WO2001002545A1 - Procede de production d'acide l-amine - Google Patents

Procede de production d'acide l-amine Download PDF

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Publication number
WO2001002545A1
WO2001002545A1 PCT/JP2000/004345 JP0004345W WO0102545A1 WO 2001002545 A1 WO2001002545 A1 WO 2001002545A1 JP 0004345 W JP0004345 W JP 0004345W WO 0102545 A1 WO0102545 A1 WO 0102545A1
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Prior art keywords
lysine
producing
amino acid
acid
fumarase
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PCT/JP2000/004345
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English (en)
Japanese (ja)
Inventor
Masakazu Sugimoto
Hisao Ito
Osamu Kurahashi
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Ajinomoto Co., Inc.
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Priority to AU57073/00A priority Critical patent/AU5707300A/en
Publication of WO2001002545A1 publication Critical patent/WO2001002545A1/fr

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P13/00—Preparation of nitrogen-containing organic compounds
    • C12P13/04—Alpha- or beta- amino acids
    • C12P13/08—Lysine; Diaminopimelic acid; Threonine; Valine
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P13/00—Preparation of nitrogen-containing organic compounds
    • C12P13/04—Alpha- or beta- amino acids
    • C12P13/14—Glutamic acid; Glutamine

Definitions

  • the present invention relates to a method for producing an L-amino acid by a fermentation method, and particularly to a method for producing L-lysine and L-glutamic acid.
  • L-lysine is widely used as a feed additive and the like
  • L-glutamic acid is widely used as a seasoning material and the like.
  • L-amino acids such as L-lysine and L-glutamic acid have been obtained by using a coryneform bacterium belonging to the genus Brevipacterium or Corynebacterium having the ability to produce these L-amino acids. It is industrially produced by fermentation. For these coryneform bacteria, strains isolated from the natural world or artificial mutants of the strains are used in order to improve productivity.
  • JP-A-63-2189 discloses that a glutamate dehydrogenase gene, an isocitrate dehydrogenase gene, an aconitate hydrase gene and a citrate synthase gene are amplified or introduced. Accordingly, a technique for increasing the ability to produce L-glucamic acid has been disclosed.
  • An object of the present invention is to provide a method for producing an L-amino acid such as L-lysine or L-amino acid by a fermentation method which is further improved, and a strain used for the same.
  • the present inventors have conducted intensive studies to solve the above-mentioned problems, and as a result, by introducing a gene encoding fumarase into coryneform bacteria and enhancing fumarase activity, L-lysine or L-glutamine The inventors have found that the production of evening acid can be increased, and have completed the present invention. That is, the present invention is as follows.
  • a coryneform bacterium having enhanced fumalase activity in cells and capable of producing L-amino acid (1) A coryneform bacterium having enhanced fumalase activity in cells and capable of producing L-amino acid.
  • L-amino acid is selected from L-lysine, L-glutamic acid, L-threonine, L-isoleucine, and L-serine.
  • the gene encoding the humalase is derived from a bacterium belonging to the genus Escherichia.
  • the coryneform bacterium of any of (1) to (4) above is cultured in a medium, L-amino acids are produced and accumulated in the culture, and L-amino acids are collected from the culture.
  • L A method for producing amino acids.
  • the coryneform bacterium of the present invention is a coryneform bacterium having an ability to produce L-amino acid and having enhanced fumarase activity in cells.
  • the L-amino acid include L-lysine, L-glutamic acid, L-threonine, L-isoleucine, L-serine and the like. Of these, L-lysine and L-glutamic acid are preferred.
  • embodiments of the present invention will be described mainly with respect to a coryneform bacterium having L-lysine-producing ability or L-glucaminic acid-producing ability, but the present invention provides a biosynthesis system specific to an L-amino acid of interest. The same applies to those located downstream.
  • coryneform bacteria referred to in the present invention are a group of microorganisms defined in Bergey's Manual of Determinative Bacteriology, 8th edition, p. 599 (1974). , Aerobic, gram positive, It is a non-acid-fast, non-spore-forming bacillus, including bacteria that were previously classified into the genus Brevipacterium but are now integrated as corynebacteria (Int. J. Syst. Bacteriol., 41, 255 (1981)), and also includes bacteria of the genus Brevipacterium and Micropaterims which are very closely related to the genus Corynepacterium. Examples of the strains of coryneform bacteria suitably used for producing L-lysine or L-glutamic acid include, for example, those shown below.
  • Corynebacterium thermoaminogenes AJ12340 (FERM BP-1539) To obtain them, for example, American Type Culture Collective Address 12301 Park lawn Drive, Rockville, Maryland 20852, United States of America). That is, a registration number corresponding to each microorganism is assigned, and the microorganism can be ordered by referring to this registration number. The registration numbers for each microorganism are listed on the catalog of the American Culture's 'Culture' collection.
  • AJ12340 strain was deposited with the Institute of Biotechnology, Industrial Technology Institute of the Ministry of International Trade and Industry (Postal Code 305-856-6 1-3 1-3 Tsukuba-Higashi, Ibaraki, Japan) based on the Budapest Treaty. Have been.
  • mutants having L-amino acid-producing ability such as L-lysine or L-glutamic acid derived from these strains can also be used in the present invention.
  • Such artificial mutants include the following. S- (2-aminoethyl) -cysteine (hereinafter abbreviated as "AEC") resistant mutant (for example, Brevibacterium 'Lactofamentum AJ11082 (NRRL B-11470), Japanese Patent Publication No. 56-1914, Japanese Patent Publication No. No. 56-1915, No. 57-14157, No. 57-14158, No. 57-30474, No. 58-10075, No. 59-4993, No. 61-35840, No.
  • AEC S- (2-aminoethyl) -cysteine
  • L-lysine-producing mutant strains (JP-A-55-9783, JP-A-53-86090) Call resistant, producing L- lysine Burebiba Kuteriumu genus or Corynebacterium Park Teri ⁇ beam genus producing mutant strain (U.S. Patent No. 4,411,997).
  • Examples of coryneform bacteria having L-threonine-producing ability include Corynebacterium acetoacidophilum AJ12318 (FERM BP-1172) (see US Pat. No. 5,188,949) and L-isoleucine-producing ability.
  • Examples of the coryneform bacterium having the above include Brevibacterium flavum AJ12149 (FERM BP-759) (see US Pat. No.
  • the ability to produce L-amino acid such as L-lysine refers to the ability of a coryneform bacterium to accumulate a significant amount of L-amino acid such as L-lysine in the medium when cultured in the medium. Or the ability to increase the content of amino acids such as L-lysine in cells.
  • a gene fragment encoding fumarase is ligated to a vector that functions in the bacterium, preferably a multicopy vector, to produce recombinant DNA. Then, this may be introduced into a coryneform bacterium capable of producing L-lysine or L-glucamic acid for transformation. An increase in the copy number of the gene encoding fumalase in the cells of the transformed strain results in enhanced fumalase activity.
  • Humalase is encoded by the fUDl gene in Escherichia coli.
  • the fumarase gene either a gene of a coryneform bacterium or a gene derived from another organism such as a bacterium belonging to the genus Escherichia can be used.
  • the nucleotide sequence of the fum gene of Escherichia coli has already been clarified (Bell, PJ et al., J. Bacteriol. 171, 3494-3503 (1989), Genbank / EMBL / DDBJ accession No. M27058).
  • a primer prepared based on the base sequence for example, the primers shown in SEQ ID NOs: 1 and 2 in the Sequence Listing, a PCR method using Escherichia coli chromosomal DNA as type I (PCR: polymerase chain reaction; J. et al; Trends Genet. 5, 185 (1989)) to obtain the fum gene.
  • Genes encoding fumarase of other microorganisms such as coryneform bacteria can be obtained in a similar manner.
  • Chromosomal DNA is obtained from bacteria that are DNA donors, for example, by the method of Saito and Miura (H. Saito and .iura Biochem. Biophys. Acta, 72, 619 (1963)), Biological Engineering Experiment, Pp. 97-98, Baifukan, 1992).
  • the gene encoding fumarase amplified by the PCR method is connected to a vector DNA capable of autonomous replication in the cells of Escherichia coli and / or coryneform bacteria to prepare a recombinant DNA, which is then transformed into Escherichia coli. Introduced into cells Then, the operation later becomes difficult.
  • a vector capable of autonomous replication in Escherichia coli cells a plasmid vector is preferable, and a vector capable of autonomous replication in a host cell is preferable.
  • the vector autonomously replicable in cells of coryneform bacteria (see Japanese Patent Laid HirakiAkira 58- 67699) pAM330, P HM1519 (see JP-A-58- 77895) and the Ru mentioned.
  • a DNA fragment capable of autonomously replicating plasmid in coryneform bacteria is extracted from these vectors and inserted into the Escherichia coli vector, whereby autonomous replication in both Escherichia coli and coryneform bacteria occurs. It can be used as a shuttle vector that is not possible. The following are examples of such a shuttle vector.
  • the microorganism holding each vector and the accession number of the international depository organization are shown in parentheses.
  • PAJ611 Escherichia Cori AJ11884 (FERM BP-138)
  • PAJ3148 Coryne ⁇ , ⁇ , ⁇ , ⁇ ⁇ 820 820 SR8203 (ATCC39137)
  • the recombinant DNA is transformed into DNA by transforming the cells of a DNA-accepting bacterium into a protoplast or spheroblast that readily incorporates the recombinant DNA, as is known for Bacillus subtilis, actinomycetes and yeast.
  • Method for introduction into recipient bacteria (Chang, S. and Choen, SN, Molec. Gen. Genet., 168, 111 (1979), -Bibb, MJ, Ward, JMand Hopwood, 0.A., Nature, 274, 398 (1978); Hinnen, A., Hicks, JBand Fink, GR, Proc. Natl. Acad. Sci. USA, 75 1929 (1978)).
  • the transformation method used in the examples of the present invention is the electric pulse method (see Japanese Patent Application Laid-Open No. 2-207791).
  • Enhancement of fumarase-encoding activity can also be achieved by the presence of multiple copies of the fumarase-encoding gene on the chromosome DNA of the host.
  • homologous recombination is performed by using a sequence present in multiple copies on chromosome DNA as a target.
  • a sequence present in multiple copies on the chromosomal DNA it is possible to use repetitive DNA and inverted repeats present at the end of a transposable element.
  • a gene encoding fumalase is mounted on a transposon and transferred, and multiple copies are introduced into chromosomal DNA. Is also possible. Either method increases the copy number of the gene encoding fumarase in the transformant, resulting in enhanced fumarase activity.
  • the enhancement of fumarase activity can be achieved not only by the gene amplification described above, but also by replacing the expression regulatory sequence such as the promoter of the gene encoding fumarase on chromosome DNA or plasmid with a strong one. Is also achieved (see Japanese Patent Application Laid-Open No. H11-215280). For example, lac promoter, trp promoter, trc promoter, tac promoter, PR promoter of lambda phage, PL promoter and the like are known as strong promoters. By substituting these promoters, fumarase activity is enhanced by enhancing expression of a gene encoding humalase.
  • the coryneform bacterium of the present invention may have enhanced enzymatic activities thereof by enhancing enzyme genes such as other amino acid synthesizing pathways or glycolytic pathways in addition to the fumarase activity.
  • enzyme genes such as other amino acid synthesizing pathways or glycolytic pathways in addition to the fumarase activity.
  • examples of genes that can be used for the production of L-lysine include Assubald Kinase Hissubunit protein or / ?, in which synergistic feedback inhibition by L-lysine and L-threonine has been substantially eliminated.
  • a gene encoding a subunit protein (W094 / 25605 International Publication Pamphlet); a wild-type phosphoenolpyruvate carboxylase gene derived from coryneform bacteria (JP-A-60-87788); a wild-type dihydropicolinic acid derived from coryneform bacteria
  • a gene encoding a synthase Japanese Patent Publication No. 6-55149 and the like are known.
  • genes that can be used for the production of L-glutamic acid include glutamate dehydrogenase (GDH, JP-A-61-268185), glutamine synthase, and glutamate synthase.
  • GDH glutamate dehydrogenase
  • glutamine synthase glutamate synthase
  • glutamate synthase glutamate synthase
  • Isosenate dehydrogenase Japanese Patent Application Laid-Open No. 62-166890, Japanese Patent Application Laid-Open No. 63-214189
  • aconitate hydratase Japanese Patent Application Laid-open No. — 294 886
  • Synthetic citrate Synthetic citrate
  • pyruvate carboxylase Japanese Patent Application Laid-Open No. 60-87788, Japanese Patent Application Laid-Open No.
  • an enzyme that catalyzes a reaction that diverges from a target L-amino acid biosynthetic pathway to produce a compound other than the L-amino acid may be reduced or lacking.
  • homoserine dehydrogenase is an enzyme that catalyzes a reaction that diverges from the L-lysine biosynthetic pathway to produce a compound other than L-lysine (see WO95 / 23864).
  • Enzymes that catalyze the reaction that branches off from the L-glutamic acid biosynthetic pathway to produce compounds other than L-glutamic acid include ketoglutaric acid dehydrogenase, isoquenate lyase, and acetyl phosphate.
  • a biotin action inhibitor such as a surfactant to a coryneform bacterium capable of producing L-glutamic acid
  • a biotin action inhibitor in a medium containing an excessive amount of biotin can be obtained.
  • L-glutamic acid can be produced in the absence of E. coli (see W096 / 06180).
  • Examples of such coryneform bacteria include Brevipacterium. Lactofermentum AJ13029 described in W096 / 06180.
  • the AJ13029 strain was granted to the Institute of Biotechnology and Industrial Technology, Institute of Industrial Science and Technology (Postal Code 305-8566, 1-3 1-3 Tsukuba-Higashi, Ibaraki, Japan) on September 2, 1994 under the accession number FERM P-14501. It was deposited and transferred to an international deposit under the Budapest Treaty on August 1, 1995, and given accession number FERM BP-5189.
  • a coryneform bacterium capable of producing L-lysine and L-glutamic acid is given a temperature-sensitive mutation against a substance that suppresses the action of biotin, thereby suppressing the action of biotin in a medium containing an excessive amount of biotin.
  • L-lysine and L-glutamic acid can be produced simultaneously in the absence of a substance (see W096 / 06180).
  • strains include Brevipacterium 'lactofermentum AJ12993 strain described in W096 / 06180.
  • the stock was issued to the Institute of Biotechnology, Institute of Biotechnology, Japan, on June 3, 1999 (Postal Code 305-8566, Tsukuba 1-chome 1-3, Ibaraki, Japan), with accession number FERM P- Deposited at 14348, transferred to an international deposit under the Budapest Treaty on August 1, 1995, and given accession number FERM BP-5188.
  • the phrase “enhanced activity” of an enzyme generally means that the enzyme activity in a cell is higher than that of a wild-type strain, and is modified by a gene recombination technique or the like. When a strain with enhanced enzyme activity is obtained, it means that the enzyme activity in the cell is higher than that of the strain before modification.
  • reduced activity usually means that the enzyme activity in a cell is lower than that of a wild-type strain, and the enzyme activity has been reduced by modification by genetic recombination technology or the like. When a strain is obtained, it means that the enzyme activity in the cell is lower than that of the strain before modification.
  • a coryneform bacterium having enhanced fumarase activity and capable of producing L-amino acid is cultured in a suitable medium, the L-amino acid accumulates in the medium.
  • a coryneform bacterium having enhanced L-lysine activity and capable of producing L-lysine acid is cultured in a suitable medium, L-lysine accumulates in the medium.
  • a coryneform bacterium having enhanced fumarase activity and capable of producing L-glucaminic acid is cultured in a suitable medium, L-glucaminic acid accumulates in the medium.
  • L-lysine and L-glucamic acid accumulate in the medium.
  • the L-lysine-producing bacterium may be cultured under L-glucaminic acid-producing conditions, or it has the ability to produce L-lysine.
  • a coryneform bacterium and a coryneform bacterium having an ability to produce L-glucaminic acid may be mixed and cultured (Japanese Patent Application Laid-Open No. 5-37993).
  • the culture medium used for producing L-amino acids such as L-lysine or L-glumic acid using the microorganism of the present invention contains a carbon source, a nitrogen source, inorganic ions, and other organic micronutrients as required. This is a normal medium.
  • Carbon sources include glucose, lactose, galactose, fructose, sucrose, molasses, carbohydrates such as starch hydrolysates, alcohols such as ethanol and inositol, acetic acid, fumaric acid, citric acid, and succinic acid. And other organic acids can be used.
  • Nitrogen sources include ammonium sulfate, ammonium nitrate, ammonium chloride, ammonium phosphate, ammonium acetate, and other inorganic ammonium salts, ammonia, peptone, meat extract, yeast extract, yeast extract, corn 'steep' liquor, soy hydrolyzate Organic nitrogen, ammonia gas, ammonia water, and the like can be used.
  • inorganic ions small amounts of potassium phosphate, magnesium sulfate, iron ions, manganese ions and the like are added.
  • organic trace nutrients it is desirable to include a required substance such as vitamin B1 or a yeast extract in an appropriate amount as necessary.
  • the cultivation is preferably carried out for 16 to 72 hours under aerobic conditions such as shaking cultivation, aeration and stirring cultivation, and the cultivation temperature is 30 ° C to 45 ° C. Control to ⁇ 9.
  • an inorganic or organic acidic or alkaline substance, ammonia gas or the like can be used.
  • L-amino acid can be collected from the fermentation liquor in the same manner as in the normal L-amino acid production method. Can be done. For example, collection of L-lysine can be usually carried out by combining an ion exchange resin method, a precipitation method and other known methods.
  • the method for collecting L-glutamic acid may be a conventional method, for example, an ion exchange resin method, a crystallization method, or the like. Specifically, L-glutamic acid may be adsorbed and separated by an anion exchange resin, or may be neutralized and crystallized. When producing both L-lysine and L-glutamic acid, when these are used as a mixture, it is unnecessary to separate these amino acids from each other. Examples Hereinafter, the present invention will be described more specifically with reference to Examples.
  • the nucleotide sequence of the fum gene of Escherichia coli has already been elucidated (Bell, P. J. et al., J. Bacteriol. 171, 3494-3503 (1989), Genbank / EMBL / DDBJ accession No. M27058). Based on the reported nucleotide sequence, SEQ ID NOS: 1 and 2: The following primers were synthesized, and the pyruvate dehydrogenase gene was amplified by PCR using the chromosomal DNA of Escherichia coli JM109 strain as type III. did.
  • S sequence number 1 corresponds to the sequence from the 1st to 24th base of the base sequence of the fum gene described in Genbank / EMBL / DDBJ accetion No. M 27058; 2 corresponds to the sequence from the 3162nd base to the 3149th base.
  • the chromosomal DNA of Escherichia coli JM109 strain was prepared according to a conventional method (Biotechnological Experiments, edited by Biotechnology Society of Japan, pp. 97-98, Baifukan, 1992).
  • PCR reaction standard reaction conditions described on page 185 of the PCR method forefront (edited by Takeo Sekiya et al., Kyoritsu Shuppan, 1998) were used.
  • Escherichia coli harboring pHC4 was named the private number AJ12617, and said on April 24, 1999, the Ministry of International Trade and Industry, National Institute of Advanced Industrial Science and Technology, Institute of Biotechnology and Industrial Technology (Zip code 305-8566).
  • the fumalase activity of the JM109 strain and the JM109 strain having pHC4 fum was determined by Kanarek, It was measured by the method described in L. et al., J. Biol. Chem., 239, 4202-4206 (1964). As a result, the JM109 strain having pHC 4 fum exhibited about 17 times the fumarase activity of the JM109 strain without pHC 4 fum, indicating that the fum gene was expressed. confirmed.
  • Brevipacterium lactofermentum AJ13029 was transformed with plasmid pHC4fum by the electric pulse method (see Japanese Patent Application Laid-Open No. 2-207791) to obtain the obtained transformant.
  • culture for producing L-glutamic acid was performed as follows. Cells of the AJ13029 / pHC4fum strain obtained by culturing in a CM2B plate medium containing 5 ⁇ g / ml chloramphenicol were mixed with L-cells having the following composition containing 5 ⁇ g / ml chloramphenicol.
  • the medium was inoculated into a glucanic acid production medium, cultured at 31.5 ° C with shaking, and shaken until the sugar in the medium was consumed.
  • the obtained culture was inoculated into a medium having the same composition in an amount of 5%, and cultured at 37 ° C with shaking until the sugar in the medium was consumed.
  • a strain obtained by transforming a plasmid pHC4, which can be autonomously replicated with a previously obtained corynebacterium bacterium, into the corynebacterium bacterium AJ13029 as a control by the electric pulse method and culturing in the same manner as described above did.
  • Protein hydrolyzate (bean concentrate) 30 ml
  • Brevipacterium lactofermentum AJ12993 was transformed with plasmid pHC4fum by the electric pulse method (see Japanese Patent Application Laid-Open No. 2-207791) to obtain the obtained transformant.
  • culture for producing L-lysine and L-glucamic acid was carried out as follows.
  • the cells of the AJ12993 / pHC4fum strain obtained by culturing in a CM2B plate medium containing 5 ⁇ g / ml chloramphenicol were mixed with the L-cell containing 5 // g / ml chloramphenicol.
  • a lysine production medium was inoculated and cultured at 31.5 ° C.
  • the culture temperature was shifted to 34 ° C, and the culture was performed with shaking until the sugar in the medium was consumed.
  • a strain obtained by transforming a plasmid PHC4 capable of autonomously replicating with a previously obtained corynebacterium bacterium into an AJ12993 bacterium of the genus Corynebacterium by an electric pulse method was cultured in the same manner as described above.
  • L-amino acid such as L-lysine or L-glucamic acid

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Abstract

Cette invention concerne un procédé de production d'acide L-aminé, tel que de l'acide de L-lysine ou L-glutamique, lequel procédé fait appel à une technique de fermentation améliorée par rapport aux techniques traditionnelles. Cette technique consiste à transférer un gène codant la fumarase dans une bactérie corynéforme capable de produire un acide L-aminé tel que de l'acide de L-lysine ou L-glutamique, ce qui augmente l'activité de la fumarase et accroît la production d'acide L-aminé. Cette invention concerne également des souches utilisées dans cette technique.
PCT/JP2000/004345 1999-07-02 2000-06-30 Procede de production d'acide l-amine WO2001002545A1 (fr)

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AU57073/00A AU5707300A (en) 1999-07-02 2000-06-30 Process for producing l-amino acid

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JP11/189517 1999-07-02
JP18951799A JP2003144160A (ja) 1999-07-02 1999-07-02 Ｌ−アミノ酸の製造法

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WO2008044409A1 (fr) 2006-10-10 2008-04-17 Ajinomoto Co., Inc. Procédé de fabrication d'un l-amino acide
WO2008075483A1 (fr) 2006-12-19 2008-06-26 Ajinomoto Co., Inc. Procédé de production d'un acide aminé l
WO2008102572A1 (fr) 2007-02-20 2008-08-28 Ajinomoto Co., Inc. Procédé de fabrication d'acide aminé l ou d'acide nucléique
WO2008114721A1 (fr) 2007-03-14 2008-09-25 Ajinomoto Co., Inc. Microorganisme capable de produire un acide aminé de type acide l-glutamique et procédé de fabrication d'acide aminé
EP2202299A1 (fr) 2008-12-22 2010-06-30 Ajinomoto Co., Inc. Procédé de production de L-Lysine
WO2014185430A1 (fr) 2013-05-13 2014-11-20 味の素株式会社 Procédé de fabrication d'acide aminé l
WO2015005406A1 (fr) 2013-07-09 2015-01-15 味の素株式会社 Procédé de fabrication de substance utile
WO2015060314A1 (fr) 2013-10-21 2015-04-30 味の素株式会社 Procédé de production d'un acide aminé de forme l
WO2015060391A1 (fr) 2013-10-23 2015-04-30 味の素株式会社 Procédé de production d'une substance cible
EP3165608A1 (fr) 2015-10-30 2017-05-10 Ajinomoto Co., Inc. Procédé de production d'acide aminé l de la famille glutamate
EP3385389A1 (fr) 2017-04-03 2018-10-10 Ajinomoto Co., Inc. Procédé de production d'acide aminé l à partir de fructose
WO2020071538A1 (fr) 2018-10-05 2020-04-09 Ajinomoto Co., Inc. Procédé de production d'une substance cible par fermentation bactérienne
WO2022092018A1 (fr) 2020-10-28 2022-05-05 味の素株式会社 Procédé de production d'acide l-aminé
EP4345166A2 (fr) 2022-09-30 2024-04-03 Ajinomoto Co., Inc. Procédé de production d'acide l-aminé

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2006340603A (ja) * 2003-06-23 2006-12-21 Ajinomoto Co Inc Ｌ−グルタミン酸の製造法

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS63119688A (ja) * 1986-11-07 1988-05-24 Kyowa Hakko Kogyo Co Ltd Ｌ−グルタミン酸およびｌ−プロリンの製造法
JPS63214189A (ja) * 1987-03-04 1988-09-06 Asahi Chem Ind Co Ltd Ｌ―グルタミン酸の製造方法
JPH04349879A (ja) * 1991-05-28 1992-12-04 Mitsubishi Petrochem Co Ltd ブレビバクテリウム属微生物の培養法
EP0841395A1 (fr) * 1995-06-07 1998-05-13 Ajinomoto Co., Inc. Procede de production de l-lysine
EP0857784A2 (fr) * 1996-12-05 1998-08-12 Ajinomoto Co., Inc. Procédé de production de L-Lysine

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS63119688A (ja) * 1986-11-07 1988-05-24 Kyowa Hakko Kogyo Co Ltd Ｌ−グルタミン酸およびｌ−プロリンの製造法
JPS63214189A (ja) * 1987-03-04 1988-09-06 Asahi Chem Ind Co Ltd Ｌ―グルタミン酸の製造方法
JPH04349879A (ja) * 1991-05-28 1992-12-04 Mitsubishi Petrochem Co Ltd ブレビバクテリウム属微生物の培養法
EP0841395A1 (fr) * 1995-06-07 1998-05-13 Ajinomoto Co., Inc. Procede de production de l-lysine
EP0857784A2 (fr) * 1996-12-05 1998-08-12 Ajinomoto Co., Inc. Procédé de production de L-Lysine

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
BELL PHILIP J. ET AL.: "Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of escherichia coli K-12", JOURNAL OF BACTERIOLOGY, vol. 171, no. 6, June 1989 (1989-06-01), pages 3494 - 3503, XP002932510 *

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WO2008044409A1 (fr) 2006-10-10 2008-04-17 Ajinomoto Co., Inc. Procédé de fabrication d'un l-amino acide
WO2008075483A1 (fr) 2006-12-19 2008-06-26 Ajinomoto Co., Inc. Procédé de production d'un acide aminé l
WO2008102572A1 (fr) 2007-02-20 2008-08-28 Ajinomoto Co., Inc. Procédé de fabrication d'acide aminé l ou d'acide nucléique
WO2008114721A1 (fr) 2007-03-14 2008-09-25 Ajinomoto Co., Inc. Microorganisme capable de produire un acide aminé de type acide l-glutamique et procédé de fabrication d'acide aminé
EP2657332A1 (fr) 2007-03-14 2013-10-30 Ajinomoto Co., Inc. Procédé de production de l'acide aminé de la famille de l'acide L-glutamique
EP2202299A1 (fr) 2008-12-22 2010-06-30 Ajinomoto Co., Inc. Procédé de production de L-Lysine
WO2014185430A1 (fr) 2013-05-13 2014-11-20 味の素株式会社 Procédé de fabrication d'acide aminé l
EP3521433A1 (fr) 2013-07-09 2019-08-07 Ajinomoto Co., Inc. Procédé de production d'acide l-glutamique
WO2015005406A1 (fr) 2013-07-09 2015-01-15 味の素株式会社 Procédé de fabrication de substance utile
WO2015060314A1 (fr) 2013-10-21 2015-04-30 味の素株式会社 Procédé de production d'un acide aminé de forme l
WO2015060391A1 (fr) 2013-10-23 2015-04-30 味の素株式会社 Procédé de production d'une substance cible
EP3165608A1 (fr) 2015-10-30 2017-05-10 Ajinomoto Co., Inc. Procédé de production d'acide aminé l de la famille glutamate
EP3385389A1 (fr) 2017-04-03 2018-10-10 Ajinomoto Co., Inc. Procédé de production d'acide aminé l à partir de fructose
WO2020071538A1 (fr) 2018-10-05 2020-04-09 Ajinomoto Co., Inc. Procédé de production d'une substance cible par fermentation bactérienne
WO2022092018A1 (fr) 2020-10-28 2022-05-05 味の素株式会社 Procédé de production d'acide l-aminé
EP4345166A2 (fr) 2022-09-30 2024-04-03 Ajinomoto Co., Inc. Procédé de production d'acide l-aminé

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