, T.T.3    Peterbauer, C.K.4    Mathiesen, G.5    Haltrich, D.6
  • 23
    • 3843123308 scopus 로고    scopus 로고
    • High-level gene expression in Lactobacillus plantarum using a pheromone-regulated bacteriocin promoter
    • Mathiesen, G.; Sørvig, E.; Blatny, J.; Naterstad, K.; Axelsson, L.; Eijsink, V. G. H. High-level gene expression in Lactobacillus plantarum using a pheromone-regulated bacteriocin promoter Lett. Appl. Microbiol. 2004, 39 (2) 137-143
    • (2004) Lett. Appl. Microbiol. , vol.39 , Issue.2 , pp. 137-143
    • Mathiesen, G.1    Sørvig, E.2    Blatny, J.3    Naterstad, K.4    Axelsson, L.5    Eijsink, V.G.H.6
  • 25
    • 22144493299 scopus 로고    scopus 로고
    • High-level, inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum using versatile expression vectors
    • Sørvig, E.; Mathiesen, G.; Naterstad, K.; Eijsink, V. G. H.; Axelsson, L. High-level, inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum using versatile expression vectors Microbiology 2005, 151 (7) 2439-2449
    • (2005) Microbiology , vol.151 , Issue.7 , pp. 2439-2449
    • Sørvig, E.1    Mathiesen, G.2    Naterstad, K.3    Eijsink, V.G.H.4    Axelsson, L.5
  • 26
    • 22144448613 scopus 로고    scopus 로고
    • Characterization of a new bacteriocin operon in sakacin P-producing Lactobacillus sakei, showing strong translational coupling between the bacteriocin and immunity genes
    • Mathiesen, G.; Huehne, K.; Kroeckel, L.; Axelsson, L.; Eijsink, V. G. H. Characterization of a new bacteriocin operon in sakacin P-producing Lactobacillus sakei, showing strong translational coupling between the bacteriocin and immunity genes Appl. Environ. Microbiol. 2005, 71 (7) 3565-3574
    • (2005) Appl. Environ. Microbiol. , vol.71 , Issue.7 , pp. 3565-3574
    • Mathiesen, G.1    Huehne, K.2    Kroeckel, L.3    Axelsson, L.4    Eijsink, V.G.H.5
  • 27
    • 33747666218 scopus 로고    scopus 로고
    • Overview of bacterial expression systems for heterologous protein production: From molecular and biochemical fundamentals to commercial systems
    • Terpe, K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems Appl. Microbiol. Biotechnol. 2006, 72 (2) 211-222
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , Issue.2 , pp. 211-222
    • Terpe, K.1
  • 28
    • 0034515202 scopus 로고    scopus 로고
    • Validation of the probiotic concept: Lactobacillus reuteri confers broad-spectrum protection against disease in humans and animals
    • Casas, I. A.; Dobrogosz, W. J. Validation of the probiotic concept: Lactobacillus reuteri confers broad-spectrum protection against disease in humans and animals Microb. Ecol. Health Dis. 2000, 12 (4) 247-285
    • (2000) Microb. Ecol. Health Dis. , vol.12 , Issue.4 , pp. 247-285
    • Casas, I.A.1    Dobrogosz, W.J.2
  • 29
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H.; Nojima, H.; Okayama, H. High efficiency transformation of Escherichia coli with plasmids Gene 1990, 96 (1) 23-28
    • (1990) Gene , vol.96 , Issue.1 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 30
    • 0030608942 scopus 로고    scopus 로고
    • Site-directed mutagenesis: A two-step method using PCR and DpnI
    • Li, S.; Wilkinson, M. F. Site-directed mutagenesis: a two-step method using PCR and DpnI BioTechniques 1997, 23 (4) 588-590
    • (1997) BioTechniques , vol.23 , Issue.4 , pp. 588-590
    • Li, S.1    Wilkinson, M.F.2
  • 31
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N.; Hunt, H. D.; Horton, R. M.; Pullen, J. K.; Pease, L. R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 1989, 77 (1) 51-59
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding Anal. Biochem. 1976, 72 (1-2) 248-254
    • (1976) Anal. Biochem. , vol.72 , Issue.12 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection and determination of keto sugars and trioses
    • Dische, Z.; Borenfreund, E. A new spectrophotometric method for the detection and determination of keto sugars and trioses J. Biol. Chem. 1951, 192 (2) 583-587
    • (1951) J. Biol. Chem. , vol.192 , Issue.2 , pp. 583-587
    • Dische, Z.1    Borenfreund, E.2
  • 37
    • 84875067543 scopus 로고    scopus 로고
    • Evaluation of the food grade expression systems NICE and pSIP for the production of 2,5-diketo- d -gluconic acid reductase from Corynebacterium glutamicum
    • Kaswurm, V.; Nguyen, T. T.; Maischberger, T.; Kulbe, K. D.; Michlmayr, H. Evaluation of the food grade expression systems NICE and pSIP for the production of 2,5-diketo- d -gluconic acid reductase from Corynebacterium glutamicum AMB Express 2013, 3 (1) 1-11
    • (2013) AMB Express , vol.3 , Issue.1 , pp. 1-11
    • Kaswurm, V.1    Nguyen, T.T.2    Maischberger, T.3    Kulbe, K.D.4    Michlmayr, H.5
  • 38
    • 0030571479 scopus 로고    scopus 로고
    • Structure and organisation of the pyrimidine biosynthesis pathway genes in Lactobacillus plantarum: A PCR strategy for sequencing without cloning
    • Elagöz, A.; Abdi, A.; Hubert, J. C.; Kammerer, B. Structure and organisation of the pyrimidine biosynthesis pathway genes in Lactobacillus plantarum: a PCR strategy for sequencing without cloning Gene 1996, 182 (1-2) 37-43
    • (1996) Gene , vol.182 , Issue.12 , pp. 37-43
    • Elagöz, A.1    Abdi, A.2    Hubert, J.C.3    Kammerer, B.4
  • 40
    • 78650802091 scopus 로고    scopus 로고
    • Production of d -tagatose, a low caloric sweetener during milk fermentation using l -arabinose isomerase
    • Rhimi, M.; Chouayekh, H.; Gouillouard, I.; Maguin, E.; Bejar, S. Production of d -tagatose, a low caloric sweetener during milk fermentation using l -arabinose isomerase Bioresour. Technol. 2011, 102 (3) 3309-3315
    • (2011) Bioresour. Technol. , vol.102 , Issue.3 , pp. 3309-3315
    • Rhimi, M.1    Chouayekh, H.2    Gouillouard, I.3    Maguin, E.4    Bejar, S.5
  • 41
    • 33745287171 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli l -arabinose isomerase (ECAI), the putative target of biological tagatose production
    • Manjasetty, B. A.; Chance, M. R. Crystal structure of Escherichia coli l -arabinose isomerase (ECAI), the putative target of biological tagatose production J. Mol. Biol. 2006, 360 (2) 297-309
    • (2006) J. Mol. Biol. , vol.360 , Issue.2 , pp. 297-309
    • Manjasetty, B.A.1    Chance, M.R.2
  • 42
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an l -arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • Chouayekh, H.; Bejar, W.; Rhimi, M.; Jelleli, K.; Mseddi, M.; Bejar, S. Characterization of an l -arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH FEMS Microbiol. Lett. 2007, 277 (2) 260-267
    • (2007) FEMS Microbiol. Lett. , 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
  • 43
    • 84855341461 scopus 로고    scopus 로고
    • D -Xylose isomerase from a marine bacterium, Vibrio sp. Strain XY-214, and d -xylulose production from β-1,3-xylan
    • Umemoto, Y.; Shibata, T.; Araki, T. d -Xylose isomerase from a marine bacterium, Vibrio sp. strain XY-214, and d -xylulose production from β-1,3-xylan Mari. Biotechnol. 2012, 14 (1) 10-20
    • (2012) Mari. Biotechnol. , vol.14 , Issue.1 , pp. 10-20
    • Umemoto, Y.1    Shibata, T.2    Araki, T.3
  • 44
    • 0029815134 scopus 로고    scopus 로고
    • Purification and cloning of a thermostable xylose (glucose) isomerase with an acidic pH optimum from Thermoanaerobacterium strain JW/SL-YS 489
    • Liu, S. Y.; Wiegel, J.; Gherardini, F. C. Purification and cloning of a thermostable xylose (glucose) isomerase with an acidic pH optimum from Thermoanaerobacterium strain JW/SL-YS 489 J. Bacteriol. 1996, 178 (20) 5938-5945
    • (1996) J. Bacteriol. , vol.178 , Issue.20 , pp. 5938-5945
    • Liu, S.Y.1    Wiegel, J.2    Gherardini, F.C.3
  • 45
    • 34248175752 scopus 로고    scopus 로고
    • Purification and characterization of l -arabinose isomerase from Lactobacillus plantarum producing d -tagatose
    • Zhang, H.; Jiang, B.; Pan, B. Purification and characterization of l -arabinose isomerase from Lactobacillus plantarum producing d -tagatose World J. Microbiol. Biotechnol. 2007, 23 (5) 641-646
    • (2007) World J. Microbiol. Biotechnol. , vol.23 , Issue.5 , pp. 641-646
    • Zhang, H.1    Jiang, B.2    Pan, B.3
  • 46
    • 79957459904 scopus 로고    scopus 로고
    • Purification and characterization of a novel thermostable xylose isomerase from Opuntia vulgaris Mill
    • Ravikumar, S.; Vikramathithan, J.; Srikumar, K. Purification and characterization of a novel thermostable xylose isomerase from Opuntia vulgaris Mill Appl. Biochem. Biotechnol. 2011, 164 (5) 593-603
    • (2011) Appl. Biochem. Biotechnol. , vol.164 , Issue.5 , pp. 593-603
    • Ravikumar, S.1    Vikramathithan, J.2    Srikumar, K.3
  • 47
    • 0014429277 scopus 로고
    • Purification, crystallization and properties of the d -xylose isomerase from Lactobacillus brevis
    • Yamanaka, K. Purification, crystallization and properties of the d -xylose isomerase from Lactobacillus brevis Biochim. Biophys. Acta-Enzymol. 1968, 151 (3) 670-680
    • (1968) Biochim. Biophys. Acta-Enzymol. , vol.151 , Issue.3 , pp. 670-680
    • Yamanaka, K.1
  • 48
    • 84255160731 scopus 로고    scopus 로고
    • Creation of metal-independent hyperthermophilic l -arabinose isomerase by homologous recombination
    • Hong, Y. H.; Lee, D. W.; Pyun, Y. R.; Lee, S. H. Creation of metal-independent hyperthermophilic l -arabinose isomerase by homologous recombination J. Agric. Food Chem. 2011, 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


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