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Volumn 47, Issue 7, 2012, Pages 1135-1143

Aldehyde dehydrogenase activity is important to the production of 3-hydroxypropionic acid from glycerol by recombinant Klebsiella pneumoniae

Author keywords

3 Hydroxypropionic acid; Aldehyde dehydrogenase; Glycerol; Klebsiella pneumoniae

Indexed keywords

1 ,3 PROPANEDIOL; 3-HYDROXYPROPIONALDEHYDE (3-HPA); 3-HYDROXYPROPIONIC ACID; ALDEHYDE DEHYDROGENASE; AZOSPIRILLUM BRASILENSE; CARBON FLUXES; CARBON YIELD; CELL ACTIVITY; ENZYMATIC REACTION; FED-BATCH BIOREACTORS; FLASK CULTURE; GENES ENCODING; GLYCEROL DEHYDRATASE; HOST STRAIN; KLEBSIELLA PNEUMONIAE; OVERALL RATE; PNEUMONIAE STRAINS; RECOMBINANT STRAINS; WILD TYPES;

EID: 84861331076     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2012.04.007     Document Type: Article
Times cited : (57)

References (33)
  • 2
    • 54949113283 scopus 로고    scopus 로고
    • Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain
    • S.M. Raj, C. Rathnasingh, J.E. Jo, and S.H. Park Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain Process Biochem 43 2008 1440 1446
    • (2008) Process Biochem , vol.43 , pp. 1440-1446
    • Raj, S.M.1    Rathnasingh, C.2    Jo, J.E.3    Park, S.H.4
  • 3
    • 54349128839 scopus 로고    scopus 로고
    • Cloning expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-hydroxypropionaldehyde as a substrate
    • J.E. Jo, S.M. Raj, C. Rathnasingh, E. Selvakumar, W.C. Jung, and S.H. Park Cloning expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-hydroxypropionaldehyde as a substrate Appl Microbiol Biotechnol 81 2008 51 60
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 51-60
    • Jo, J.E.1    Raj, S.M.2    Rathnasingh, C.3    Selvakumar, E.4    Jung, W.C.5    Park, S.H.6
  • 4
    • 69949118104 scopus 로고    scopus 로고
    • Effect of process parameters on 3-hydroxypropionic acid production from glycerol using a recombinant Escherichia coli
    • S.M. Raj, C. Rathnasingh, W.C. Jung, and S.H. Park Effect of process parameters on 3-hydroxypropionic acid production from glycerol using a recombinant Escherichia coli Appl Microbiol Biotechnol 84 2009 649 657
    • (2009) Appl Microbiol Biotechnol , vol.84 , pp. 649-657
    • Raj, S.M.1    Rathnasingh, C.2    Jung, W.C.3    Park, S.H.4
  • 5
    • 70350497694 scopus 로고    scopus 로고
    • Development and evaluation of efficient recombinant Escherichia coli strains for the production of 3-hydroxypropionic acid from glycerol
    • C. Rathnasingh, S.M. Raj, J.E. Jo, and S.H. Park Development and evaluation of efficient recombinant Escherichia coli strains for the production of 3-hydroxypropionic acid from glycerol Biotechnol Bioeng 104 2009 729 739
    • (2009) Biotechnol Bioeng , vol.104 , pp. 729-739
    • Rathnasingh, C.1    Raj, S.M.2    Jo, J.E.3    Park, S.H.4
  • 6
    • 0028181877 scopus 로고
    • 12 production by Citrobacter freundii or Klebsiella pneumoniae during tempeh fermentation and proof of enterotoxin absence by PCR
    • 12 production by Citrobacter freundii or Klebsiella pneumoniae during tempeh fermentation and proof of enterotoxin absence by PCR Appl Environ Microbiol 60 1994 1495 1499
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1495-1499
    • Keuth, S.1    Bisping, B.2
  • 7
    • 0017243175 scopus 로고
    • Glycerol dissimilation and its regulation in bacteria
    • E.C. Lin Glycerol dissimilation and its regulation in bacteria Annu Rev Microbiol 30 1976 535 578
    • (1976) Annu Rev Microbiol , vol.30 , pp. 535-578
    • Lin, E.C.1
  • 9
    • 70349985735 scopus 로고    scopus 로고
    • Microbial production of 1,3-propanediol: Recent developments and emerging opportunities
    • R.K. Saxena, P. Anand, S. Saran, and J. Isar Microbial production of 1,3-propanediol: recent developments and emerging opportunities Biotechnol Adv 27 2009 895 913
    • (2009) Biotechnol Adv , vol.27 , pp. 895-913
    • Saxena, R.K.1    Anand, P.2    Saran, S.3    Isar, J.4
  • 10
    • 77953558759 scopus 로고    scopus 로고
    • +-dependent aldehyde dehydrogenase encoded by the puuC gene of Klebsiella pneumoniae DSM 2026 that utilizes 3- hydroxypropionaldehyde as a substrate
    • +-dependent aldehyde dehydrogenase encoded by the puuC gene of Klebsiella pneumoniae DSM 2026 that utilizes 3-hydroxypropionaldehyde as a substrate Biotechnol Bioprocess Eng 15 2010 131 138
    • (2010) Biotechnol Bioprocess Eng , vol.15 , pp. 131-138
    • Raj, S.M.1    Rathnasingh, C.2    Jung, W.C.3    Selvakumar, E.4    Park, S.H.5
  • 11
    • 31444451180 scopus 로고    scopus 로고
    • Optimization of expression of dhaT gene encoding 1,3-propanediol oxidoreductase from Klebsiella pneumoniae in Escherichia coli using the methods of uniform design and regression analysis
    • Y. Cao, Q. Xia, and B. Fang Optimization of expression of dhaT gene encoding 1,3-propanediol oxidoreductase from Klebsiella pneumoniae in Escherichia coli using the methods of uniform design and regression analysis J Chem Technol Biotechnol 81 2006 109 112
    • (2006) J Chem Technol Biotechnol , vol.81 , pp. 109-112
    • Cao, Y.1    Xia, Q.2    Fang, B.3
  • 12
    • 78651093186 scopus 로고    scopus 로고
    • YqhD: A broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals
    • L.R. Jarboe YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals Appl Microbiol Biotechnol 89 2011 249 257
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 249-257
    • Jarboe, L.R.1
  • 13
    • 0042367748 scopus 로고    scopus 로고
    • Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae
    • W. Wang, J. Sun, M. Hartlep, W.D. Deckwer, and A.P. Zeng Combined use of proteomic analysis and enzyme activity assays for metabolic pathway analysis of glycerol fermentation by Klebsiella pneumoniae Biotechnol Bioeng 83 2003 525 536
    • (2003) Biotechnol Bioeng , vol.83 , pp. 525-536
    • Wang, W.1    Sun, J.2    Hartlep, M.3    Deckwer, W.D.4    Zeng, A.P.5
  • 14
    • 84862909110 scopus 로고    scopus 로고
    • Isolation and characterization of the new Klebsiella pneumoniae J2B strain showing improved growth characteristics with reduced lipopolysaccharide formation
    • M.V. Arasu, V. Kumar, S. Ashok, H.H. Song, C. Rathnasingh, and H.J. Lee Isolation and characterization of the new Klebsiella pneumoniae J2B strain showing improved growth characteristics with reduced lipopolysaccharide formation Biotechnol Bioprocess Eng 16 2011 1134 1143
    • (2011) Biotechnol Bioprocess Eng , vol.16 , pp. 1134-1143
    • Arasu, M.V.1    Kumar, V.2    Ashok, S.3    Song, H.H.4    Rathnasingh, C.5    Lee, H.J.6
  • 15
    • 37049173057 scopus 로고
    • Acid-catalysed hydration of acrylaldehyde: Kinetics of the reaction and isolation of β-hydroxypropionaldehyde
    • R.H. Hall, and E.S. Stern 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
  • 18
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: Application to open reading frame characterization
    • A.J. Link, D. Phillips, and G.M. Church Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization J Bacteriol 179 1997 6228 6237
    • (1997) J Bacteriol , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 19
    • 0029583961 scopus 로고
    • Transformation of wildtype Klebsiella pneumoniae with plasmid DNA by electroporation
    • F.F. Severine, J. Bernard, and F. Christiane Transformation of wildtype Klebsiella pneumoniae with plasmid DNA by electroporation J Microbiol Methods 24 1995 49 54
    • (1995) J Microbiol Methods , vol.24 , pp. 49-54
    • Severine, F.F.1    Bernard, J.2    Christiane, F.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli 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
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 43149093576 scopus 로고    scopus 로고
    • Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes
    • J.M. Perez, F.A. Arenas, G.A. Pradenas, J.M. Sandoval, and C.C. Vasquez Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes J Biol Chem 283 2008 7346 7353
    • (2008) J Biol Chem , vol.283 , pp. 7346-7353
    • Perez, J.M.1    Arenas, F.A.2    Pradenas, G.A.3    Sandoval, J.M.4    Vasquez, C.C.5
  • 23
    • 67349171897 scopus 로고    scopus 로고
    • Regulation of glycerol metabolism in Enterobacter aerogenes NBRC12010 under electrochemical conditions
    • K. Hatayama, and T. Yagishita Regulation of glycerol metabolism in Enterobacter aerogenes NBRC12010 under electrochemical conditions Appl Microbiol Biotechnol 83 2009 749 756
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 749-756
    • Hatayama, K.1    Yagishita, T.2
  • 24
    • 44349173795 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12
    • Y.N. Kim, L.O. Ingram, and K.T. Shanmugam Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12 J Bacteriol 190 2008 3851 3858
    • (2008) J Bacteriol , vol.190 , pp. 3851-3858
    • Kim, Y.N.1    Ingram, L.O.2    Shanmugam, K.T.3
  • 25
    • 0025818639 scopus 로고
    • Effect of the energy source on the NADH/NAD ratio and on pyruvate catabolism in anaerobic chemostat cultures of Enterococcus faecalis NCTC 775
    • J.L. Snoep, M.J. Teixeira de Mattos, and O.M. Neijssel Effect of the energy source on the NADH/NAD ratio and on pyruvate catabolism in anaerobic chemostat cultures of Enterococcus faecalis NCTC 775 FEMS Microbiol Lett 81 1991 63 66
    • (1991) FEMS Microbiol Lett , vol.81 , pp. 63-66
    • Snoep, J.L.1    Teixeira De Mattos, M.J.2    Neijssel, O.M.3
  • 26
    • 0026647636 scopus 로고
    • Isolation, characterization, and physiological role of the pyruvate dehydrogenase complex and a-acetolactate synthase of Lactococcus lactis subsp. lactis var. diacetylactis
    • J.L. Snoep, M.J. Teixeira de Mattos, M.J. Starrenburg, and J. Hugenholtz Isolation, characterization, and physiological role of the pyruvate dehydrogenase complex and a-acetolactate synthase of Lactococcus lactis subsp. lactis var. diacetylactis J Bacteriol 174 1992 4838 4841
    • (1992) J Bacteriol , vol.174 , pp. 4838-4841
    • Snoep, J.L.1    Teixeira De Mattos, M.J.2    Starrenburg, M.J.3    Hugenholtz, J.4
  • 27
    • 79955564954 scopus 로고    scopus 로고
    • Development of recombinant Klebsiella pneumoniae ΔdhaT strain for the co-production of 3-hydroxypropionic acid and 1,3-propanediol from glycerol
    • S. Ashok, S.M. Raj, C. Rathnasingh, and S.H. Park Development of recombinant Klebsiella pneumoniae ΔdhaT strain for the co-production of 3-hydroxypropionic acid and 1,3-propanediol from glycerol Appl Microbiol Biotechnol 90 2011 1253 1265
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 1253-1265
    • Ashok, S.1    Raj, S.M.2    Rathnasingh, C.3    Park, S.H.4
  • 28
    • 0030474662 scopus 로고    scopus 로고
    • 12 from propionic acid bacteria under periodic variation of dissolved oxygen concentration
    • 12 from propionic acid bacteria under periodic variation of dissolved oxygen concentration J Ferment Bioeng 82 1996 484 491
    • (1996) J Ferment Bioeng , vol.82 , pp. 484-491
    • Ye, K.1    Shijo, M.2    Jin, S.3    Shimizu, K.4
  • 29
    • 0020463437 scopus 로고
    • DHA system mediating aerobic and anaerobic dissimilation of glycerol in Klebsiella pneumoniae NCIB 418
    • R.G. Forage, and E.C. Lin DHA system mediating aerobic and anaerobic dissimilation of glycerol in Klebsiella pneumoniae NCIB 418 J Bacteriol 151 1982 591 599
    • (1982) J Bacteriol , vol.151 , pp. 591-599
    • Forage, R.G.1    Lin, E.C.2
  • 30
    • 0036189303 scopus 로고    scopus 로고
    • The level of pyruvate-formate lyase controls the shift from homolactic to mixed-acid product formation in Lactococcus lactis
    • C.R. Melchiorsen, K.V. Jokumsen, J. Villadsen, H. Israelsen, and J. Arnau The level of pyruvate-formate lyase controls the shift from homolactic to mixed-acid product formation in Lactococcus lactis Appl Microbiol Biotechnol 58 2002 338 344
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 338-344
    • Melchiorsen, C.R.1    Jokumsen, K.V.2    Villadsen, J.3    Israelsen, H.4    Arnau, J.5
  • 32
    • 33749399255 scopus 로고    scopus 로고
    • A novel-ketoglutaric semialdehyde dehydrogenase: Evolutionary insight into an alternative pathway of bacterial l-arabinose metabolism
    • S. Watanabe, T. Kodaki, and K. Makino A novel-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial l-arabinose metabolism J Biol Chem 281 2006 28876 28888
    • (2006) J Biol Chem , vol.281 , pp. 28876-28888
    • Watanabe, S.1    Kodaki, T.2    Makino, K.3


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