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Volumn 26, Issue , 2014, Pages 50-55

Renewable jet fuel

Author keywords

[No Author keywords available]

Indexed keywords

APPLIED SCIENCE; COMMERCIAL APPLICATIONS; FUNDAMENTAL RESEARCH; MICROBIAL BIOSYNTHESIS; MICROBIAL BIOTECHNOLOGY; NOVEL STRATEGIES; PISTON ENGINES;

EID: 84884920437     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2013.09.006     Document Type: Review
Times cited : (115)

References (40)
  • 1
    • 84884925125 scopus 로고    scopus 로고
    • Platts I: Fuel Price Analysis. IATA
    • Platts I: Fuel Price Analysis. IATA: http://www.iata.org/publications/economics/fuel-monitor/Pages/price-analysis.aspx.
  • 2
    • 0035864935 scopus 로고    scopus 로고
    • Advanced aviation fuels: a look ahead via a historical perspective
    • Maurice L.Q., Lander H., Edwards T., Harrison W.E. Advanced aviation fuels: a look ahead via a historical perspective. Fuels 2001, 80:747-756.
    • (2001) Fuels , vol.80 , pp. 747-756
    • Maurice, L.Q.1    Lander, H.2    Edwards, T.3    Harrison, W.E.4
  • 7
    • 79959363472 scopus 로고    scopus 로고
    • Comprehensive two-dimensional gas chromatography for the analysis of synthetic and crude-derived jet fuels
    • van der Westhuizen R., Ajam M., De Coning P., Beens J., de Villiers A., Sandra P. Comprehensive two-dimensional gas chromatography for the analysis of synthetic and crude-derived jet fuels. J Chromatogr A 2011, 1218:4478-4486.
    • (2011) J Chromatogr A , vol.1218 , pp. 4478-4486
    • van der Westhuizen, R.1    Ajam, M.2    De Coning, P.3    Beens, J.4    de Villiers, A.5    Sandra, P.6
  • 8
    • 84867022890 scopus 로고    scopus 로고
    • Alternative biofuel production in non-natural hosts
    • McEwen J.T., Atsumi S. Alternative biofuel production in non-natural hosts. Curr Opin Biotechnol 2012, 23:744-750.
    • (2012) Curr Opin Biotechnol , vol.23 , pp. 744-750
    • McEwen, J.T.1    Atsumi, S.2
  • 10
  • 11
    • 84859950774 scopus 로고    scopus 로고
    • ATP drives direct photosynthetic production of 1-butanol in cyanobacteria
    • Lan E.I., Liao J.C. ATP drives direct photosynthetic production of 1-butanol in cyanobacteria. Proc Natl Acad Sci U S A 2012, 109:6018-6023.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6018-6023
    • Lan, E.I.1    Liao, J.C.2
  • 14
    • 84869465095 scopus 로고    scopus 로고
    • From fields to fuels: recent advances in the microbial production of biofuels
    • Kung Y., Runguphan W., Keasling J.D. From fields to fuels: recent advances in the microbial production of biofuels. ACS Synth Biol 2012, 1:498-513.
    • (2012) ACS Synth Biol , vol.1 , pp. 498-513
    • Kung, Y.1    Runguphan, W.2    Keasling, J.D.3
  • 16
    • 77955481009 scopus 로고    scopus 로고
    • Current understanding of fatty acid biosynthesis and the acyl carrier protein
    • Chan D.I., Vogel H.J. Current understanding of fatty acid biosynthesis and the acyl carrier protein. Biochem J 2010, 430:1-19.
    • (2010) Biochem J , vol.430 , pp. 1-19
    • Chan, D.I.1    Vogel, H.J.2
  • 17
    • 0028960890 scopus 로고
    • Defective export of a periplasmic enzyme disrupts regulation of fatty acid synthesis
    • Cho H., Cronan J.E. Defective export of a periplasmic enzyme disrupts regulation of fatty acid synthesis. J Biol Chem 1995, 270:4216-4219.
    • (1995) J Biol Chem , vol.270 , pp. 4216-4219
    • Cho, H.1    Cronan, J.E.2
  • 18
    • 77953022686 scopus 로고    scopus 로고
    • Quantitative analysis and engineering of fatty acid biosynthesis in E. coli
    • Liu T., Vora H., Khosla C. Quantitative analysis and engineering of fatty acid biosynthesis in E. coli. Metab Eng 2010, 12:378-386.
    • (2010) Metab Eng , vol.12 , pp. 378-386
    • Liu, T.1    Vora, H.2    Khosla, C.3
  • 19
    • 81155158878 scopus 로고    scopus 로고
    • Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity
    • Jing F., Cantu D.C., Tvaruzkova J., Chipman J.P., Nikolau B.J., Yandeau-Nelson M.D., Reilly P.J. Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity. BMC Biochem 2011, 12:44.
    • (2011) BMC Biochem , vol.12 , pp. 44
    • Jing, F.1    Cantu, D.C.2    Tvaruzkova, J.3    Chipman, J.P.4    Nikolau, B.J.5    Yandeau-Nelson, M.D.6    Reilly, P.J.7
  • 20
    • 0021753756 scopus 로고
    • Fatty acid synthesis in mitochondria of Euglena gracilis
    • Inui H., Miyatake K., Nakano Y., Kitaoka S. Fatty acid synthesis in mitochondria of Euglena gracilis. Eur J Biochem 1984, 142:121-126.
    • (1984) Eur J Biochem , vol.142 , pp. 121-126
    • Inui, H.1    Miyatake, K.2    Nakano, Y.3    Kitaoka, S.4
  • 21
    • 80051941601 scopus 로고    scopus 로고
    • Engineered reversal of the β-oxidation cycle for the synthesis of fuels and chemicals
    • Dellomonaco C., Clomburg J.M., Miller E.N., Gonzalez R. Engineered reversal of the β-oxidation cycle for the synthesis of fuels and chemicals. Nature 2011, 476:355-359.
    • (2011) Nature , vol.476 , pp. 355-359
    • Dellomonaco, C.1    Clomburg, J.M.2    Miller, E.N.3    Gonzalez, R.4
  • 22
    • 79953307747 scopus 로고    scopus 로고
    • Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins
    • Krebs C., Bollinger J.M., Booker S.J. Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins. Curr Opin Chem Biol 2011, 15:291-303.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 291-303
    • Krebs, C.1    Bollinger, J.M.2    Booker, S.J.3
  • 24
    • 79960638391 scopus 로고    scopus 로고
    • Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes
    • Das D., Eser B.E., Han J., Sciore A., Marsh E.N. Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes. Angew Chem Int Ed Engl 2011, 50:7148-7152.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 7148-7152
    • Das, D.1    Eser, B.E.2    Han, J.3    Sciore, A.4    Marsh, E.N.5
  • 25
    • 82955240582 scopus 로고    scopus 로고
    • Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor
    • Eser B.E., Das D., Han J., Jones P.R., Marsh E.N. Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor. Biochemistry 2011, 50:10743-10750.
    • (2011) Biochemistry , vol.50 , pp. 10743-10750
    • Eser, B.E.1    Das, D.2    Han, J.3    Jones, P.R.4    Marsh, E.N.5
  • 26
    • 84867482224 scopus 로고    scopus 로고
    • Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases
    • Li N., Chang W.C., Warui D.M., Booker S.J., Krebs C., Bollinger J.M. Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases. Biochemistry 2012, 51:7908-7916.
    • (2012) Biochemistry , vol.51 , pp. 7908-7916
    • Li, N.1    Chang, W.C.2    Warui, D.M.3    Booker, S.J.4    Krebs, C.5    Bollinger, J.M.6
  • 27
    • 84876063529 scopus 로고    scopus 로고
    • Probing the mechanism of cyanobacterial aldehyde decarbonylase using a cyclopropyl aldehyde
    • Paul B., Das D., Ellington B., Marsh E.N. Probing the mechanism of cyanobacterial aldehyde decarbonylase using a cyclopropyl aldehyde. J Am Chem Soc 2013, 135:5234-5237.
    • (2013) J Am Chem Soc , vol.135 , pp. 5234-5237
    • Paul, B.1    Das, D.2    Ellington, B.3    Marsh, E.N.4
  • 28
    • 79954995511 scopus 로고    scopus 로고
    • Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase
    • Li N., Nørgaard H., Warui D.M., Booker S.J., Krebs C., Bollinger J.M. Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase. J Am Chem Soc 2011, 133:6158-6161.
    • (2011) J Am Chem Soc , vol.133 , pp. 6158-6161
    • Li, N.1    Nørgaard, H.2    Warui, D.M.3    Booker, S.J.4    Krebs, C.5    Bollinger, J.M.6
  • 29
    • 79952588441 scopus 로고    scopus 로고
    • Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase
    • Warui D.M., Li N., Nørgaard H., Krebs C., Bollinger J.M., Booker S.J. Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase. J Am Chem Soc 2011, 133:3316-3319.
    • (2011) J Am Chem Soc , vol.133 , pp. 3316-3319
    • Warui, D.M.1    Li, N.2    Nørgaard, H.3    Krebs, C.4    Bollinger, J.M.5    Booker, S.J.6
  • 30
    • 84879829539 scopus 로고    scopus 로고
    • Production of propane and other short-chain alkanes by structure-based engineering of ligand specificity in aldehyde-deformylating oxygenase
    • Khara B., Menon N., Levy C., Mansell D., Das D., Marsh E.N., Leys D., Scrutton N.S. Production of propane and other short-chain alkanes by structure-based engineering of ligand specificity in aldehyde-deformylating oxygenase. Chembiochem 2013, 14:1204-1208.
    • (2013) Chembiochem , vol.14 , pp. 1204-1208
    • Khara, B.1    Menon, N.2    Levy, C.3    Mansell, D.4    Das, D.5    Marsh, E.N.6    Leys, D.7    Scrutton, N.S.8
  • 31
    • 84871952399 scopus 로고    scopus 로고
    • Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities
    • Akhtar M.K., Turner N.J., Jones P.R. Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities. Proc Natl Acad Sci U S A 2013, 110:87-92.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 87-92
    • Akhtar, M.K.1    Turner, N.J.2    Jones, P.R.3
  • 33
    • 84862601628 scopus 로고    scopus 로고
    • Isobutyraldehyde production from Escherichia coli by removing aldehyde reductase activity
    • Rodriguez G.M., Atsumi S. Isobutyraldehyde production from Escherichia coli by removing aldehyde reductase activity. Microb Cell Fact 2012, 11:90.
    • (2012) Microb Cell Fact , vol.11 , pp. 90
    • Rodriguez, G.M.1    Atsumi, S.2
  • 35
    • 0015240460 scopus 로고
    • The generation of superoixide radical during the autoxidation of ferredoxins
    • Misra H.P., Fridovich I. The generation of superoixide radical during the autoxidation of ferredoxins. J Biol Chem 1971, 246:6886-6890.
    • (1971) J Biol Chem , vol.246 , pp. 6886-6890
    • Misra, H.P.1    Fridovich, I.2
  • 38
    • 0033986294 scopus 로고    scopus 로고
    • Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis
    • Choi K.H., Heath R.J., Rock C.O. Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis. J Bacteriol 2000, 182:365-370.
    • (2000) J Bacteriol , vol.182 , pp. 365-370
    • Choi, K.H.1    Heath, R.J.2    Rock, C.O.3
  • 39
    • 0021271149 scopus 로고
    • Cloning and manipulation of the Escherichia coli cyclopropane fatty acid synthase gene: physiological aspects of enzyme overproduction
    • Grogan D.W., Cronan J.E. Cloning and manipulation of the Escherichia coli cyclopropane fatty acid synthase gene: physiological aspects of enzyme overproduction. J Bacteriol 1984, 158:286-295.
    • (1984) J Bacteriol , vol.158 , pp. 286-295
    • Grogan, D.W.1    Cronan, J.E.2
  • 40
    • 0030064049 scopus 로고    scopus 로고
    • Modification of the fatty acid composition of Escherichia coli by coexpression of a plant acyl-acyl carrier protein desaturase and ferredoxin
    • Cahoon E.B., Mills L.A., Shanklin J. Modification of the fatty acid composition of Escherichia coli by coexpression of a plant acyl-acyl carrier protein desaturase and ferredoxin. J Bacteriol 1996, 178:936-939.
    • (1996) J Bacteriol , vol.178 , pp. 936-939
    • Cahoon, E.B.1    Mills, L.A.2    Shanklin, J.3


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