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Volumn 32, Issue , 2015, Pages 23-29

Direct fermentation route for the production of acrylic acid

Author keywords

Acrylic acid; Direct fermentation; E. coli; Glucose

Indexed keywords

CARBOXYLIC ACIDS; CHEMICAL INDUSTRY; CLIMATE CHANGE; ESCHERICHIA COLI; FERMENTATION; GLUCOSE; ORGANIC ACIDS; PETROCHEMICALS;

EID: 84942239426     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2015.08.005     Document Type: Article
Times cited : (44)

References (40)
  • 2
    • 84885458113 scopus 로고    scopus 로고
    • Acrylyl-coenzyme a reductase, an enzyme involved in the assimilation of 3-hydroxypropionate by Rhodobacter sphaeroides
    • Asao M., Alber B.E. Acrylyl-coenzyme a reductase, an enzyme involved in the assimilation of 3-hydroxypropionate by Rhodobacter sphaeroides. J. Bacteriol. 2013, 195:4716-4725.
    • (2013) J. Bacteriol. , vol.195 , pp. 4716-4725
    • Asao, M.1    Alber, B.E.2
  • 3
    • 37249052742 scopus 로고    scopus 로고
    • A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in archaea
    • Berg I.A., Kockelkorn D., Buckel W., Fuchs G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in archaea. Science 2007, 318:1782-1786.
    • (2007) Science , vol.318 , pp. 1782-1786
    • Berg, I.A.1    Kockelkorn, D.2    Buckel, W.3    Fuchs, G.4
  • 4
    • 0019401061 scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans
    • Buckel W., Dorn U., Semmler R. Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur. J. Biochem. 1981, 118:315-321.
    • (1981) Eur. J. Biochem. , vol.118 , pp. 315-321
    • Buckel, W.1    Dorn, U.2    Semmler, R.3
  • 5
    • 84907350970 scopus 로고    scopus 로고
    • Generation of an atlas for commodity chemical production in Escherichia coli and a novel pathway prediction algorithm, GEM-Path
    • Campodonico M.A., Andrews B.A., Asenjo J.A., Palsson B.O., Feist A.M. Generation of an atlas for commodity chemical production in Escherichia coli and a novel pathway prediction algorithm, GEM-Path. Metab. Eng. 2014, 25:140-158.
    • (2014) Metab. Eng. , vol.25 , pp. 140-158
    • Campodonico, M.A.1    Andrews, B.A.2    Asenjo, J.A.3    Palsson, B.O.4    Feist, A.M.5
  • 6
    • 80053459756 scopus 로고    scopus 로고
    • Biotechnological routes based on lactic acid production from biomass
    • Chao G., Cuiqing M., Ping X. Biotechnological routes based on lactic acid production from biomass. Biotechnol. Adv. 2011, 29:930-939.
    • (2011) Biotechnol. Adv. , vol.29 , pp. 930-939
    • Chao, G.1    Cuiqing, M.2    Ping, X.3
  • 7
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov P.P., Wackernagel W. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 1995, 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 8
    • 84923809316 scopus 로고    scopus 로고
    • Biorefineries for the production of top building block chemicals and their derivatives
    • Choi S., Song C.W., Shin J.H., Lee S.Y. Biorefineries for the production of top building block chemicals and their derivatives. Metab. Eng. 2015, 28:223-239.
    • (2015) Metab. Eng. , vol.28 , pp. 223-239
    • Choi, S.1    Song, C.W.2    Shin, J.H.3    Lee, S.Y.4
  • 10
    • 34447129755 scopus 로고    scopus 로고
    • Chemical routes for the transformation of biomass into chemicals
    • Corma A., Iborra S., Velty A. Chemical routes for the transformation of biomass into chemicals. Chem. Rev. 2007, 107:2411-2502.
    • (2007) Chem. Rev. , vol.107 , pp. 2411-2502
    • Corma, A.1    Iborra, S.2    Velty, A.3
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K.A., Wanner B.L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 2000, 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0019887780 scopus 로고
    • Inactivation of hydroxymethylglutaryl-CoA reductase from yeast by coenzyme a disulfide
    • Gilbert H.F., Stewart M.D. Inactivation of hydroxymethylglutaryl-CoA reductase from yeast by coenzyme a disulfide. J. Biol. Chem. 1981, 256(4):1782-1785.
    • (1981) J. Biol. Chem. , vol.256 , Issue.4 , pp. 1782-1785
    • Gilbert, H.F.1    Stewart, M.D.2
  • 14
    • 0029272210 scopus 로고
    • Catalysts and supports for conversion of lactic acid to acrylic acid and 2, 3-pentanedione
    • Gunter G.C., Langford R.H., Jackson J.E., Miller D.J. Catalysts and supports for conversion of lactic acid to acrylic acid and 2, 3-pentanedione. Ind. Eng. Chem. Res. 1995, 34:974-980.
    • (1995) Ind. Eng. Chem. Res. , vol.34 , pp. 974-980
    • Gunter, G.C.1    Langford, R.H.2    Jackson, J.E.3    Miller, D.J.4
  • 15
    • 37049173057 scopus 로고
    • Acid-catalysed hydration of acrylaldehyde: kinetics of the reaction and isolation of β-hydroxypropionaldehyde
    • Hall R.H., Stern E.S. Acid-catalysed hydration of acrylaldehyde: kinetics of the reaction and isolation of β-hydroxypropionaldehyde. J. Chem. Soc. 1950, 490-498.
    • (1950) J. Chem. Soc. , pp. 490-498
    • Hall, R.H.1    Stern, E.S.2
  • 16
    • 0026550360 scopus 로고
    • (R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA
    • Hofmeister A.E., Buckel W. (R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA. Eur. J. Biochem. 1992, 206(2):547-552.
    • (1992) Eur. J. Biochem. , vol.206 , Issue.2 , pp. 547-552
    • Hofmeister, A.E.1    Buckel, W.2
  • 17
    • 0030838035 scopus 로고    scopus 로고
    • Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli
    • Hofmeister A.E., Textor S., Buckel W. Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli. J. Bacteriol. 1997, 179(15):4937-4941.
    • (1997) J. Bacteriol. , vol.179 , Issue.15 , pp. 4937-4941
    • Hofmeister, A.E.1    Textor, S.2    Buckel, W.3
  • 18
    • 3042654769 scopus 로고    scopus 로고
    • Occurrence, biochemistry and possible biotechnological application of the 3-hydroxypropionate cycle
    • Ishii M., Chuakrut S., Arai H., Igarashi Y. Occurrence, biochemistry and possible biotechnological application of the 3-hydroxypropionate cycle. Appl. Microbiol. Biotechnol. 2004, 64:605-610.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 605-610
    • Ishii, M.1    Chuakrut, S.2    Arai, H.3    Igarashi, Y.4
  • 19
    • 78651093186 scopus 로고    scopus 로고
    • YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals
    • Jarboe L.R. yqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals. Appl. Microbiol. Biotechnol. 2011, 89(2):249-257.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , Issue.2 , pp. 249-257
    • Jarboe, L.R.1
  • 20
    • 33847125660 scopus 로고    scopus 로고
    • Fermentative production of lactic acid from biomass: an overview on process developments and future perspectives
    • John R.P., Nampoothiri K.M., Pandey A. Fermentative production of lactic acid from biomass: an overview on process developments and future perspectives. Appl. Microbiol. Biotechnol. 2007, 74:524-534.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 524-534
    • John, R.P.1    Nampoothiri, K.M.2    Pandey, A.3
  • 21
    • 84897412160 scopus 로고    scopus 로고
    • Elevated production of 3-hydroxypropionic acid by metabolic engineering of the glycerol metabolism in Escherichia coli
    • Jung W.S., Kang J.H., Chu H.S., Choi I.S., Cho K.M. Elevated production of 3-hydroxypropionic acid by metabolic engineering of the glycerol metabolism in Escherichia coli. Metab. Eng. 2014, 23:116-122.
    • (2014) Metab. Eng. , vol.23 , pp. 116-122
    • Jung, W.S.1    Kang, J.H.2    Chu, H.S.3    Choi, I.S.4    Cho, K.M.5
  • 24
    • 0027756102 scopus 로고
    • A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae
    • Larsson K., Ansell R., Eriksson P., Adler L. A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae. Mol. Microbiol. 1993, 10(5):1101-1111.
    • (1993) Mol. Microbiol. , vol.10 , Issue.5 , pp. 1101-1111
    • Larsson, K.1    Ansell, R.2    Eriksson, P.3    Adler, L.4
  • 25
    • 0035241925 scopus 로고    scopus 로고
    • Selective oxidation of propane to acrylic acid with molecular oxygen
    • Lin M.M. Selective oxidation of propane to acrylic acid with molecular oxygen. Appl. Catal. A Gen. 2001, 207:1-16.
    • (2001) Appl. Catal. A Gen. , vol.207 , pp. 1-16
    • Lin, M.M.1
  • 27
    • 0028075976 scopus 로고
    • Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans
    • Mack M., Bendrat K., Zelder O., Eckel E., Linder D., Buckel W. Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans. Eur. J. Biochem. 1994, 226:41-51.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 41-51
    • Mack, M.1    Bendrat, K.2    Zelder, O.3    Eckel, E.4    Linder, D.5    Buckel, W.6
  • 28
    • 0029920291 scopus 로고    scopus 로고
    • Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway
    • Norbeck J., Pâhlman A.K., Akhtar N., Blomberg A., Adler L. Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 1996, 271(23):13875-13881.
    • (1996) J. Biol. Chem. , vol.271 , Issue.23 , pp. 13875-13881
    • Norbeck, J.1    Pâhlman, A.K.2    Akhtar, N.3    Blomberg, A.4    Adler, L.5
  • 29
    • 2342579992 scopus 로고    scopus 로고
    • Future feedstocks for commodity polymers: EcotheneTM - Sustainability in the 21st century
    • Presentation at Utrecht University.
    • Nossin, P., Joosten, J., Bruggink, A., 2002. Future feedstocks for commodity polymers: EcotheneTM - Sustainability in the 21st century. Presentation at Utrecht University.
    • (2002)
    • Nossin, P.1    Joosten, J.2    Bruggink, A.3
  • 30
    • 0025464913 scopus 로고
    • Biological production of acrylic acid from cheese whey by resting cells of Clostridium propionicum
    • O'Brien D.J., Panzer C.C., Eisele W.P. Biological production of acrylic acid from cheese whey by resting cells of Clostridium propionicum. Biotechnol. Prog. 1990, 6:237-242.
    • (1990) Biotechnol. Prog. , vol.6 , pp. 237-242
    • O'Brien, D.J.1    Panzer, C.C.2    Eisele, W.P.3
  • 31
    • 26444466741 scopus 로고    scopus 로고
    • Chromosomal duplications and cointegrates generated by the bacteriophage lamdba Red system in Escherichia coli K-12
    • Poteete A.R., Fenton A.C., Nadkarni A. Chromosomal duplications and cointegrates generated by the bacteriophage lamdba Red system in Escherichia coli K-12. BMC Mol. Biol. 2004, 5:22.
    • (2004) BMC Mol. Biol. , vol.5 , pp. 22
    • Poteete, A.R.1    Fenton, A.C.2    Nadkarni, A.3
  • 32
    • 70350497694 scopus 로고    scopus 로고
    • Development and evaluation of efficient recombinant Escherichia coli strains for the production of 3-hydroxypropionic acid from glycerol
    • Rathnasingh C., Raj S.M., Jo J., Park S.H. Development and evaluation of efficient recombinant Escherichia coli strains for the production of 3-hydroxypropionic acid from glycerol. Biotechnol. Bioeng. 2009, 104:729-739.
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 729-739
    • Rathnasingh, C.1    Raj, S.M.2    Jo, J.3    Park, S.H.4
  • 36
    • 67650302869 scopus 로고    scopus 로고
    • 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales
    • Teufel R., Kung J.W., Kockelkorn D., Alber B.E., Fuchs G. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J. Bacteriol. 2009, 191(14):4572-4581.
    • (2009) J. Bacteriol. , vol.191 , Issue.14 , pp. 4572-4581
    • Teufel, R.1    Kung, J.W.2    Kockelkorn, D.3    Alber, B.E.4    Fuchs, G.5
  • 37
    • 84862160176 scopus 로고    scopus 로고
    • Involvement of the AtoSCDAEB regulon in the high molecular weight poly-(R)-3-hydroxybutyrate biosynthesis in phaCAB+ Escherichia coli
    • Theodorou E.C., Theodorou M.C., Kyriakidis D.A. Involvement of the AtoSCDAEB regulon in the high molecular weight poly-(R)-3-hydroxybutyrate biosynthesis in phaCAB+ Escherichia coli. Metab. Eng. 2012, 14:354-365.
    • (2012) Metab. Eng. , vol.14 , pp. 354-365
    • Theodorou, E.C.1    Theodorou, M.C.2    Kyriakidis, D.A.3
  • 39
    • 28444491504 scopus 로고    scopus 로고
    • Enhancement of lactate and succinate formation in adhE or pta-ackA mutants of NADH dehydrogenase-deficient Escherichia coli
    • Yun N.R., San K.Y., Bennett G.N. Enhancement of lactate and succinate formation in adhE or pta-ackA mutants of NADH dehydrogenase-deficient Escherichia coli. J. Appl. Microbiol. 2005, 99:1404-1412.
    • (2005) J. Appl. Microbiol. , vol.99 , pp. 1404-1412
    • Yun, N.R.1    San, K.Y.2    Bennett, G.N.3
  • 40
    • 80555130923 scopus 로고    scopus 로고
    • Production of 3-hydroxypropionate homopolymer and poly(3-hydroxypropionate-co-4-hydroxybutyrate) copolymer by recombinant Escherichia coli
    • Zhou Q., Shi Z.Y., Meng D.C., Wu Q., Chen J.C., Chen G.Q. Production of 3-hydroxypropionate homopolymer and poly(3-hydroxypropionate-co-4-hydroxybutyrate) copolymer by recombinant Escherichia coli. Metab. Eng. 2011, 13:777-785.
    • (2011) Metab. Eng. , vol.13 , pp. 777-785
    • Zhou, Q.1    Shi, Z.Y.2    Meng, D.C.3    Wu, Q.4    Chen, J.C.5    Chen, G.Q.6


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