WO2000056859A1 - Procede de production des l-aminoacides - Google Patents

Procede de production des l-aminoacides Download PDF

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Publication number
WO2000056859A1
WO2000056859A1 PCT/JP2000/001655 JP0001655W WO0056859A1 WO 2000056859 A1 WO2000056859 A1 WO 2000056859A1 JP 0001655 W JP0001655 W JP 0001655W WO 0056859 A1 WO0056859 A1 WO 0056859A1
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Prior art keywords
lysine
producing
acid
amino acid
gene
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Japanese (ja)
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Masakazu Sugimoto
Hisao Ito
Osamu Kurahashi
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Ajinomoto Co Inc
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Ajinomoto Co Inc
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Priority to AU31943/00A priority Critical patent/AU3194300A/en
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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
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N1/00—Microorganisms; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
    • C12N1/20—Bacteria; Culture media therefor
    • C12N1/205—Bacterial isolates
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
    • C12R2001/00—Microorganisms ; Processes using microorganisms
    • C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
    • C12R2001/15—Corynebacterium

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
  • L-glutamic acid is widely used as a seasoning material.
  • L-amino acids such as L-lysine and L-glutamic acid have been produced by fermentation using a coryneform bacterium belonging to the genus Brevibacterium or Corynebacterium having the ability to produce L-amino acid. It is industrially produced.
  • coryneform bacteria strains isolated from the natural world or human mutants of the strains are used in order to improve productivity.
  • various techniques have been disclosed for increasing the activity of producing L-amino acids by enhancing the activity of L-amino acid biosynthetic enzymes by recombinant DNA technology.
  • a gene encoding aspartokinase (mutant lysC) in which feedback inhibition by L-lysine and L-threonine has been released a dihydrodipicolinate reductase gene ( dapB), the dihydrodibicolinate synthase gene (dapA), the diaminopimelate decarboxylase gene (lysA), and the diaminopimelate dehydrogenase gene (ddh) (W096 / 40934), LysA and DDH (JP-A-9-1322774).
  • LysC-LysA and phosphoenolpyruvate carboxylase gene (ppc) (Japanese Patent Application Laid-Open No. 10-165180), mutant lysC, dapB, dapA, lysA and aspartic acid aminotransferase gene (aspC) (Kaihei 10-215883) is known to improve the L-lysine-producing ability of the bacterium. .
  • 63-214189 discloses that the glutamate dehydrogenase gene, the disoquatate dehydrogenase gene, the aconitate hydrase enzyme, and the citrate synthase gene are enhanced. 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-glutamic acid by a fermentation method which has been further improved than before, and a strain used therefor.
  • the present inventors have conducted intensive studies to solve the above problems, and as a result, introduced a gene encoding phosphoeno-rubyruvic acid synthase into coryneform bacteria, It has been found that the production of L-lysine or L-glucaminic acid can be increased by enhancing the zease activity, thereby completing the present invention.
  • the present invention is as follows.
  • a coryneform bacterium which has enhanced phosphoenolpyruvate synthase activity in cells and has the ability to produce amino acids.
  • the coryneform bacterium according to any one of (1) to (4) is cultured in a medium, L-amino acid is produced and accumulated in the culture, and L-amino acid is collected from the culture. Method for producing L-amino acid.
  • L-amino acid is selected from L-lysine, L-glutamic acid, L-threonine, L-isoleucine and L-serine.
  • the coryneform bacterium of the present invention is a coryneform bacterium having L-amino acid-producing ability and enhanced phosphoenorubyruvate synthase activity in cells.
  • the L-amino acid include L-lysine, L-glutamic acid, L-threonine, L-isoleucine, L-serine and the like. Among these, L-lysine and L-glutamic acid are preferred.
  • the power of describing an embodiment of the present invention mainly for a coryneform bacterium having an L-lysine-producing ability or an L-glucamic acid-producing ability
  • the present invention provides a biosynthesis system specific to an L-amino acid. Phosphoenolpyruvate synthase can be similarly applied to those located downstream.
  • coryneform bacteria As the coryneform bacteria referred to in the present invention, a group defined in Bergey's Manual of Determinative Bacteriology, 8th edition, p. 599 (1974) It is an aerobic, gram-positive, non-acid-fast, non-sporulating bacillus that was previously classified as Brevibacterium, but is now integrated as Corynepacterium. Bactenol., 41, 255 (1981), and also includes bacteria of the genus Brevibacterium and Micropaterium, which are closely related to the genus Corynebacterium. The strains of coryneform bacteria suitably used for the production of L-lysine or L-glutamic acid include, for example, those shown below.
  • mutants having L-lysine-producing ability or L-glutamic acid-producing ability derived from these strains can also be used in the present invention.
  • Such human mutants include the following. S— (2-aminoethyl) monocysteine (hereinafter abbreviated as “AEC”) resistant mutant (for example, Brevibacterium Tof amentum AJ11082 (NRRL B-11470), JP-B 56-1914, JP-B 56-1915, JP-B 57-14157, JP-B 57-14158, JP-B 57-30474, JP-B 58- 10075, JP-B-59-4993, JP-B-61-35840, JP-B-62-24074, JP-B-62-36673, JP-B-5-11958, JP-B7-11-112437, JP-B7-112438 Mutants that require amino acids such as L-homoserine for their growth (Japanese Patent Publication
  • L-amino acid-producing ability refers to the ability of a coryneform bacterium to accumulate a significant amount of L-amino acid in a medium when cultured in the medium, or the L-amino acid in the cells. Refers to the ability to increase amino acid content.
  • a gene fragment encoding phosphoenolpyruvate synthase must be isolated from a vector, preferably a multicopy vector, which functions in the bacterium. Ligation may be performed to produce a recombinant DNA, which 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 phosphoenol pyruvate synthase in the cells of the transformed strain resulted in phosphoenol Rubilate synthase activity is enhanced. Phosphoenorubyruvate synthase is encoded by the pps gene in Escherichia coli.
  • phosphoenol pyruvate synthase gene 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 pps gene of Escherichia coli has already been determined (Mol. Gen. Genet., 231 (2), 332-336 (1992), Genbank / EMBL / DDBJ accession No. M69116).
  • a primer prepared based on the sequence for example, the primers shown in SEQ ID NOs: 1 and 2 in the Sequence Listing, a PCR method using Escherichia coli chromosome DNA as type III (PCR: polymerase chain reaction; White, TJ et al. ., Trends Genet. 5, 185 (1989)) to obtain the pps gene.
  • Genes encoding phosphoenolpyruvate synthase of other microorganisms such as coryneform bacteria can be obtained in a similar manner.
  • Chromosomal DNA can be obtained from bacteria that are DNA donors, for example, by the method of Saito and Miura (H. Saito and K. Miura, Biochem. Biophys. Acta, 72, 619 (1963), Bioengineering Experiments, Edited by the Society, pp. 97-98, Baifukan, 1992).
  • the gene encoding phosphoenolpyruvate synthase amplified by the PCR method is connected to a vector DNA that can be replicated autonomously in cells of Escherichia coli and / or coryneform bacteria to transform the recombinant DNA. If prepared and introduced into Escherichia coli cells, subsequent operations will be 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.
  • Examples of vectors that can replicate autonomously in coryneform bacteria cells include PAM330 (see Japanese Patent Application Laid-Open No. 58-67699) and PHM1519 (see Japanese Patent Application Laid-Open No. 58-77895).
  • a DNA fragment capable of autonomously replicating plasmid in coryneform bacteria is extracted from these vectors and inserted into the Escherichia coli vector, and then autonomously expressed in both Escherichia coli and coryneform bacteria. Cannot be duplicated It can be used as a so-called shuttle vector.
  • the accession number of the international depository organization of the microorganisms holding each vector is shown in parentheses.
  • PAJ440 C Chills, Chillis AJ11901 (FEM BP-140)
  • cells of DNA recipients such as those known for Bacillus subtilis, actinomycetes and yeast, can be transformed into protoplasts or spheroplasts that readily incorporate the recombinant DNA and the recombinant DNA can be converted to DNA.
  • Method for introduction into recipient bacteria (Chang, S. and Choen, SN, Molec. Gen. Genet., 168, 111 (1979); Bibb'MJ, Ward, JM and Hopwood, OA, Nature, 274, 398 (1978) Hinnen, A., Hicks. JB and Fink, GR, Proc. Natl. Acad. Sci. USA, 751929 (1978)).
  • the transformation method used in the examples is the electric pulse method (see Japanese Patent Application Laid-Open No. Hei 2-20771).
  • Enhancement of phosphoenol pyruvate synthase-encoding activity can also be achieved by allowing the gene encoding phosphoenolpyruvate synthase to be present in multiple copies on the chromosomal DNA of the host.
  • multiple copies of the gene on chromosomal DNA can be used as a target. Performed by homologous recombination.
  • a relative DNA and an inverted repeat at the end of a transposable element can be used as a sequence present in multiple copies on the chromosomal DNA.
  • a gene encoding phosphoenol pyruvate synthase is mounted on a transposon, transferred, and placed on chromosomal DNA. It is also possible to introduce multiple copies. Either method results in an increase in the number of coenzymes encoding phosphoenolpyruvate synthase in the transformed strain, resulting in an increase in phosphoenolpyruvate synthase activity.
  • Enhancement of phosphoenolpyruvate synthase activity can be achieved not only by the gene amplification described above, but also by the expression control sequences such as the promoter of the gene encoding phosphoenolpyruvate synthase on chromosomal DNA or plasmid. It can also be achieved by replacing it with a powerful one. For example, lac promoter, trp promoter evening -, trc promoter one, tac promoter, P R promoter one evening one lambda phage, P L promoter Isseki Chief is known as a powerful promoter evening one. Substitution with these promoters enhances phosphoenol pyruvate synthase activity by enhancing the expression of genes encoding phosphoenol pyruvate synthase.
  • the coryneform bacterium of the present invention is characterized in that, by introducing or amplifying an enzyme gene of another amino acid biosynthetic pathway or glycolytic pathway in addition to the phosphoenol pyruvate synthase activity, the enzyme activity of the coryneform bacterium is increased. May be enhanced.
  • genes that can be used for the production of L-lysine include aspartokinase subunits in which synergistic feedback inhibition by L-lysine and L-threonine has been substantially eliminated.
  • genes that can be used for the production of L-glutamic acid include glycosylated phosphofructokinase (PFK, Japanese Patent Application Laid-Open No. 63-169292), and phosphoenolpyruvine in the anaplerotidic pathway.
  • Acid carboxylase PEPC, JP-A-60-87788, JP-A-62-55089
  • citrate synthase of the TCA cycle CS, JP-A-62-2010 No. 1985, JP-A-63-119968, a.
  • a biotin action inhibitor such as a surfactant to a coryneform bacterium capable of producing L-glutamic acid
  • the biotin action inhibitor in a medium containing an excessive amount of biotin can be added.
  • L-glutamic acid can be produced in the absence of E. coli (see W096 / 06180).
  • An example of such a coryneform bacterium is Brevipacterium 'lactofarmentum AJ13029 described in W096 / 06180.
  • the AJ13029 strain was registered on September 2, 1994 with the Institute of Biotechnology and Industrial Technology, Institute of Industrial Science and Technology, Ministry of International Trade and Industry (zip code 305-8566, 1-3 1-3 Higashi, Tsukuba, Ibaraki, Japan) and the accession number FERM. Deposited as P-14501, transferred to an international deposit under the Budapest Treaty on August 1, 1995, and given accession number FERM BP-5189.
  • the biotin-inhibiting substance can be expressed in a medium containing an excessive amount of biotin.
  • L-Lysine and L-glutamic acid can be produced simultaneously in the absence (see W096 / 06180).
  • Examples of such a strain include Brevibacterium 'Lactofamentum AJ12993 strain described in W096 / 06180. The shares were issued by the Ministry of International Trade and Industry on June 3, 1994. Deposited at the National Institute of Advanced Industrial Science and Technology (Postal Code: 305-8566, 1-3 1-3 Higashi, Tsukuba, Ibaraki, Japan) under the accession number FERM P-14348. It has been transferred to an international deposit under the United Nations Convention and has been assigned the 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 genetic recombination technology 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.
  • L-amino acid When a coryneform bacterium having enhanced phosphoenorubyruvate synthase activity and capable of producing L-amino acid is cultured in a suitable medium, L-amino acid accumulates in the medium. For example, when a coryneform bacterium having enhanced phosphoenolpyruvate synthase activity and capable of producing L-lysine acid is cultured in a suitable medium, L-lysine is accumulated in the medium. In addition, when a coryneform bacterium having enhanced phosphoenol pyruvate synthase activity and having L-gluminic acid producing ability is cultured in a suitable medium, L-gluminic acid accumulates in the medium.
  • L-lysine and L-glucamic acid accumulate in the medium. I do.
  • L-lysine and L-glucaminic acid are simultaneously produced by fermentation, the L-lysine-producing bacterium may be cultured under L-glucaminic acid production conditions or L-lysine-producing ability.
  • a coryneform bacterium having an ability to produce L-glucamic acid may be mixed and cultured (Japanese Patent Application Laid-Open No. 5-37993).
  • the medium used to produce L-amino acids using the microorganism of the present invention is a normal medium containing a carbon source, a nitrogen source, inorganic ions and, if necessary, other organic micronutrients.
  • Carbon sources include glucose, lactose, galactose, fructose, sucrose, molasses, carbohydrates such as starch hydrolysates, alcohols such as ethanolinositol, acetic acid, fumaric acid, and citric acid.
  • organic acids such as succinic acid.
  • Nitrogen sources include ammonium sulfate, ammonium nitrate, ammonium chloride, Inorganic ammonium salts such as ammonium phosphate and ammonium acetate, ammonia, peptone, meat extract, yeast extract, yeast extract, organic nitrogen such as soybean hydrolysate, soybean hydrolyzate, ammonia gas, ammonia water, etc. 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 a vitamin 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 and aeration / agitation cultivation.
  • aerobic conditions such as shaking cultivation and aeration / agitation cultivation.
  • pH adjustment an inorganic or organic acidic or alkaline substance, ammonia gas or the like can be used.
  • the L-amino acid can be collected from the fermentation liquor in the same manner as in the usual method for producing an L-amino acid.
  • L-lysine can be usually carried out by a combination of 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.
  • L-glutamic acid may be adsorbed and separated by an anion exchange resin, or may be neutralized and crystallized.
  • the nucleotide sequence of the pps gene of Escherichia coli has already been elucidated (Mol. Gen. Genet., 231 (2), 332-336 (1992), Genbank / EMBL / DDBJ accession No. M69116). Based on the reported nucleotide sequence, the primers shown in SEQ ID NOs: 1 and 2 in the Sequence Listing were synthesized, and the chromosomal DNA of Escherichia coli 'JM109 strain was type III, and the phosphoenolpyruvate synthase gene was subjected to PCR by PCR. Was amplified.
  • SEQ ID NO: 1 is Genbank / EMBL / DDBJ accession No. It corresponds to the sequence from the first to the 23rd base of the base sequence of the PPS gene described in M69116, and SEQ ID NO: 2 corresponds to the sequence from the 366 to the 3640th base.
  • the chromosome DNA of Escherichia coli JM109 strain was prepared by a conventional method (Bioengineering 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 front line (Takeo Sekiya et al., Edited by Kyoritsu Shuppan, 1989) were used.
  • the purified PCR product is purified by a conventional method, and then ligated with Smal-cleaved plasmid pHC4 using the Reigession Kit (Takara Shuzo). Then, the Escherichia coli KM JM109 Combinent Cell (Takara Shuzo) ) And transformed into L medium containing 30 zg / ml of chloramphenicol (Bacto Tryptone 10 g / L, Pactoist Extract 5 g / L NaCl 5 g / L, Agar 15 g / L, pH 7.2) ), And after overnight culture, appeared white colonies were picked up and separated into single colonies to obtain transformed strains. Plasmid was extracted from the obtained transformant to obtain a plasmid pHC4 pps in which the pps gene was bound to the vector.
  • Escherichia coli harboring pHC4 was named private number AJ12617, and on April 24, 1991, the Institute of Biotechnology and Industrial Technology, Institute of Industrial Science and Technology, Ministry of International Trade and Industry (zip code 305-8566, Ibaraki, Japan) Deposit No. FERM P-12215 at Tsukuba Higashi 1-chome 1-3), transferred to an international deposit based on the Budapest Treaty on August 26, 1991, and given a deposit number FERM BP-35332. ing.
  • the JM109 strain and the JM109 strain retaining pH pps 4 pps were used.
  • the JM109 strain having pHC of 4 pps showed about 15 times the phosphoenolylrubic acid synthase activity of the JM109 strain not having pHC of 4 pps.
  • Cells of the AJ13029 / pHC4pps strain obtained by culturing in a CM2B plate medium containing 5 g / ml chloramphenicol were mixed with L-gluminamine having the following composition containing 5 g / ml chloramphenicol.
  • An acid production medium was inoculated, shake-cultured at 31.5 ° C, and shake-cultured 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 corynebacterium bacterium AJ13029 strain was cultured in the same manner as described above, and a strain transformed with an already obtained corynebacterium bacterium autonomously replicating plasmid pHC4 by the electric pulse method was cultured as described above. .
  • Corynebacterium sp.AJ11082 was used as a control with a plasmid pHC4 that can replicate autonomously with already obtained Corynebacterium sp. Transformation by electric pulse method The transformed strain was cultured as described above.
  • Protein hydrolyzate (bean concentrate) 30 ml
  • Brevibacterium lactofermentum AJ12993 was transformed with plasmid pHC4pps by the electric pulse method (see Japanese Patent Application Laid-Open No. 2-207791) to obtain the resulting transformant.
  • culture for producing L-lysine and L-glucamic acid was performed as follows.
  • the AJ12993 / pHC4pps strain obtained by culturing on a CM2B plate medium containing 5 g / ml chloramphenicol was inoculated into the L-lysine production medium containing Sg / ml chloramphenicol. 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 of Corynebacterium sp. AJ12993 was transformed by an electropulse method with a plasmid PHC4 capable of autonomous replication with a previously obtained Corynebacterium sp., And cultured in the same manner as described above.
  • the ability of coryneform bacteria to produce L-amino acid such as L-lysine or L-glutamic acid can be improved. Also, an efficient method for producing an L-amino acid such as L-lysine or L-glutamic acid is provided.

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Abstract

L'invention concerne une bactérie du type coryne dotée d'une activité phosphoénolpyruvate synthase renforcée dans la cellule et capable de produire des L-aminoacides. Le procédé consiste à cultiver ladite bactérie dans un milieu, ce qui permet de constituer et d'accumuler, dans ledit milieu, des L-aminoacides et, ensuite, de les prélever dudit milieu.
PCT/JP2000/001655 1999-03-19 2000-03-17 Procede de production des l-aminoacides Ceased WO2000056859A1 (fr)

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AU31943/00A AU3194300A (en) 1999-03-19 2000-03-17 Process for producing l-amino acid

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JP7638099 1999-03-19
JP11/76380 1999-03-19
JP22492999 1999-08-09
JP11/224929 1999-08-09

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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
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
EP0877090A1 (fr) * 1995-08-30 1998-11-11 Ajinomoto Co., Inc. Procede de production d'acides amines levogyres

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
EP0841395A1 (fr) * 1995-06-07 1998-05-13 Ajinomoto Co., Inc. Procede de production de l-lysine
EP0877090A1 (fr) * 1995-08-30 1998-11-11 Ajinomoto Co., Inc. Procede de production d'acides amines levogyres
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
NIERSBACH, M. ET. AL.: "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase.", MOLECULAR & GENERAL GENETICS, vol. 231, no. 2, January 1992 (1992-01-01), pages 332 - 336, XP002928861 *

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