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Volumn 132, Issue 4, 2007, Pages 385-394

Effect of different carbon sources on central metabolic fluxes and the recombinant production of a hydrolase from Thermobifida fusca in Bacillus megaterium

Author keywords

Bacillus megaterium; Central carbon pathways; Energy metabolism; Metabolic flux analysis; Recombinant protein production

Indexed keywords

CARBOXYLIC ACIDS; CHEMOSTATS; GLUCOSE; METABOLISM;

EID: 35748946941     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.08.004     Document Type: Article
Times cited : (35)

References (32)
  • 1
    • 12544253339 scopus 로고    scopus 로고
    • Protein and vitamin production in Bacillus megaterium
    • Totowa B.J.L. (Ed), Humana Press Inc.
    • Barg H., Malten M., Jahn M., and Jahn D. Protein and vitamin production in Bacillus megaterium. In: Totowa B.J.L. (Ed). Microbiol Processes and Products (2005), Humana Press Inc. 165-184
    • (2005) Microbiol Processes and Products , pp. 165-184
    • Barg, H.1    Malten, M.2    Jahn, M.3    Jahn, D.4
  • 2
    • 0038267065 scopus 로고    scopus 로고
    • Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways
    • Blencke H.M., Homuth G., Ludwig H., Mader U., Hecker M., and Stülke J. Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab. Eng. 5 (2003) 133-149
    • (2003) Metab. Eng. , vol.5 , pp. 133-149
    • Blencke, H.M.1    Homuth, G.2    Ludwig, H.3    Mader, U.4    Hecker, M.5    Stülke, J.6
  • 3
    • 0034844144 scopus 로고    scopus 로고
    • Stoichiometric growth model for riboflavin-producing Bacillus subtilis
    • Dauner M., and Sauer U. Stoichiometric growth model for riboflavin-producing Bacillus subtilis. Biotechnol. Bioeng. 76 (2001) 132-143
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 132-143
    • Dauner, M.1    Sauer, U.2
  • 4
    • 0034847930 scopus 로고    scopus 로고
    • Metabolic flux analysis with a comprehensive isotopomer model in Bacillus subtilis
    • Dauner M., Bailey J.E., and Sauer U. Metabolic flux analysis with a comprehensive isotopomer model in Bacillus subtilis. Biotechnol. Bioeng. 76 (2001) 144-156
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 144-156
    • Dauner, M.1    Bailey, J.E.2    Sauer, U.3
  • 5
    • 33748852420 scopus 로고    scopus 로고
    • Production of a recombinant polyester-cleaving hydrolase from Thermobifida fusca in Escherichia coli
    • Dresler K., Van Den Heuvel J., Müller R.-J., and Deckwer W.-D. Production of a recombinant polyester-cleaving hydrolase from Thermobifida fusca in Escherichia coli. Bioprocess Biosyst. Eng. 29 (2006) 169-183
    • (2006) Bioprocess Biosyst. Eng. , vol.29 , pp. 169-183
    • Dresler, K.1    Van Den Heuvel, J.2    Müller, R.-J.3    Deckwer, W.-D.4
  • 6
    • 0037335931 scopus 로고    scopus 로고
    • Metabolic flux profiling of Escherichia coli mutants in central carbon metabolism using GC-MS
    • Fischer E., and Sauer U. Metabolic flux profiling of Escherichia coli mutants in central carbon metabolism using GC-MS. Eur. J. Biochem. 270 (2003) 880-891
    • (2003) Eur. J. Biochem. , vol.270 , pp. 880-891
    • Fischer, E.1    Sauer, U.2
  • 9
    • 0029764209 scopus 로고    scopus 로고
    • A direct comparison of approaches for increasing carbon flow to aromatic biosynthesis in Escherichia coli
    • Gosset G., Yong-Xiao J., and Berry A. A direct comparison of approaches for increasing carbon flow to aromatic biosynthesis in Escherichia coli. J. Ind. Microbiol. 17 (1996) 47-52
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 47-52
    • Gosset, G.1    Yong-Xiao, J.2    Berry, A.3
  • 10
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels
    • Heukeshoven J., and Dernick R. Improved silver staining procedure for fast staining in PhastSystem Development Unit. I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9 (1988) 28-32
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 11
    • 2942545896 scopus 로고    scopus 로고
    • Pyruvate formation and suppression in recombinant Bacillus megaterium cultivation
    • Hollmann R., and Deckwer W.-D. Pyruvate formation and suppression in recombinant Bacillus megaterium cultivation. J. Biotechnol. 111 (2004) 89-96
    • (2004) J. Biotechnol. , vol.111 , pp. 89-96
    • Hollmann, R.1    Deckwer, W.-D.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0026816626 scopus 로고
    • Mass isotopomer pattern and precursor-product relationship
    • Lee W.-N.P., and Bergner E.A. Mass isotopomer pattern and precursor-product relationship. Biol. Mass Spectrom. 21 (1992) 114-122
    • (1992) Biol. Mass Spectrom. , vol.21 , pp. 114-122
    • Lee, W.-N.P.1    Bergner, E.A.2
  • 14
    • 0026204952 scopus 로고
    • Mass isotopomer analysis: theoretical and practical considerations
    • Lee W.-N.P., Byerley L.O., and Bergner E.A. Mass isotopomer analysis: theoretical and practical considerations. Biol. Mass Spectrom. 20 (1991) 451-458
    • (1991) Biol. Mass Spectrom. , vol.20 , pp. 451-458
    • Lee, W.-N.P.1    Byerley, L.O.2    Bergner, E.A.3
  • 15
    • 12544256176 scopus 로고    scopus 로고
    • Production and secretion of recombinant Leuconostoc mesenteroides dextransucrase DsrS in Bacillus megaterium
    • Malten M., Hollmann R., Deckwer W.-D., and Jahn D. Production and secretion of recombinant Leuconostoc mesenteroides dextransucrase DsrS in Bacillus megaterium. Biotechnol. Bioeng. 89 (2005) 206-218
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 206-218
    • Malten, M.1    Hollmann, R.2    Deckwer, W.-D.3    Jahn, D.4
  • 16
    • 0029930612 scopus 로고    scopus 로고
    • Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coli
    • Millard C.S., Chao Y.P., Liao J.C., and Donnelly M.I. Enhanced production of succinic acid by overexpression of phosphoenolpyruvate carboxylase in Escherichia coli. Appl. Env. Microbiol. 62 (1996) 1808-1810
    • (1996) Appl. Env. Microbiol. , vol.62 , pp. 1808-1810
    • Millard, C.S.1    Chao, Y.P.2    Liao, J.C.3    Donnelly, M.I.4
  • 17
    • 0031967783 scopus 로고    scopus 로고
    • Pyruvate carboxylase from Corynebacterium glutamicum: characterization, expression and inactivation of the pyc gene
    • Peters-Wendisch P.G., Kreutzer C., Kalinowski J., Pátek M., Sahm H., and Eikmanns B.J. Pyruvate carboxylase from Corynebacterium glutamicum: characterization, expression and inactivation of the pyc gene. Microbiology 144 (1998) 915-927
    • (1998) Microbiology , vol.144 , pp. 915-927
    • Peters-Wendisch, P.G.1    Kreutzer, C.2    Kalinowski, J.3    Pátek, M.4    Sahm, H.5    Eikmanns, B.J.6
  • 19
    • 0026750940 scopus 로고
    • Catabolite repression of the xyl operon in Bacillus megaterium
    • Rygus T., and Hillen W. Catabolite repression of the xyl operon in Bacillus megaterium. J. Bacteriol. 174 (1992) 3049-3055
    • (1992) J. Bacteriol. , vol.174 , pp. 3049-3055
    • Rygus, T.1    Hillen, W.2
  • 20
    • 1242306261 scopus 로고    scopus 로고
    • High-throughput phenomics: experimental methods for mapping fluxomes
    • Sauer U. High-throughput phenomics: experimental methods for mapping fluxomes. Curr. Opin. Biotechnol. 15 (2004) 58-63
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 58-63
    • Sauer, U.1
  • 21
    • 0033588791 scopus 로고    scopus 로고
    • Estimation of P-to-O ratio in Bacillus subtilis and its influence on maximum riboflavin yield
    • Sauer U., and Bailey J.E. Estimation of P-to-O ratio in Bacillus subtilis and its influence on maximum riboflavin yield. Biotechnol. Bioeng. 64 (1999) 750-754
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 750-754
    • Sauer, U.1    Bailey, J.E.2
  • 22
    • 17644375240 scopus 로고    scopus 로고
    • The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria
    • Sauer U., and Eikmanns B.J. The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria. FEMS Microbiol. Rev. 29 (2005) 765-794
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 765-794
    • Sauer, U.1    Eikmanns, B.J.2
  • 23
    • 0028025693 scopus 로고
    • Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus
    • Schmidt-Dannert C., Sztajer H., Stocklein W., Menge U., and Schmid R.D. Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochim. Biophys. Acta 1214 (1994) 43-53
    • (1994) Biochim. Biophys. Acta , vol.1214 , pp. 43-53
    • Schmidt-Dannert, C.1    Sztajer, H.2    Stocklein, W.3    Menge, U.4    Schmid, R.D.5
  • 24
    • 14844295003 scopus 로고    scopus 로고
    • CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes
    • Servant P., Le Coq D., and Aymerich S. CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes. Mol. Microbiol. 55 (2005) 1435-1451
    • (2005) Mol. Microbiol. , vol.55 , pp. 1435-1451
    • Servant, P.1    Le Coq, D.2    Aymerich, S.3
  • 25
    • 0032600888 scopus 로고    scopus 로고
    • Metabolic fluxes and metabolic engineering
    • Stephanopoulos G. Metabolic fluxes and metabolic engineering. Metab. Eng. 1 (1999) 1-11
    • (1999) Metab. Eng. , vol.1 , pp. 1-11
    • Stephanopoulos, G.1
  • 26
    • 0029146299 scopus 로고
    • 13C-labelling of proteinogenic amino acids-an efficient tool to investigate intermediary metabolism
    • 13C-labelling of proteinogenic amino acids-an efficient tool to investigate intermediary metabolism. Eur. J. Biochem. 232 (1995) 433-448
    • (1995) Eur. J. Biochem. , vol.232 , pp. 433-448
    • Szyperski, T.1
  • 27
    • 26844493677 scopus 로고    scopus 로고
    • Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glycosyltransferase
    • (Article no. 4)
    • Wang W., Hollmann R., Fürch T., Nimtz M., Malten M., Jahn D., and Deckwer W.-D. Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glycosyltransferase. Proteome Sci. 3 (2005) (Article no. 4)
    • (2005) Proteome Sci. , vol.3
    • Wang, W.1    Hollmann, R.2    Fürch, T.3    Nimtz, M.4    Malten, M.5    Jahn, D.6    Deckwer, W.-D.7
  • 28
    • 33749518241 scopus 로고    scopus 로고
    • Proteomic characterization of transient expression and secretion of a stress-related metalloprotease in high cell density culture of Bacillus megaterium
    • Wang W., Sun J., Hollmann R., Zeng A.-P., and Deckwer W.-D. Proteomic characterization of transient expression and secretion of a stress-related metalloprotease in high cell density culture of Bacillus megaterium. J. Biotechnol. 126 (2006) 313-324
    • (2006) J. Biotechnol. , vol.126 , pp. 313-324
    • Wang, W.1    Sun, J.2    Hollmann, R.3    Zeng, A.-P.4    Deckwer, W.-D.5
  • 29
    • 0036371291 scopus 로고    scopus 로고
    • 13C metabolic flux analysis
    • 13C metabolic flux analysis. Gen. Eng. 24 (2002) 215-238
    • (2002) Gen. Eng. , vol.24 , pp. 215-238
    • Wiechert, W.1
  • 30
    • 0028919496 scopus 로고
    • Inactivation of the major extracellular protease from Bacillus megaterium DSM319 by gene replacement
    • Wittchen K.-D., and Meinhardt F. Inactivation of the major extracellular protease from Bacillus megaterium DSM319 by gene replacement. Appl. Microbiol. Biotechnol. 42 (1995) 871-877
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 871-877
    • Wittchen, K.-D.1    Meinhardt, F.2
  • 31
    • 33845645093 scopus 로고    scopus 로고
    • High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium
    • Yang Y., Biedendieck R., Wang W., Gamer M., Malten M., Jahn D., and Deckwer W.-D. High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium. Microb. Cell Fact. 5 (2006) 36
    • (2006) Microb. Cell Fact. , vol.5 , pp. 36
    • Yang, Y.1    Biedendieck, R.2    Wang, W.3    Gamer, M.4    Malten, M.5    Jahn, D.6    Deckwer, W.-D.7
  • 32
    • 33947178303 scopus 로고    scopus 로고
    • Codon optimized Thermobifida fusca hydrolase secreted by Bacillus megaterium
    • Yang Y., Malten M., Grote A., Jahn D., and Deckwer W.-D. Codon optimized Thermobifida fusca hydrolase secreted by Bacillus megaterium. Biotechnol. Bioeng. 96 (2007) 780-794
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 780-794
    • Yang, Y.1    Malten, M.2    Grote, A.3    Jahn, D.4    Deckwer, W.-D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.