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Volumn 19, Issue 5, 2008, Pages 414-419

Metabolic engineering for advanced biofuels production from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; ETHANOL; FUELS; HYDROSTATIC PRESSURE; TECHNOLOGY; VAPOR PRESSURE;

EID: 53049083876     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2008.08.008     Document Type: Review
Times cited : (258)

References (27)
  • 1
    • 33748762752 scopus 로고    scopus 로고
    • Microdiesel: Escherichia coli engineered for fuel production
    • This study demonstrates that ethanol can be esterified to a fatty acid in E. coli, which provides significant possibility for a whole-cell catalyst for the production of biodiesel.
    • Kalscheuer R., Stolting T., and Steinbuchel A. Microdiesel: Escherichia coli engineered for fuel production. Microbiology 152 (2006) 2529-2536. This study demonstrates that ethanol can be esterified to a fatty acid in E. coli, which provides significant possibility for a whole-cell catalyst for the production of biodiesel.
    • (2006) Microbiology , vol.152 , pp. 2529-2536
    • Kalscheuer, R.1    Stolting, T.2    Steinbuchel, A.3
  • 2
    • 37349093415 scopus 로고    scopus 로고
    • Engineered synthetic pathway for isopropanol production in Escherichia coli
    • This paper demonstrates isopropanol production from E. coli by expressing various combinations of genes from C. acetobutylicum ATCC 824, E. coli K-12 MG1655, C. beijerinckii NRRL B593, and T. brockii HTD4. The isopropanol production from E. coli is higher than those produced by C. acetobutylicum.
    • Hanai T., Atsumi S., and Liao J.C. Engineered synthetic pathway for isopropanol production in Escherichia coli. Appl Environ Microbiol 73 (2007) 7814-7818. This paper demonstrates isopropanol production from E. coli by expressing various combinations of genes from C. acetobutylicum ATCC 824, E. coli K-12 MG1655, C. beijerinckii NRRL B593, and T. brockii HTD4. The isopropanol production from E. coli is higher than those produced by C. acetobutylicum.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7814-7818
    • Hanai, T.1    Atsumi, S.2    Liao, J.C.3
  • 3
    • 35148889024 scopus 로고    scopus 로고
    • Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity
    • The authors developed a screening method to isolate isoprenoid biosynthetic genes. With this method, two terpene synthase genes are cloned from the isoprene-producing bacterium Bacillus subtilis strain 6051.
    • Withers S.T., Gottlieb S.S., Lieu B., Newman J.D., and Keasling J.D. Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity. Appl Environ Microbiol 73 (2007) 6277-6283. The authors developed a screening method to isolate isoprenoid biosynthetic genes. With this method, two terpene synthase genes are cloned from the isoprene-producing bacterium Bacillus subtilis strain 6051.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6277-6283
    • Withers, S.T.1    Gottlieb, S.S.2    Lieu, B.3    Newman, J.D.4    Keasling, J.D.5
  • 4
    • 38049001166 scopus 로고    scopus 로고
    • Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels
    • This paper presents a metabolic engineering approach using E. coli to produce higher alcohols including isobutanol, n-butanol, 2-methyl-1-butanol, and 3-methyl-1-butanol from glucose, a renewable carbon source. This strategy uses the host's amino acid biosynthetic pathway and diverts its 2-ketoacid intermediates for alcohol synthesis.
    • Atsumi S., Hanai T., and Liao J.C. Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels. Nature 451 (2008) 86-89. This paper presents a metabolic engineering approach using E. coli to produce higher alcohols including isobutanol, n-butanol, 2-methyl-1-butanol, and 3-methyl-1-butanol from glucose, a renewable carbon source. This strategy uses the host's amino acid biosynthetic pathway and diverts its 2-ketoacid intermediates for alcohol synthesis.
    • (2008) Nature , vol.451 , pp. 86-89
    • Atsumi, S.1    Hanai, T.2    Liao, J.C.3
  • 5
    • 53049097710 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for 1-butanol production
    • 10.1016/j.ymben.2007.08.003. Clostridium is a natural producer of n-butanol. However, the relatively unknown genetic system and complex physiology of Clostridium present difficulties in engineering its metabolism for optimal production of n-butanol. To deal with these problems, the authors engineered a synthetic pathway in E. coli and demonstrated the production of 1-butanol from this non-native user-friendly host.
    • Atsumi S., Cann A.F., Connor M.R., Shen C.R., Smith K.M., Brynildsen M.P., Chou K.J., Hanai T., and Liao J.C. Metabolic engineering of Escherichia coli for 1-butanol production. Metab Eng (2008) 10.1016/j.ymben.2007.08.003. Clostridium is a natural producer of n-butanol. However, the relatively unknown genetic system and complex physiology of Clostridium present difficulties in engineering its metabolism for optimal production of n-butanol. To deal with these problems, the authors engineered a synthetic pathway in E. coli and demonstrated the production of 1-butanol from this non-native user-friendly host.
    • (2008) Metab Eng
    • Atsumi, S.1    Cann, A.F.2    Connor, M.R.3    Shen, C.R.4    Smith, K.M.5    Brynildsen, M.P.6    Chou, K.J.7    Hanai, T.8    Liao, J.C.9
  • 6
    • 0020678924 scopus 로고
    • Butanol production by a butanol-tolerant strain of Clostridium acetobutylicum in extruded corn broth
    • Lin Y.L., and Blaschek H.P. Butanol production by a butanol-tolerant strain of Clostridium acetobutylicum in extruded corn broth. Appl Environ Microbiol 45 (1983) 966-973
    • (1983) Appl Environ Microbiol , vol.45 , pp. 966-973
    • Lin, Y.L.1    Blaschek, H.P.2
  • 7
    • 0022970603 scopus 로고
    • Acetone-butanol fermentation revisited
    • Jones D.T., and Woods D.R. Acetone-butanol fermentation revisited. Microbiol Rev 50 (1986) 484-524
    • (1986) Microbiol Rev , vol.50 , pp. 484-524
    • Jones, D.T.1    Woods, D.R.2
  • 8
    • 0342809224 scopus 로고
    • The butyl alcohol-isopropyl alcohol fermentation
    • Osburn O.L., Brown R.W., and Werkman C.H. The butyl alcohol-isopropyl alcohol fermentation. J Biol Chem 121 (1937) 685-695
    • (1937) J Biol Chem , vol.121 , pp. 685-695
    • Osburn, O.L.1    Brown, R.W.2    Werkman, C.H.3
  • 9
    • 0343365512 scopus 로고
    • Acetone-butanol-isopropanol production by Clostridium beijerinckii (synonym, Clostridium butylicum)
    • Chen J.S., and Hiu S.F. Acetone-butanol-isopropanol production by Clostridium beijerinckii (synonym, Clostridium butylicum). Biotechnol Lett 8 (1986) 371-376
    • (1986) Biotechnol Lett , vol.8 , pp. 371-376
    • Chen, J.S.1    Hiu, S.F.2
  • 10
    • 0031886572 scopus 로고    scopus 로고
    • Expression of Clostridium acetobutylicum ATCC 824 genes in Escherichia coli for acetone production and acetate detoxification
    • Bermejo L.L., Welker N.E., and Papoutsakis E.T. Expression of Clostridium acetobutylicum ATCC 824 genes in Escherichia coli for acetone production and acetate detoxification. Appl Environ Microbiol 64 (1998) 1079-1085
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1079-1085
    • Bermejo, L.L.1    Welker, N.E.2    Papoutsakis, E.T.3
  • 11
    • 0031208319 scopus 로고    scopus 로고
    • Molecular cloning, nucleotide sequencing, and expression of genes encoding alcohol dehydrogenases from the thermophile Thermoanaerobacter brockii and the mesophile Clostridium beijerinckii
    • Peretz M., Bogin O., Tel-Or S., Cohen A., Li G., Chen J.S., and Burstein Y. Molecular cloning, nucleotide sequencing, and expression of genes encoding alcohol dehydrogenases from the thermophile Thermoanaerobacter brockii and the mesophile Clostridium beijerinckii. Anaerobe 3 (1997) 259-270
    • (1997) Anaerobe , vol.3 , pp. 259-270
    • Peretz, M.1    Bogin, O.2    Tel-Or, S.3    Cohen, A.4    Li, G.5    Chen, J.S.6    Burstein, Y.7
  • 12
    • 0017125173 scopus 로고
    • Molecular and catalytic properties of the acetoacetyl-coenzyme A thiolase of Escherichia coli
    • Duncombe G.R., and Frerman F.E. Molecular and catalytic properties of the acetoacetyl-coenzyme A thiolase of Escherichia coli. Arch Biochem Biophys 176 (1976) 159-170
    • (1976) Arch Biochem Biophys , vol.176 , pp. 159-170
    • Duncombe, G.R.1    Frerman, F.E.2
  • 13
    • 0023089497 scopus 로고
    • Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system
    • Jenkins L.S., and Nunn W.D. Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system. J Bacteriol 169 (1987) 42-52
    • (1987) J Bacteriol , vol.169 , pp. 42-52
    • Jenkins, L.S.1    Nunn, W.D.2
  • 14
    • 0027317888 scopus 로고
    • Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii
    • Ismaiel A.A., Zhu C.X., Colby G.D., and Chen J.S. Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii. J Bacteriol 175 (1993) 5097-5105
    • (1993) J Bacteriol , vol.175 , pp. 5097-5105
    • Ismaiel, A.A.1    Zhu, C.X.2    Colby, G.D.3    Chen, J.S.4
  • 15
    • 0019554401 scopus 로고
    • Novel NADP-linked alcohol-aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria
    • Lamed R.J., and Zeikus J.G. Novel NADP-linked alcohol-aldehyde/ketone oxidoreductase in thermophilic ethanologenic bacteria. Biochem J 195 (1981) 183-190
    • (1981) Biochem J , vol.195 , pp. 183-190
    • Lamed, R.J.1    Zeikus, J.G.2
  • 16
    • 0029762151 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of genes encoding phosphotransacetylase and acetate kinase from Clostridium acetobutylicum ATCC 824
    • Boynton Z.L., Bennett G.N., and Rudolph F.B. Cloning, sequencing, and expression of genes encoding phosphotransacetylase and acetate kinase from Clostridium acetobutylicum ATCC 824. Appl Environ Microbiol 62 (1996) 2758-2766
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2758-2766
    • Boynton, Z.L.1    Bennett, G.N.2    Rudolph, F.B.3
  • 17
    • 0036180998 scopus 로고    scopus 로고
    • Molecular characterization and transcriptional analysis of adhE2, the gene encoding the NADH-dependent aldehyde/alcohol dehydrogenase responsible for butanol production in alcohologenic cultures of Clostridium acetobutylicum ATCC 824
    • Fontaine L., Meynial-Salles I., Girbal L., Yang X., Croux C., and Soucaille P. Molecular characterization and transcriptional analysis of adhE2, the gene encoding the NADH-dependent aldehyde/alcohol dehydrogenase responsible for butanol production in alcohologenic cultures of Clostridium acetobutylicum ATCC 824. J Bacteriol 184 (2002) 821-830
    • (2002) J Bacteriol , vol.184 , pp. 821-830
    • Fontaine, L.1    Meynial-Salles, I.2    Girbal, L.3    Yang, X.4    Croux, C.5    Soucaille, P.6
  • 18
    • 0000158375 scopus 로고
    • Thiolase from Clostridium acetobutylicum ATCC 824 and its role in the synthesis of acids and solvents
    • Wiesenborn D.P., Rudolph F.B., and Papoutsakis E.T. Thiolase from Clostridium acetobutylicum ATCC 824 and its role in the synthesis of acids and solvents. Appl Environ Microbiol 54 (1988) 2717-2722
    • (1988) Appl Environ Microbiol , vol.54 , pp. 2717-2722
    • Wiesenborn, D.P.1    Rudolph, F.B.2    Papoutsakis, E.T.3
  • 19
    • 0027444637 scopus 로고
    • Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii
    • Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., MacGillivray R.T., and Stankovich M.T. Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii. Biochemistry 32 (1993) 10736-10742
    • (1993) Biochemistry , vol.32 , pp. 10736-10742
    • Becker, D.F.1    Fuchs, J.A.2    Banfield, D.K.3    Funk, W.D.4    MacGillivray, R.T.5    Stankovich, M.T.6
  • 20
    • 0032516906 scopus 로고    scopus 로고
    • Cloning and analysis of the genes for a novel electron-transferring flavoprotein from Megasphaera elsdenii. Expression and characterization of the recombinant protein
    • O'Neill H., Mayhew S.G., and Butler G. Cloning and analysis of the genes for a novel electron-transferring flavoprotein from Megasphaera elsdenii. Expression and characterization of the recombinant protein. J Biol Chem 273 (1998) 21015-21024
    • (1998) J Biol Chem , vol.273 , pp. 21015-21024
    • O'Neill, H.1    Mayhew, S.G.2    Butler, G.3
  • 21
    • 0028808264 scopus 로고
    • Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli
    • Wallace K.K., Bao Z.Y., Dai H., Digate R., Schuler G., Speedie M.K., and Reynolds K.A. Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. Eur J Biochem 233 (1995) 954-962
    • (1995) Eur J Biochem , vol.233 , pp. 954-962
    • Wallace, K.K.1    Bao, Z.Y.2    Dai, H.3    Digate, R.4    Schuler, G.5    Speedie, M.K.6    Reynolds, K.A.7
  • 22
    • 0001438133 scopus 로고
    • The mechanism of the formation of higher alcohols from amino acids by Saccharomyces cerevisiae
    • Sentheshanuganathan S. The mechanism of the formation of higher alcohols from amino acids by Saccharomyces cerevisiae. Biochem J 74 (1960) 568-576
    • (1960) Biochem J , vol.74 , pp. 568-576
    • Sentheshanuganathan, S.1
  • 23
    • 4444266764 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of alpha-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis
    • de la Plaza M., Fernandez de Palencia P., Pelaez C., and Requena T. Biochemical and molecular characterization of alpha-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids by Lactococcus lactis. FEMS Microbiol Lett 238 (2004) 367-374
    • (2004) FEMS Microbiol Lett , vol.238 , pp. 367-374
    • de la Plaza, M.1    Fernandez de Palencia, P.2    Pelaez, C.3    Requena, T.4
  • 24
    • 0017172034 scopus 로고
    • Biosynthesis of norvaline, norleucine, and homoisoleucine in Serratia marcescens
    • Kisumi M., Sugiura M., and Chibata I. Biosynthesis of norvaline, norleucine, and homoisoleucine in Serratia marcescens. J Biochem 80 (1976) 333-339
    • (1976) J Biochem , vol.80 , pp. 333-339
    • Kisumi, M.1    Sugiura, M.2    Chibata, I.3
  • 25
    • 0042772962 scopus 로고
    • Construction of l-threonine overproducing strains of Escherichia coli K-12 using recombinant
    • Miwa K., Tsuchida T., Kurahashi O., Nakamori S., Sano K., and Momose H. Construction of l-threonine overproducing strains of Escherichia coli K-12 using recombinant. Agric Biol Chem 47 (1983) 2329-2334
    • (1983) Agric Biol Chem , vol.47 , pp. 2329-2334
    • Miwa, K.1    Tsuchida, T.2    Kurahashi, O.3    Nakamori, S.4    Sano, K.5    Momose, H.6
  • 27
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini J.C., and Poulter C.D. Creating isoprenoid diversity. Science 277 (1997) 1788-1789
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2


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