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Volumn 165, Issue 4, 2010, Pages 268-275

Heterologous expression of the Bacillus subtilis (natto) alanine dehydrogenase in Escherichia coli and Lactococcus lactis

Author keywords

Alanine; Alanine dehydrogenase; Fermentation; Lactococcus lactis; Ldh promoter

Indexed keywords

ALANINE DEHYDROGENASE; BACILLUS SUBTILIS; E. COLI; HETEROLOGOUS EXPRESSION; LACTIC ACID BACTERIA; LACTOCOCCUS LACTIS; PARENT STRAIN; STRAIN IMPROVEMENT; STREPTOCOCCUS THERMOPHILUS; SUBTILIS; SWEET TASTE;

EID: 77954483356     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2009.05.008     Document Type: Article
Times cited : (22)

References (22)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 77954862044 scopus 로고    scopus 로고
    • Process for producing l-alanine US Patent 3,458,400.
    • Chibata TI, Kakimoto T, Kato. J. Process for producing l-alanine 1996. US Patent 3,458,400.
    • (1996)
    • Chibata, T.I.1    Kakimoto, T.2    Kato, J.3
  • 3
    • 0028179540 scopus 로고
    • Use of the Escherichia coli β-Glucuronidase (gusA) gene as a reporter gene for analyzing promoters in lactic acid bacteria
    • Christ P., Guus S., de Vos W.M. Use of the Escherichia coli β-Glucuronidase (gusA) gene as a reporter gene for analyzing promoters in lactic acid bacteria. Appl Environ Microbiol 1994, 60:587-593.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 587-593
    • Christ, P.1    Guus, S.2    de Vos, W.M.3
  • 4
    • 0010095461 scopus 로고    scopus 로고
    • The induction of alanine dehydrogenase
    • Freese E., Oosterwyk J. The induction of alanine dehydrogenase. Biochemistry 1996, 2:1212-1216.
    • (1996) Biochemistry , vol.2 , pp. 1212-1216
    • Freese, E.1    Oosterwyk, J.2
  • 5
    • 0019869869 scopus 로고
    • Kinetic mechanism of Bacillus subtilis l-alanine dehydrogenase
    • Grimshaw C.E., Cleland W.W. Kinetic mechanism of Bacillus subtilis l-alanine dehydrogenase. Biochemistry 1981, 20:5650-5655.
    • (1981) Biochemistry , vol.20 , pp. 5650-5655
    • Grimshaw, C.E.1    Cleland, W.W.2
  • 6
    • 0033031823 scopus 로고    scopus 로고
    • Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering
    • Hols P., Kleerebezem M., Schanck A.N., et al. Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering. Nat Biotechnol 1999, 17:588-592.
    • (1999) Nat Biotechnol , vol.17 , pp. 588-592
    • Hols, P.1    Kleerebezem, M.2    Schanck, A.N.3
  • 7
    • 0347337722 scopus 로고    scopus 로고
    • Alanine dehydrogenase from the psychrophilic bacterium strain PA-43: overexpression, molecular characterization, and sequence analysis
    • Irwin J.A., Lynch S.V., Coughlan S., et al. Alanine dehydrogenase from the psychrophilic bacterium strain PA-43: overexpression, molecular characterization, and sequence analysis. Extremophiles 2003, 7:135-143.
    • (2003) Extremophiles , vol.7 , pp. 135-143
    • Irwin, J.A.1    Lynch, S.V.2    Coughlan, S.3
  • 8
    • 1642294918 scopus 로고    scopus 로고
    • L-Alanine Auxotrophy of Lactobacillus johnsonii as demonstrated by physiological, genomic, and gene complementation approaches
    • Kaaij H.V.D., Desiere F., Mollet B., Germond J.E. l-Alanine Auxotrophy of Lactobacillus johnsonii as demonstrated by physiological, genomic, and gene complementation approaches. Appl Environ Microbiol Mar 2004, 1869-1873.
    • (2004) Appl Environ Microbiol Mar , pp. 1869-1873
    • Kaaij, H.V.D.1    Desiere, F.2    Mollet, B.3    Germond, J.E.4
  • 9
    • 34548487173 scopus 로고    scopus 로고
    • Cancer chemopreventive effects of lactic acid bacteria
    • Kim J.E., Kim J.Y., Lee K.W., Lee H.J. Cancer chemopreventive effects of lactic acid bacteria. J Microbiol Biotechnol 2007, 17:1227-1235.
    • (2007) J Microbiol Biotechnol , vol.17 , pp. 1227-1235
    • Kim, J.E.1    Kim, J.Y.2    Lee, K.W.3    Lee, H.J.4
  • 10
    • 0038066313 scopus 로고    scopus 로고
    • Metabolic pathway engineering in lactic acid bacteria
    • Kleerebezem M., Hugenholtz J. Metabolic pathway engineering in lactic acid bacteria. Curr Opin Biotechnol 2003, 14:232-237.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 232-237
    • Kleerebezem, M.1    Hugenholtz, J.2
  • 11
    • 27544451339 scopus 로고    scopus 로고
    • 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis
    • Kleerebezem M. 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis. Appl Microbiol Biotechnol 2005, 68:705-717.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 705-717
    • Kleerebezem, M.1
  • 12
    • 0345471372 scopus 로고    scopus 로고
    • Quorum sensing controlled gene expression in lactic acid bacteria
    • Kuipers O.P., Pascalle G.G.A., Ruyter D., et al. Quorum sensing controlled gene expression in lactic acid bacteria. J Biotechnol 1998, 64:15-21.
    • (1998) J Biotechnol , vol.64 , pp. 15-21
    • Kuipers, O.P.1    Pascalle, G.G.A.2    Ruyter, D.3
  • 13
    • 0027162304 scopus 로고
    • Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity
    • Kuipers O.P., Beerthuyzen M.M., Siezen R.J., et al. Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity. Eur J Biochem 1993, 216:281-291.
    • (1993) Eur J Biochem , vol.216 , pp. 281-291
    • Kuipers, O.P.1    Beerthuyzen, M.M.2    Siezen, R.J.3
  • 14
    • 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 1970, 27:680-685.
    • (1970) Nature , vol.27 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 34548337142 scopus 로고    scopus 로고
    • +-ATPase- and lactate dehydrogenase-defective mutant of Escherichia coli expression alanine dehydrogenase
    • +-ATPase- and lactate dehydrogenase-defective mutant of Escherichia coli expression alanine dehydrogenase. Biotechnol Products Process Eng 2007, 76:819-825.
    • (2007) Biotechnol Products Process Eng , vol.76 , pp. 819-825
    • Masaru, W.1    Kotomi, N.2    Atsushi, Y.3
  • 16
    • 12344282128 scopus 로고    scopus 로고
    • Fibrinolytic enzymes in Asian traditional fermented foods
    • Mine Y., Wong A.H.K., Jiang B. Fibrinolytic enzymes in Asian traditional fermented foods. Food Res Int 2005, 38:243-250.
    • (2005) Food Res Int , vol.38 , pp. 243-250
    • Mine, Y.1    Wong, A.H.K.2    Jiang, B.3
  • 17
    • 48349084356 scopus 로고    scopus 로고
    • Traditional healthful fermented products of Japan
    • Murooka Y., Yamshita M. Traditional healthful fermented products of Japan. J Ind Microbiol Biotechnol 2008, 35:791-798.
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 791-798
    • Murooka, Y.1    Yamshita, M.2
  • 18
    • 58649092806 scopus 로고    scopus 로고
    • Technological and functional applications of low-calories sweeteners from Lactic acid bacteria
    • Patra F., Tomar S.K., Arora S. Technological and functional applications of low-calories sweeteners from Lactic acid bacteria. J Food Sci 2009, 74:R16-R23.
    • (2009) J Food Sci , vol.74
    • Patra, F.1    Tomar, S.K.2    Arora, S.3
  • 19
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • Ruyter P.G.D., Kuipers O.P., Vos W.M.D. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol 1996, 62:3662-3667.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3662-3667
    • Ruyter, P.G.D.1    Kuipers, O.P.2    Vos, W.M.D.3
  • 20
    • 0027371155 scopus 로고
    • Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus subtilis
    • Siranosian K.J., Ireton K., Grossman A.D. Alanine dehydrogenase (ald) is required for normal sporulation in Bacillus subtilis. J Bacteriol 1993, 175(21):6789-6796.
    • (1993) J Bacteriol , vol.175 , Issue.21 , pp. 6789-6796
    • Siranosian, K.J.1    Ireton, K.2    Grossman, A.D.3
  • 21
    • 33748556857 scopus 로고    scopus 로고
    • Fed-batch two-phase production of alanine by a metabolically engineered Escherichia coli
    • Smith G.M., Lee S.A., Reilly K.C., et al. Fed-batch two-phase production of alanine by a metabolically engineered Escherichia coli. Biotechnol Lett 2006, 281:695-1700.
    • (2006) Biotechnol Lett , vol.281 , pp. 695-1700
    • Smith, G.M.1    Lee, S.A.2    Reilly, K.C.3
  • 22
    • 0010098502 scopus 로고
    • Occurrence of an L (+)-alanine-dehydrogenasein. Bacillus subtilis
    • Wiame J.M., Pierard A. Occurrence of an L (+)-alanine-dehydrogenasein. Bacillus subtilis. Nature 1955, 176:1073-1075.
    • (1955) Nature , vol.176 , pp. 1073-1075
    • Wiame, J.M.1    Pierard, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.