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Volumn 75, Issue 1, 2009, Pages 29-38

Biotechnological process for production of β-dipeptides from cyanophycin on a technical scale and its optimization

Author keywords

[No Author keywords available]

Indexed keywords

ACID EXTRACTIONS; ALCALIGENES; ASPARTATE; BIOTECHNOLOGICAL PROCESSES; CYANOPHYCIN; DEGRADATION PARAMETERS; DI PEPTIDES; EXTRACELLULAR; FERMENTATIVE PRODUCTIONS; HIGH-PERFORMANCE LIQUID CHROMATOGRAPHIES; INDUSTRIAL MATERIALS; MINERAL SALTS MEDIUMS; OPTIMIZED PROCESSES; OVERALL EFFICIENCIES; PHASE I; PHASE II; SERINE PROTEASES; SOLE CARBON SOURCES; SPECIFIC BINDINGS;

EID: 58149359424     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01344-08     Document Type: Article
Times cited : (47)

References (51)
  • 1
    • 0033714944 scopus 로고    scopus 로고
    • Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308
    • Aboulmagd, E., F. B. Oppermann-Sanio, and A. Steinbuchel. 2000. Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308. Arch. Microbiol. 174:297-306.
    • (2000) Arch. Microbiol , vol.174 , pp. 297-306
    • Aboulmagd, E.1    Oppermann-Sanio, F.B.2    Steinbuchel, A.3
  • 2
    • 0035668788 scopus 로고    scopus 로고
    • Heterologous expression of cyanophycin synthetase and cyanophycin synthesis in the industrial relevant bacteria Corynebacterium glutamicum and Ralstonia eutropha and in Pseudomonas putida
    • Aboulmagd, E., I. Voss, F. B. Oppermann-Sanio, and A. Steinbüchel. 2001. Heterologous expression of cyanophycin synthetase and cyanophycin synthesis in the industrial relevant bacteria Corynebacterium glutamicum and Ralstonia eutropha and in Pseudomonas putida. Biomacromolecules 2:1338-1342.
    • (2001) Biomacromolecules , vol.2 , pp. 1338-1342
    • Aboulmagd, E.1    Voss, I.2    Oppermann-Sanio, F.B.3    Steinbüchel, A.4
  • 3
    • 0342351485 scopus 로고
    • Lipases with improved surfactant resistance
    • International patent WO 95/30744
    • Aehle, W., G. Gerritse, and H. B. Lenting. 1995. Lipases with improved surfactant resistance. International patent WO 95/30744.
    • (1995)
    • Aehle, W.1    Gerritse, G.2    Lenting, H.B.3
  • 4
    • 0018822016 scopus 로고
    • Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308
    • Allen, M. M., M. F. Hutchinson, and P. J. Weathers, 1980. Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308. J. Bacteriol. 141:687-693.
    • (1980) J. Bacteriol , vol.141 , pp. 687-693
    • Allen, M.M.1    Hutchinson, M.F.2    Weathers, P.J.3
  • 5
    • 0000401988 scopus 로고
    • Inclusions: Cyanophycin
    • Allen, M. M, 1988. Inclusions: cyanophycin. Methods Enzymol. 167;207-213.
    • (1988) Methods Enzymol , vol.167 , pp. 207-213
    • Allen, M.M.1
  • 6
    • 0002370906 scopus 로고
    • Le comunicazioni intracellulari delle Nostochinee.
    • Borzi, A. 1887. Le comunicazioni intracellulari delle Nostochinee. Malpighia 1:28-74.
    • (1887) Malpighia , vol.1 , pp. 28-74
    • Borzi, A.1
  • 8
    • 0032162609 scopus 로고    scopus 로고
    • Preparation and characterization of a poly(β-hydroxyalkanoate) latex produced by Pseudomonas oleovorans
    • Dufresne, A., and E, Samain. 1998. Preparation and characterization of a poly(β-hydroxyalkanoate) latex produced by Pseudomonas oleovorans. Macromolecules 31:6426-6433.
    • (1998) Macromolecules , vol.31 , pp. 6426-6433
    • Dufresne, A.1    Samain, E.2
  • 9
    • 58149348669 scopus 로고
    • Expertise clinique de l'aspartate d'arginine.
    • Duruy, A. 1966. Expertise clinique de l'aspartate d'arginine. Med. Int. 1:203.
    • (1966) Med. Int , vol.1 , pp. 203
    • Duruy, A.1
  • 10
    • 29144497375 scopus 로고    scopus 로고
    • Protamylasse, a residual compound of industrial starch production, provides a suitable medium for large-scale cyanophycin production
    • Elbahloul, Y., K. Frey, J. Sanders, and A. Steinbüchel. 2005. Protamylasse, a residual compound of industrial starch production, provides a suitable medium for large-scale cyanophycin production. Appl. Environ. Microbiol. 71:7759-7767.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 7759-7767
    • Elbahloul, Y.1    Frey, K.2    Sanders, J.3    Steinbüchel, A.4
  • 11
    • 0036304471 scopus 로고    scopus 로고
    • Frey, K, M., F. B. Oppermann-Sanio, H. Schmidt, and A, Steinbiichel, 2002. Technical-scale production of cyanophycin with recombinant strains of Escherichia coli. Appl. Environ. Microbiol. 68:3377-3384.
    • Frey, K, M., F. B. Oppermann-Sanio, H. Schmidt, and A, Steinbiichel, 2002. Technical-scale production of cyanophycin with recombinant strains of Escherichia coli. Appl. Environ. Microbiol. 68:3377-3384.
  • 12
    • 34447331068 scopus 로고    scopus 로고
    • Analysis of genome sequences for genes of cyanophycin metabolism: Identifying putative cyanophycin metabolizing prokaryotes
    • Füser, G., and A. Steinbüchel. 2007. Analysis of genome sequences for genes of cyanophycin metabolism: identifying putative cyanophycin metabolizing prokaryotes. Macromol. Biosci. 7:278-296.
    • (2007) Macromol. Biosci , vol.7 , pp. 278-296
    • Füser, G.1    Steinbüchel, A.2
  • 13
    • 0031840830 scopus 로고    scopus 로고
    • Development of a lipase fermentation process that uses a recombinant Pseudomonas alcaligenes strain
    • Gerritse, G., R. W. Hommes, and W. J. Quax. 1998. Development of a lipase fermentation process that uses a recombinant Pseudomonas alcaligenes strain. Appl. Environ. Microbiol. 64:2644-2651.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 2644-2651
    • Gerritse, G.1    Hommes, R.W.2    Quax, W.J.3
  • 14
    • 0019384375 scopus 로고
    • Enzyme activities related to cyanophycin metabolism in heterocysts and vegetative cells of Anabaena spp
    • Gupta, M., and N. G. Carr. 1981. Enzyme activities related to cyanophycin metabolism in heterocysts and vegetative cells of Anabaena spp. J. Gen. Microbiol. 125:17-23.
    • (1981) J. Gen. Microbiol , vol.125 , pp. 17-23
    • Gupta, M.1    Carr, N.G.2
  • 15
    • 4143051569 scopus 로고    scopus 로고
    • Polyaspartic acids
    • S. R. Fahnestock and A. Steinbüchel ed, Wiley, Weinheim. Germany
    • Joentgen, W., N. Müller, A. Mitschker, and H. Schmidt. 2003. Polyaspartic acids, p. 175-199. In S. R. Fahnestock and A. Steinbüchel (ed.), Biopolymers, vol. 7. Wiley, Weinheim. Germany.
    • (2003) Biopolymers , vol.7 , pp. 175-199
    • Joentgen, W.1    Müller, N.2    Mitschker, A.3    Schmidt, H.4
  • 16
    • 0036236197 scopus 로고    scopus 로고
    • Evaluation of non-cyanobacterial genome sequences for occurrence of genes encoding proteins homologous to cyanophycin synthetase and cloning of an active cyanophycin synthetase from Acinetobacter sp. strain DSM 587
    • Krehenbrink, M., F. B. Oppermann-Sanio, and A. Steinbüchel. 2002. Evaluation of non-cyanobacterial genome sequences for occurrence of genes encoding proteins homologous to cyanophycin synthetase and cloning of an active cyanophycin synthetase from Acinetobacter sp. strain DSM 587. Arch. Microbiol. 177:371-380.
    • (2002) Arch. Microbiol , vol.177 , pp. 371-380
    • Krehenbrink, M.1    Oppermann-Sanio, F.B.2    Steinbüchel, A.3
  • 17
    • 0019139168 scopus 로고
    • Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate
    • Lacks, S. A., and S. S. Springhorn. 1980. Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. J. Biol. Chem. 225:7467-7473.
    • (1980) J. Biol. Chem , vol.225 , pp. 7467-7473
    • Lacks, S.A.1    Springhorn, S.S.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 40649085329 scopus 로고    scopus 로고
    • Prelox for improvement of erectile function: A review
    • Lamm, S., F. Schönlau, and P. Rohdewald. 2003. Prelox for improvement of erectile function: a review. Eur. Bull. Drug Res. 11:29-37.
    • (2003) Eur. Bull. Drug Res , vol.11 , pp. 29-37
    • Lamm, S.1    Schönlau, F.2    Rohdewald, P.3
  • 20
    • 0029555330 scopus 로고
    • In vivo pharmacokinetics study for the assessment of poly(L-aspartic acid) as a drug carrier for colon-specific drug delivery
    • Leopold, C. S., and D. R. Friend. 1995. In vivo pharmacokinetics study for the assessment of poly(L-aspartic acid) as a drug carrier for colon-specific drug delivery. J. Pharmacokinet. Biopharm. 4:397-406.
    • (1995) J. Pharmacokinet. Biopharm , vol.4 , pp. 397-406
    • Leopold, C.S.1    Friend, D.R.2
  • 21
    • 0034928543 scopus 로고    scopus 로고
    • Pattern of cyanophycin accumulation in nitrogen-fixing and non-nitrogen-fixing cyanobacteria
    • Li, H., D. M. Sherman, S. Bao, and L. A. Sherman. 2001. Pattern of cyanophycin accumulation in nitrogen-fixing and non-nitrogen-fixing cyanobacteria. Arch. Microbiol. 176:9-18.
    • (2001) Arch. Microbiol , vol.176 , pp. 9-18
    • Li, H.1    Sherman, D.M.2    Bao, S.3    Sherman, L.A.4
  • 22
    • 0030002855 scopus 로고    scopus 로고
    • Effect of the nitrogen source on phycobiliprotein synthesis and cell reserves in a chromatically adapting filamentous cyanobacterium
    • Liotenberg, S., D. Campbell, R. Rippka, J. Houmard, and N. T. de Marsac. 1996. Effect of the nitrogen source on phycobiliprotein synthesis and cell reserves in a chromatically adapting filamentous cyanobacterium. Microbiology 142:611-622.
    • (1996) Microbiology , vol.142 , pp. 611-622
    • Liotenberg, S.1    Campbell, D.2    Rippka, R.3    Houmard, J.4    de Marsac, N.T.5
  • 23
    • 0025054141 scopus 로고
    • Transient accumulation of cyanophycin in Anabaena cylindrical and Synechocystis 6308
    • Mackerras, A. H., N. M. de Chazal, and G. D. Smith, 1990. Transient accumulation of cyanophycin in Anabaena cylindrical and Synechocystis 6308. J. Gen. Microbiol. 136:2057-2065.
    • (1990) J. Gen. Microbiol , vol.136 , pp. 2057-2065
    • Mackerras, A.H.1    de Chazal, N.M.2    Smith, G.D.3
  • 24
    • 0025310598 scopus 로고
    • Visceral protein levels in trauma patients are greater with peptide diet than with intact protein diet
    • Meredith, J. W., J. A. Ditesheim, and G. Zaloga.1990. Visceral protein levels in trauma patients are greater with peptide diet than with intact protein diet. J. Trauma 30: 825-828."
    • (1990) J. Trauma , vol.30 , pp. 825-828
    • Meredith, J.W.1    Ditesheim, J.A.2    Zaloga, G.3
  • 26
    • 58149337498 scopus 로고    scopus 로고
    • Moore, E. R. B, B. J. Tindall, V. A. P. Martins Dos Santos, D. R. H. Pieper, J. Ramos, and N. J. Palleroni. May 1999, posting date. Pseudomonas: non-medical. In M. Dworkin ct al, ed, The prokaryotes: an evolving electronic resource for the microbiological community, 3rd ed, release 3.0. Springer, New York, NY. doi:l0.l007/0-387-30746-X-21
    • Moore, E. R. B., B. J. Tindall, V. A. P. Martins Dos Santos, D. R. H. Pieper, J. Ramos, and N. J. Palleroni. May 1999, posting date. Pseudomonas: non-medical. In M. Dworkin ct al. (ed.), The prokaryotes: an evolving electronic resource for the microbiological community, 3rd ed., release 3.0. Springer, New York, NY. doi:l0.l007/0-387-30746-X-21.
  • 27
    • 0028219162 scopus 로고
    • A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels
    • Nesterenko, M. V., M. Tilley, and S. J. Upton, 1994. A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels. J. Biochem. Biophys. Methods 3:239-242.
    • (1994) J. Biochem. Biophys. Methods , vol.3 , pp. 239-242
    • Nesterenko, M.V.1    Tilley, M.2    Upton, S.J.3
  • 28
    • 0037067662 scopus 로고    scopus 로고
    • Isolation of cyanophycin degrading bacteria, cloning and characterization of an extracellular cyanophycinase gene (cphE) from Pseudomonas anguilliseptica strain BI-the cphE gene from P. anguilliseptica BI encodes a cyanophycin-hydro-lyzing enzyme
    • Obst, M., F. B. Oppermann-Sanio, and A. Steinbüchel. 2002. Isolation of cyanophycin degrading bacteria, cloning and characterization of an extracellular cyanophycinase gene (cphE) from Pseudomonas anguilliseptica strain BI-the cphE gene from P. anguilliseptica BI encodes a cyanophycin-hydro-lyzing enzyme. J. Biol. Chem. 277:25096-25105.
    • (2002) J. Biol. Chem , vol.277 , pp. 25096-25105
    • Obst, M.1    Oppermann-Sanio, F.B.2    Steinbüchel, A.3
  • 29
    • 0842323017 scopus 로고    scopus 로고
    • Isolation and characterization of gram-positive cyanophycin-degrading bacteria-kinetic studies on cyanophycin depolymerase activity in aerobic bacteria
    • Obst, M., A. Sallam, H. Luftmann, and A. Steinbüchel. 2004. Isolation and characterization of gram-positive cyanophycin-degrading bacteria-kinetic studies on cyanophycin depolymerase activity in aerobic bacteria. Biomac-romolecules 5:153-161.
    • (2004) Biomac-romolecules , vol.5 , pp. 153-161
    • Obst, M.1    Sallam, A.2    Luftmann, H.3    Steinbüchel, A.4
  • 30
    • 4143054876 scopus 로고    scopus 로고
    • Microbial degradation of poly(amino acid)s
    • Obst, M., and A. Steinbüchel. 2004. Microbial degradation of poly(amino acid)s. Biomacromolecules 5:1166-1176.
    • (2004) Biomacromolecules , vol.5 , pp. 1166-1176
    • Obst, M.1    Steinbüchel, A.2
  • 31
    • 22144476898 scopus 로고    scopus 로고
    • Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G isolated from an anaerobic bacterium consortium
    • Obst, M., A. Krug, H. Luftmann, and A. Steinbüchel. 2005. Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G isolated from an anaerobic bacterium consortium. Appl. Environ. Microbiol. 71:3642-3652.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 3642-3652
    • Obst, M.1    Krug, A.2    Luftmann, H.3    Steinbüchel, A.4
  • 32
    • 58149354809 scopus 로고    scopus 로고
    • Obst, M., and A. Steinbüchel, 2006. Cyanophycin-an ideal bacterial nitrogen storage material with unique chemical properties, p. 167-194. In J. M. 47. Shively (ed.), Inclusions in prokaryotes. 1. Springer-Verlag, Berlin, Germany.
    • Obst, M., and A. Steinbüchel, 2006. Cyanophycin-an ideal bacterial nitrogen storage material with unique chemical properties, p. 167-194. In J. M. 47. Shively (ed.), Inclusions in prokaryotes. vol. 1. Springer-Verlag, Berlin, Germany.
  • 33
    • 0036164128 scopus 로고    scopus 로고
    • Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production
    • Oppermann-Sanio, F. B., and A. Steinbuchel. 2002. Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production. Naturwissenschaftcn 89:11-22.
    • (2002) Naturwissenschaftcn , vol.89 , pp. 11-22
    • Oppermann-Sanio, F.B.1    Steinbuchel, A.2
  • 34
    • 4143108184 scopus 로고    scopus 로고
    • Cyanophycin
    • S. R. Fahnestock and A. Steinbuchel ed, Wiley- VCH, Weinheim, Germany
    • Oppermann-Sanio, F. B., and A. Steinbüchel. 2003. Cyanophycin, p. 83-106. In S. R. Fahnestock and A. Steinbuchel (ed.), Biopolymers, vol. 7. Wiley- VCH, Weinheim, Germany.
    • (2003) Biopolymers , vol.7 , pp. 83-106
    • Oppermann-Sanio, F.B.1    Steinbüchel, A.2
  • 35
    • 0033167939 scopus 로고    scopus 로고
    • Cyanophycinase, a peptidase degrading the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartic acid (cyanophycin). Molecular cloning of the gene 50. of Synechocystis sp. PCC6803, expression in Escherichia coli, and biochemical characterization of the purified enzyme
    • Richter, R., M. Hejazi, R. Kraft, K. Ziegler, and W. Loekau. 1999. Cyanophycinase, a peptidase degrading the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartic acid (cyanophycin). Molecular cloning of the gene 50. of Synechocystis sp. PCC6803, expression in Escherichia coli, and biochemical characterization of the purified enzyme. Eur. J. Biochem. 263:163-169.
    • (1999) Eur. J. Biochem , vol.263 , pp. 163-169
    • Richter, R.1    Hejazi, M.2    Kraft, R.3    Ziegler, K.4    Loekau, W.5
  • 36
    • 44949198468 scopus 로고    scopus 로고
    • Anaerobic and aerobic degradation of cyanophycin by the denitrifying bacterium Pseudomonas alcaligenes strain DIPI and the role of three other co-isolates in a mixed bacterial consortium
    • Sallam, A., and A. Steinbüchel. 2008. Anaerobic and aerobic degradation of cyanophycin by the denitrifying bacterium Pseudomonas alcaligenes strain DIPI and the role of three other co-isolates in a mixed bacterial consortium. Appl. Environ. Microbiol. 74:3434-3443.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 3434-3443
    • Sallam, A.1    Steinbüchel, A.2
  • 38
    • 0031599328 scopus 로고    scopus 로고
    • Chemical synthesis of polyaspartates: A biodegradable alternative to currently used polyearboxylate homo- and copolymers
    • Schwamborn, M. 1998. Chemical synthesis of polyaspartates: a biodegradable alternative to currently used polyearboxylate homo- and copolymers. Polym. Degrad. Stabil. 59:39-45.
    • (1998) Polym. Degrad. Stabil , vol.59 , pp. 39-45
    • Schwamborn, M.1
  • 39
    • 14244272402 scopus 로고
    • Intéret de l'aspartate d'arginine sargenor chez des athletes de compétition en périod d'entrainement intensif.
    • Sellier, J. 1979. Intéret de l'aspartate d'arginine sargenor chez des athletes de compétition en périod d'entrainement intensif. Rev. Med. Toulouse 5:879.
    • (1979) Rev. Med. Toulouse , vol.5 , pp. 879
    • Sellier, J.1
  • 40
    • 0033713355 scopus 로고    scopus 로고
    • 2-fixing cultures of the cyanobacterium Anabaena sp. PCC7120. J. Phycol. 36:932-941.
    • 2-fixing cultures of the cyanobacterium Anabaena sp. PCC7120. J. Phycol. 36:932-941.
  • 41
    • 0017263448 scopus 로고
    • The biosynthesis of multi-L-arginyl-poly(L- aspartic acid) in the filamentous cyanobacterium Anabaena cylindrica
    • Simon, R. D. 1976. The biosynthesis of multi-L-arginyl-poly(L- aspartic acid) in the filamentous cyanobacterium Anabaena cylindrica. Biochim. Biophys. Acta 422: 407-418.
    • (1976) Biochim. Biophys. Acta , vol.422 , pp. 407-418
    • Simon, R.D.1
  • 42
    • 0016881981 scopus 로고
    • Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in cyanobacteria
    • Simon, R. D., and P. Weathers. 1976. Determination of the structure of the novel polypeptide containing aspartic acid and arginine which is found in cyanobacteria. Biochim. Biophys. Acta 420:165-176.
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 165-176
    • Simon, R.D.1    Weathers, P.2
  • 43
    • 0001899348 scopus 로고
    • Inclusion bodies in the cyanobacteria: Cyanophycin, polyphosphate, polyhedral bodies
    • P. Fay and C. van Baalen ed, Elsevier, Amsterdam. The Netherlands
    • Simon, R. D. 1987. Inclusion bodies in the cyanobacteria: cyanophycin, polyphosphate, polyhedral bodies, p. 199-225. In P. Fay and C. van Baalen (ed.), The cyanobacteria. Elsevier, Amsterdam. The Netherlands.
    • (1987) The cyanobacteria , pp. 199-225
    • Simon, R.D.1
  • 44
    • 0034493599 scopus 로고    scopus 로고
    • Interrelation between cyanophycin synthesis, L-arginine catabolism and photosynthesis in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Stephan, D. P., H. G, Ruppel, and E. K. Pistorius. 2000. Interrelation between cyanophycin synthesis, L-arginine catabolism and photosynthesis in the cyanobacterium Synechocystis sp. strain PCC 6803. Z. Naturforsch. 55: 927-942.
    • (2000) Z. Naturforsch , vol.55 , pp. 927-942
    • Stephan, D.P.H.G.1    Ruppel2    Pistorius, E.K.3
  • 45
    • 0021847777 scopus 로고
    • Break of unresponsiveness to delayed-type hypersensitivity to sheep red blood cells by pertussis toxin
    • Tamura, S. I., H. Tanaka, R. Takayama, H. Sato, Y. Sato, and N. Uehida. 1985. Break of unresponsiveness to delayed-type hypersensitivity to sheep red blood cells by pertussis toxin. Cell. Immunol. 92:376-386.
    • (1985) Cell. Immunol , vol.92 , pp. 376-386
    • Tamura, S.I.1    Tanaka, H.2    Takayama, R.3    Sato, H.4    Sato, Y.5    Uehida, N.6
  • 46
    • 29544440779 scopus 로고    scopus 로고
    • Voss, I., and A. Steinbuchel. 2006. Application of a KDPG-aldolase gene-dependent addiction system for enhanced production of cyanophycin in Ralstonia eutropha strain H16. Metab. Eng. 8:66-78.
    • Voss, I., and A. Steinbuchel. 2006. Application of a KDPG-aldolase gene-dependent addiction system for enhanced production of cyanophycin in Ralstonia eutropha strain H16. Metab. Eng. 8:66-78.
  • 47
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sul fate-polyacrylamide gel electrophoresis
    • Weber, K., and M. Osborn. 1969. The reliability of molecular weight determinations by dodecyl sul fate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244: 4406-4412.
    • (1969) J. Biol. Chem , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 48
    • 0036206049 scopus 로고    scopus 로고
    • Cyanophycin production in a phycoerythrin-containing marine Synechococcus strain of unusual phylogenetic affinity
    • Wingard, L. L., S. R. Miller, J. M. Sellker, E. Stenn, M. M. Allen, and A. M. Wood. 2002. Cyanophycin production in a phycoerythrin-containing marine Synechococcus strain of unusual phylogenetic affinity. Appl. Environ. Microbiol. 68:1772-1777.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 1772-1777
    • Wingard, L.L.1    Miller, S.R.2    Sellker, J.M.3    Stenn, E.4    Allen, M.M.5    Wood, A.M.6
  • 49
    • 0025343062 scopus 로고
    • Characterization and anticancer activity of the micelle forming polymeric anticancer drug adriamycin-conjugated poly(ethylene glycol)-poly (aspartic acid) block copolymer
    • Yokoyama, M., M. Miyauchi, N. Yamada, T. Okano, Y. Sakurai, K. Kataoka, and S, Inoue. 1990. Characterization and anticancer activity of the micelle forming polymeric anticancer drug adriamycin-conjugated poly(ethylene glycol)-poly (aspartic acid) block copolymer. Cancer Res. 6: 1693-1700.
    • (1990) Cancer Res , vol.6 , pp. 1693-1700
    • Yokoyama, M.1    Miyauchi, M.2    Yamada, N.3    Okano, T.4    Sakurai, Y.5    Kataoka, K.6    Inoue, S.7
  • 50
    • 0032523821 scopus 로고    scopus 로고
    • Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacteria] reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)
    • Ziegler, K., A. Diener, C. Herpin, R. Richter, R. Deutzmann, and W. Loekau. 1998. Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacteria] reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). Eur. J. Biochem. 254: 154-159.
    • (1998) Eur. J. Biochem , vol.254 , pp. 154-159
    • Ziegler, K.1    Diener, A.2    Herpin, C.3    Richter, R.4    Deutzmann, R.5    Loekau, W.6
  • 51
    • 0036560886 scopus 로고    scopus 로고
    • Cyanophycin synthetase-like enzymes of n on-cyanobacterial eubacteria: Characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense
    • Ziegler, K., R. Deutzmann, and W. Loekau. 2002. Cyanophycin synthetase-like enzymes of n on-cyanobacterial eubacteria: characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense. Z. Naturforsch. 57c:522-529.
    • (2002) Z. Naturforsch , vol.57 c , pp. 522-529
    • Ziegler, K.1    Deutzmann, R.2    Loekau, W.3


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