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Volumn , Issue , 2008, Pages 177-190

Advances in enzyme immobilization through the use of recombinant DNA technology

Author keywords

Double tagged protein; Enzyme immobilization; Fusion protein; Recombinant DNA; Self cloning; Surface display; Whole cell biocatalyst

Indexed keywords


EID: 68949120258     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (50)
  • 1
    • 0035424201 scopus 로고    scopus 로고
    • Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis
    • Duetz, W.A., van Beilen J. B. and Witholt, B. (2001). Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis. Curr. Opin. Biotechnol, 12, 419-425.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 419-425
    • Duetz, W.A.1    van Beilen, J.B.2    Witholt, B.3
  • 2
    • 0034210138 scopus 로고    scopus 로고
    • Preparation of high-activity whole cell biocatalysts by permeabilization of recombinant yeasts with alcohol
    • Liu, Y., Fujita, Y., Kondo, A. and Fukuda, H. (2000). Preparation of high-activity whole cell biocatalysts by permeabilization of recombinant yeasts with alcohol. J. Biosci. Bioeng, 2000, 89, 554-558.
    • (2000) J. Biosci. Bioeng , vol.89 , pp. 554-558
    • Liu, Y.1    Fujita, Y.2    Kondo, A.3    Fukuda, H.4
  • 3
    • 4644315650 scopus 로고    scopus 로고
    • Accelerating whole-cell biocatalysis by reducing outer membrane permeability barrier
    • Ni, Y. and Chen, R. R. (2004). Accelerating whole-cell biocatalysis by reducing outer membrane permeability barrier. Biotechnol. Bioeng, 87, 804-811.
    • (2004) Biotechnol. Bioeng , vol.87 , pp. 804-811
    • Ni, Y.1    Chen, R.R.2
  • 4
    • 33847273107 scopus 로고    scopus 로고
    • Permeability issues in whole-cell bioprocesses and cellular membrane engineering
    • Chen, R. R. (2007). Permeability issues in whole-cell bioprocesses and cellular membrane engineering. Appl. Microbiol. Biotechnol, 74, 730-738.
    • (2007) Appl. Microbiol. Biotechnol , vol.74 , pp. 730-738
    • Chen, R.R.1
  • 5
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides using surface-expressed organophosphorus hydrolase
    • Richins, R. D., Kaneva, I., Mulchandani, A. and Chen, W. (1997). Biodegradation of organophosphorus pesticides using surface-expressed organophosphorus hydrolase. Nat. Biotechnol, 15, 984-987.
    • (1997) Nat. Biotechnol , vol.15 , pp. 984-987
    • Richins, R.D.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 6
    • 0037212403 scopus 로고    scopus 로고
    • Microbial cell-surface display
    • Lee, S. Y., Choi, J. H. and Xu, Z. (2003). Microbial cell-surface display. Trends Biotechnol, 21, 45-52.
    • (2003) Trends Biotechnol , vol.21 , pp. 45-52
    • Lee, S.Y.1    Choi, J.H.2    Xu, Z.3
  • 7
    • 33645031498 scopus 로고    scopus 로고
    • Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production
    • Wang, Z., Qi. Q. and Wang, P. G. (2006). Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production. Appl. Environ. Microbiol, 72, 1873-1877.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 1873-1877
    • Wang, Z.1    Qi, Q.2    Wang, P.G.3
  • 8
    • 0342710346 scopus 로고    scopus 로고
    • Bacterial surface display: trends and progress
    • Stahl, S., and Uhlen, M. (1997). Bacterial surface display: trends and progress. TIBTECH, 15, 185-192.
    • (1997) TIBTECH , vol.15 , pp. 185-192
    • Stahl, S.1    Uhlen, M.2
  • 9
    • 0031863713 scopus 로고    scopus 로고
    • Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae
    • Jung, H. C., Lebeault, J. M. and Pan, J. G. (1998). Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nat. Biotechnol, 16, 576-580.
    • (1998) Nat. Biotechnol , vol.16 , pp. 576-580
    • Jung, H.C.1    Lebeault, J.M.2    Pan, J.G.3
  • 10
    • 0033772459 scopus 로고    scopus 로고
    • Expressing genes in different Escherichia coli compartments
    • Cornelis, P. (2000) Expressing genes in different Escherichia coli compartments. Curr. Opin. Biotechnol, 11, 450-454.
    • (2000) Curr. Opin. Biotechnol , vol.11 , pp. 450-454
    • Cornelis, P.1
  • 11
    • 4644247440 scopus 로고    scopus 로고
    • Display of bacterial lipase on the Escherichia coli cell surface by using FadL as an anchoring motif and use of the enzyme in enantioselective biocatalysis
    • Lee, S. H., Choi, J. I., Park, S. J., Lee, S. Y. and Park, B. C. (2004). Display of bacterial lipase on the Escherichia coli cell surface by using FadL as an anchoring motif and use of the enzyme in enantioselective biocatalysis. Appl. Environ. Microbiol, 70, 5074-5080.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 5074-5080
    • Lee, S.H.1    Choi, J.I.2    Park, S.J.3    Lee, S.Y.4    Park, B.C.5
  • 12
    • 0344560614 scopus 로고    scopus 로고
    • Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif
    • Xu, Z., and Lee, S. Y. (1999). Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif. Appl. Environ. Microbiol, 65, 5142-5147.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 5142-5147
    • Xu, Z.1    Lee, S.Y.2
  • 14
    • 0029983637 scopus 로고    scopus 로고
    • Display of beta-lactamase on the Escherichia coli surface: outer membrane phenotypes conferred by Lpp'-OmpA'-beta-lactamase fusions
    • Georgiou, G., Stephens, D. L., Stathopoulos, C., Poetschke, H. L., Mendenhall, J. and Earhart, C. F. (1996). Display of beta-lactamase on the Escherichia coli surface: outer membrane phenotypes conferred by Lpp'-OmpA'-beta-lactamase fusions. Protein Eng, 9, 239-247.
    • (1996) Protein Eng , vol.9 , pp. 239-247
    • Georgiou, G.1    Stephens, D.L.2    Stathopoulos, C.3    Poetschke, H.L.4    Mendenhall, J.5    Earhart, C.F.6
  • 15
    • 0032055018 scopus 로고    scopus 로고
    • Expression of carboxymethylcellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein
    • Jung, H. C., Park, J. H., Park, S. H., Lebeault, J. M. and Pan, J. G. (1998). Expression of carboxymethylcellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein. Enzyme Microb. Technol, 22, 348-354.
    • (1998) Enzyme Microb. Technol , vol.22 , pp. 348-354
    • Jung, H.C.1    Park, J.H.2    Park, S.H.3    Lebeault, J.M.4    Pan, J.G.5
  • 16
    • 0029808395 scopus 로고    scopus 로고
    • In vivo immobilization of enzymatically active polypeptides on the cell surface of Staphylococcus carnosus
    • Strauss, A. and Gotz, F. (1996). In vivo immobilization of enzymatically active polypeptides on the cell surface of Staphylococcus carnosus. Mol. Microbiol, 21, 491-500.
    • (1996) Mol. Microbiol , vol.21 , pp. 491-500
    • Strauss, A.1    Gotz, F.2
  • 17
    • 10444272492 scopus 로고    scopus 로고
    • Use of Pseudomonas putida EstA as an anchoring motif for display of a periplasmic enzyme on the surface of Escherichia coli
    • Yang, T. H., Pan, J. G., Seo, Y. S. and Rhee, J. S. (2004). Use of Pseudomonas putida EstA as an anchoring motif for display of a periplasmic enzyme on the surface of Escherichia coli. Appl. Environ. Microbiol, 70, 6968-6976.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6968-6976
    • Yang, T.H.1    Pan, J.G.2    Seo, Y.S.3    Rhee, J.S.4
  • 18
    • 33645716056 scopus 로고    scopus 로고
    • Display of active enzymes on the cell surface of Escherichia coli using PgsA anchor protein and their application to bioconversion
    • Narita, J., Okano, K., Tateno, T., Tanino, T., Sewaki, T., Sung, M. H., Fukuda, H. and Kondo, A. (2006). Display of active enzymes on the cell surface of Escherichia coli using PgsA anchor protein and their application to bioconversion. Appl. Microbiol. Biotechnol, 70, 564-572.
    • (2006) Appl. Microbiol. Biotechnol , vol.70 , pp. 564-572
    • Narita, J.1    Okano, K.2    Tateno, T.3    Tanino, T.4    Sewaki, T.5    Sung, M.H.6    Fukuda, H.7    Kondo, A.8
  • 19
    • 33644852586 scopus 로고    scopus 로고
    • Efficient and stable display of functional proteins on bacterial magnetic particles using Mms13 as a novel anchor molecule
    • Yoshino, T. and Matsunaga, T. (2006). Efficient and stable display of functional proteins on bacterial magnetic particles using Mms13 as a novel anchor molecule. Appl. Environ. Microbiol, 72, 465-471.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 465-471
    • Yoshino, T.1    Matsunaga, T.2
  • 20
    • 0033585444 scopus 로고    scopus 로고
    • Site-protected fixation and immobilization of Escherichia coli cells displaying surface-anchored ß-lactamase
    • Freeman, A., Abramov, S. and Georgiou, G. (1999). Site-protected fixation and immobilization of Escherichia coli cells displaying surface-anchored ß-lactamase. Biotechnol. Bioeng, 62, 155-159.
    • (1999) Biotechnol. Bioeng , vol.62 , pp. 155-159
    • Freeman, A.1    Abramov, S.2    Georgiou, G.3
  • 21
    • 33646568435 scopus 로고    scopus 로고
    • Display of a thermostable lipase on the surface of a solvent-resistant bacterium, Pseudomonas putida GM730, and its applications in whole-cell biocatalysis
    • Jung, H.-C., Kwon, S.-J. and Pan, J.-G. (2006). Display of a thermostable lipase on the surface of a solvent-resistant bacterium, Pseudomonas putida GM730, and its applications in whole-cell biocatalysis. BMC Biotechnol, 6, 23.
    • (2006) BMC Biotechnol , vol.6 , pp. 23
    • Jung, H.-C.1    Kwon, S.-J.2    Pan, J.-G.3
  • 22
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder, E.T., Wittrup, K.D. (1997). Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotech, 15, 553-57.
    • (1997) Nat. Biotech , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 24
    • 0034045526 scopus 로고    scopus 로고
    • Genetic immobilization of proteins on the yeast cell surface
    • Ueda, M. and Tanaka, A. (2000). Genetic immobilization of proteins on the yeast cell surface. Biotechnol. Adv, 18, 121-140.
    • (2000) Biotechnol. Adv , vol.18 , pp. 121-140
    • Ueda, M.1    Tanaka, A.2
  • 26
    • 33645031498 scopus 로고    scopus 로고
    • Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production
    • Wang, Z., Qi, Q. and Wang, P. G. (2006). Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production. Appl. Environ. Microbiol, 72, 1873-1877.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 1873-1877
    • Wang, Z.1    Qi, Q.2    Wang, P.G.3
  • 27
    • 0029311193 scopus 로고
    • Self-cloning in filamentous fungi: application to the construction of endothiapepsin overproducers in Cryphonectria parasitica
    • Jara, P., Delmas, P., Razanamparany, V., Olsen, L., Dupin, P., Bayol, A., Begueret, J. and Loison, G. (1995). Self-cloning in filamentous fungi: application to the construction of endothiapepsin overproducers in Cryphonectria parasitica. J. Biotechnol, 40, 111-120.
    • (1995) J. Biotechnol , vol.40 , pp. 111-120
    • Jara, P.1    Delmas, P.2    Razanamparany, V.3    Olsen, L.4    Dupin, P.5    Bayol, A.6    Begueret, J.7    Loison, G.8
  • 28
    • 3843106901 scopus 로고    scopus 로고
    • Construction of a self-cloning sake yeast that overexpresses alcohol acetyltransferase gene by a two-step gene replacement protocol
    • Hirosawa, I., Aritomi, K., Hoshida, H., Kashiwagi, S., Nishizawa, Y. and Akada, R. (2004). Construction of a self-cloning sake yeast that overexpresses alcohol acetyltransferase gene by a two-step gene replacement protocol. Appl. Microbiol. Biotechnol, 65, 68-73.
    • (2004) Appl. Microbiol. Biotechnol , vol.65 , pp. 68-73
    • Hirosawa, I.1    Aritomi, K.2    Hoshida, H.3    Kashiwagi, S.4    Nishizawa, Y.5    Akada, R.6
  • 29
    • 0032975332 scopus 로고    scopus 로고
    • Development of a self-cloning system for Actinomadura verrucosospora and identification of polyketide synthase genes essential for production of the angucyclic antibiotic pradimicin
    • Dairi, T., Hamano, Y., Furumai, T. and Oki, T. (1999). Development of a self-cloning system for Actinomadura verrucosospora and identification of polyketide synthase genes essential for production of the angucyclic antibiotic pradimicin. Appl. Environ. Microbiol, 65, 2703-2709.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 2703-2709
    • Dairi, T.1    Hamano, Y.2    Furumai, T.3    Oki, T.4
  • 30
    • 0022410133 scopus 로고
    • Self-cloning in Streptomyces griseus of an str gene cluster for streptomycin biosynthesis and streptomycin resistance
    • Ohnuki, T., Imanaka, T. and Aiba, S. (1985). Self-cloning in Streptomyces griseus of an str gene cluster for streptomycin biosynthesis and streptomycin resistance. J. Bacteriol, 164, 85-94.
    • (1985) J. Bacteriol , vol.164 , pp. 85-94
    • Ohnuki, T.1    Imanaka, T.2    Aiba, S.3
  • 31
    • 0026559510 scopus 로고
    • Self cloning in Micromonospora olivasterospora of fms genes for fortimicin A (astromicin) biosynthesis
    • Dairi, T., Ohta, T., Hashimoto, E. and Hasegawa, M. (1992). Self cloning in Micromonospora olivasterospora of fms genes for fortimicin A (astromicin) biosynthesis. Mol. Gen. Genet, 232, 262-270.
    • (1992) Mol. Gen. Genet , vol.232 , pp. 262-270
    • Dairi, T.1    Ohta, T.2    Hashimoto, E.3    Hasegawa, M.4
  • 32
    • 0029999566 scopus 로고    scopus 로고
    • Increase of xanthan production by self-cloning of a 3.0-kb EcoRI-KpnI chromosomal fragment in Xanthomonas campestris
    • Wei, C.-L., Choy, K.-T., Lin, N.-T. and Tseng, Y.-H. (1996). Increase of xanthan production by self-cloning of a 3.0-kb EcoRI-KpnI chromosomal fragment in Xanthomonas campestris. Biotechno. Lett, 18, 1301-1304.
    • (1996) Biotechno. Lett , vol.18 , pp. 1301-1304
    • Wei, C.-L.1    Choy, K.-T.2    Lin, N.-T.3    Tseng, Y.-H.4
  • 34
    • 0344687415 scopus 로고    scopus 로고
    • Regeneration of cofactors for use in biocatalysis
    • Zhao, H. and van der Donk, W. A. (2003). Regeneration of cofactors for use in biocatalysis. Curr. Opin. Biotechnol, 14, 583-589.
    • (2003) Curr. Opin. Biotechnol , vol.14 , pp. 583-589
    • Zhao, H.1    van der Donk, W.A.2
  • 35
    • 33846197938 scopus 로고    scopus 로고
    • Biocatalysis for pharmaceutical intermediates: the future is now
    • Pollard, D. J. and Woodley, J. M. (2006). Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol, 25, 66-73.
    • (2006) Trends Biotechnol , vol.25 , pp. 66-73
    • Pollard, D.J.1    Woodley, J.M.2
  • 36
    • 0031259833 scopus 로고    scopus 로고
    • Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins
    • Nilsson, J., Stahl, S., Lundeberg, J., Uhlen, M. and Nygren, P. A. (1997). Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins. Protein Expr. Purif, 11, 1-16.
    • (1997) Protein Expr. Purif , vol.11 , pp. 1-16
    • Nilsson, J.1    Stahl, S.2    Lundeberg, J.3    Uhlen, M.4    Nygren, P.A.5
  • 37
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusion: from molecular and biochemical fundamentals to commercial systems
    • Terpe, K. (2003). Overview of tag protein fusion: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol, 60, 523-533.
    • (2003) Appl. Microbiol. Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 39
    • 18144390619 scopus 로고    scopus 로고
    • Chitin-binding domain based immobilization of Dhydantoinase
    • Chern, J.-T. and Chao, Y.-P. (2005). Chitin-binding domain based immobilization of Dhydantoinase. J. Biotechnol, 117, 267-275.
    • (2005) J. Biotechnol , vol.117 , pp. 267-275
    • Chern, J.-T.1    Chao, Y.-P.2
  • 40
    • 0037134639 scopus 로고    scopus 로고
    • Immobilization and utilization of the recombinant fusion proteins trypsin-streptavidin and streptavidin-transglutaminase for modification of whey protein isolate functionality
    • Wilcox, C. P., Clare, D. A., Valentine, V. W. and Swaisgood, H. E. (2002) Immobilization and utilization of the recombinant fusion proteins trypsin-streptavidin and streptavidin-transglutaminase for modification of whey protein isolate functionality. J. Agric. Food Chem, 50, 3723-3730.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 3723-3730
    • Wilcox, C.P.1    Clare, D.A.2    Valentine, V.W.3    Swaisgood, H.E.4
  • 41
    • 0025435164 scopus 로고
    • Affinity immobilization of a genetically engineered bifunctional hybrid protein
    • Baneyx, F., Schmidt, C., Georgiou, G. (1990). Affinity immobilization of a genetically engineered bifunctional hybrid protein. Enzyme Microb. Technol, 12, 337-342.
    • (1990) Enzyme Microb. Technol , vol.12 , pp. 337-342
    • Baneyx, F.1    Schmidt, C.2    Georgiou, G.3
  • 43
    • 0035148782 scopus 로고    scopus 로고
    • One-step purification, covalent immobilization, and additional stabilization of poly-his-tagged proteins using novel heterofunctional chelate-epoxy supports
    • Mateo, C., Fernandez-Lorente, G., Cortes, E., Garcia, J. L., Fernandez-Lafuente, R. and Guisan, J. M. (2001). One-step purification, covalent immobilization, and additional stabilization of poly-his-tagged proteins using novel heterofunctional chelate-epoxy supports. Biotechnol. Bioeng, 76 (2001) 269-267.
    • (2001) Biotechnol. Bioeng , vol.76 , pp. 269-267
    • Mateo, C.1    Fernandez-Lorente, G.2    Cortes, E.3    Garcia, J.L.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 44
    • 0030224856 scopus 로고    scopus 로고
    • Multiple affinity domains for the detection, purification and immobilization of recombinant proteins
    • Nilsson, J., Larsson, M., Stahl, S., Nygren, P. A. and Uhlen, M. (1996). Multiple affinity domains for the detection, purification and immobilization of recombinant proteins. J. Mol. Recognit, 9, 585-594.
    • (1996) J. Mol. Recognit , vol.9 , pp. 585-594
    • Nilsson, J.1    Larsson, M.2    Stahl, S.3    Nygren, P.A.4    Uhlen, M.5
  • 45
    • 0842267059 scopus 로고    scopus 로고
    • A novel multi-affinity tag system to produce high levels of soluble and biotinylated proteins in Escherichia coli
    • Ashraf, S. S., Benson, R. E., Payne, E. S., Halbleib, C. M. and Gron, H. (2004). A novel multi-affinity tag system to produce high levels of soluble and biotinylated proteins in Escherichia coli. Protein Expr.Purif, 33, 238-245.
    • (2004) Protein Expr.Purif , vol.33 , pp. 238-245
    • Ashraf, S.S.1    Benson, R.E.2    Payne, E.S.3    Halbleib, C.M.4    Gron, H.5
  • 46
    • 0031214792 scopus 로고    scopus 로고
    • High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system
    • Pryor, K. D. and Leiting, B. (1997). High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system. Protein Expr. Purif, 10, 309-319.
    • (1997) Protein Expr. Purif , vol.10 , pp. 309-319
    • Pryor, K.D.1    Leiting, B.2
  • 47
    • 0035866279 scopus 로고    scopus 로고
    • A novel multiple affinity purification tag and its use in identification of proteins associated with a cyclin-CDK complex
    • Honey, S., Schneider, B. L., Schieltz, D. M., Yates, J. R. and Futcher, B. (2001). A novel multiple affinity purification tag and its use in identification of proteins associated with a cyclin-CDK complex. Nucleic Acids Res, 29, E24.
    • (2001) Nucleic Acids Res , vol.29
    • Honey, S.1    Schneider, B.L.2    Schieltz, D.M.3    Yates, J.R.4    Futcher, B.5
  • 48
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: a general procedure of protein complex purification
    • Puig, O., Caspary, F., Rigaut, G., Rutz, B., Bouveret, E., Bragado-Nilsson, E., Wilm, M. and Seraphin, B. (2001). The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods, 24, 218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Seraphin, B.8
  • 49
    • 0027431041 scopus 로고
    • Immobilization of dihydrofolate reductase by engineered cysteine residue attached to its C-terminal end
    • Iwakura, M. and Kokubu, T. (1993). Immobilization of dihydrofolate reductase by engineered cysteine residue attached to its C-terminal end. J. Biochem. (Tokyo), 114, 339-343.
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 339-343
    • Iwakura, M.1    Kokubu, T.2
  • 50
    • 33644983895 scopus 로고    scopus 로고
    • Production of 2-keto-3-deoxy-D-glycero-Dgalacto- nonopyranulosonic acid (KDN) using fusion protein of N-acetyl-D-neuraminic acid aldolase
    • Wang, T.-H. and Lee, W.-C. (2006). Production of 2-keto-3-deoxy-D-glycero-Dgalacto- nonopyranulosonic acid (KDN) using fusion protein of N-acetyl-D-neuraminic acid aldolase. Biochem. Eng. J, 29, 75-80.
    • (2006) Biochem. Eng. J , vol.29 , pp. 75-80
    • Wang, T.-H.1    Lee, W.-C.2


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