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WO1994001577A1 - Procede de production d'un d-aminoacide optiquement actif - Google Patents

Procede de production d'un d-aminoacide optiquement actif Download PDF

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Publication number
WO1994001577A1
WO1994001577A1 PCT/JP1993/000910 JP9300910W WO9401577A1 WO 1994001577 A1 WO1994001577 A1 WO 1994001577A1 JP 9300910 W JP9300910 W JP 9300910W WO 9401577 A1 WO9401577 A1 WO 9401577A1
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WO
WIPO (PCT)
Prior art keywords
group
amino acid
substituted
substituted carbonyl
benzoyl
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/JP1993/000910
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English (en)
Japanese (ja)
Inventor
Michito Tagawa
Eiko Okamoto
Sachiko Akutsu
Masao Kuwahara
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Research Association for Biotechnology of Agricultural Chemicals
Original Assignee
Research Association for Biotechnology of Agricultural Chemicals
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Research Association for Biotechnology of Agricultural Chemicals filed Critical Research Association for Biotechnology of Agricultural Chemicals
Publication of WO1994001577A1 publication Critical patent/WO1994001577A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • 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
    • C12P41/00—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture
    • C12P41/006—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by reactions involving C-N bonds, e.g. nitriles, amides, hydantoins, carbamates, lactames, transamination reactions, or keto group formation from racemic mixtures
    • C12P41/007—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by reactions involving C-N bonds, e.g. nitriles, amides, hydantoins, carbamates, lactames, transamination reactions, or keto group formation from racemic mixtures by reactions involving acyl derivatives of racemic amines

Definitions

  • D-Phenylalanine has recently attracted attention as a raw material for the synthesis of analgesics and antibiotics.
  • Miyahara et al. Have recently disclosed a separation method (Japanese Patent Laid-Open No. 63-91097, Mitsui Toatsu Co., Ltd.).
  • D-acylase of phenylalanine There are few reports on D-acylase of phenylalanine.
  • D-aminoacylase activity has been reported for each strain of the genera Pseudomonas, Alcaligenes, and Streptomyces. et al; Appl. Environ. Microbiol. 54 984 (1988). M. Moriguchi, K. Ikeda; ibid. 54 2767 (1988), K. Kubo, et. Al; Agri c. Biol. Chem. 42 107 (1987), i bid. 44 1089 (1980)). However, since all of them have weak activities and also retain high aminoacylase activity, it is considered that few D-aminoacylase-producing strains produce only highly active D-forms. Disclosure of the invention
  • mutations can be generated in these strains to obtain strains with higher productivity.
  • the enzyme-producing strain of the present invention can also be artificially created.
  • microbiological properties of these microorganisms are as follows.
  • Rhodococcus rhodochrous 2 0 3 0-2 (Rhodococcus rhodochrous 2 0 3 0-2) strain
  • Glycolyl test I (Acetyl type) Cell wall sugar composition
  • strain 1 589-8-1 When the mycological properties of the strain 1 589-8-1 are compared with the descriptions in Purged's' Manual of 'Systematic' and 'Bacterial mouth', the cultivation properties, physiological properties and acid production from saccharides From the characteristics and the like of the strain, 158 9 — 1 strain is recognized as a strain belonging to the species of Pimelopactor simplex. This strain is available from the National Institute of Advanced Industrial Science and Technology
  • microorganism strain that can be used in the present invention is not limited to the above examples.
  • Culture of the microorganism used in the present invention is usually performed under aerobic conditions such as shaking culture or submerged aeration and stirring.
  • the culture temperature is 20 to 37, and the culture pH is 6 to 9 for 1 to 7 days.
  • the culture medium contains carbon sources, nitrogen sources, inorganic salts and trace organic nutrients that the bacteria used can utilize. That is, glucose, maltose, starch hydrolysate, carbohydrates such as molasses can be used as the carbon source, and various inorganic and organic ammonium salts or meat extracts such as ammonia, ammonium sulfate, ammonium chloride, etc. can be used as the nitrogen source. Natural organic nitrogen sources such as yeast extract, polypeptone, corn steep liquor, and casein hydrolyzate can also be used.
  • a ruponyl group-degrading enzyme for example, desacyl group enzyme
  • enzymes can be purified from cultured cells by appropriately combining known methods, and enzyme preparations having different degrees of purification can be used.
  • the displacing enzyme eg, desacylase
  • the cultured cells, the treated cells, or enzyme preparations having different degrees of purification are immobilized on a carrier by a known method and used for the reaction.
  • the concentration of the N-substituted carbonyl-D-amino acid and / or its salt represented by the general formula [I] to be used as the substrate of the present invention is not limited, but it is usually used at 0.05 to 20%. .
  • the reaction temperature is 1 0 ⁇ 6 0 e C, preferably at 2 0-5 0.
  • the reaction is carried out at a pH of from 4 to 10 and preferably from 6 to 9 for 0.5 to 24 hours.
  • D-amino acid and N-substituted carbonyl-amino acid from the reaction solution, for example, a direct crystallization method by concentration, isoelectric point precipitation, or the like, It can be performed by a known method such as on-exchange resin treatment and membrane separation, and the qualitative and quantitative determination of the generated D-amino acid can be performed by thin-layer chromatography or high-performance liquid chromatography.
  • Optical isomers can be identified by optical rotation analysis or high performance liquid chromatography using an optical isomer separation column.
  • the unreacted N-substituted carbonyl-amino acid can be chemically racemized by a conventional method and then subjected to the above reaction again.
  • D-amino acids and N— which are optically active substances are obtained from N-substituted carbonyl-DL-amino acids and salts thereof which can be easily chemically synthesized by performing an amide carbonyl reaction.
  • Substituted carboamino acids can be selectively produced in a simple process under mild conditions
  • the substituted carbonyl group-degrading enzyme used in the present invention efficiently decomposes only the substituted carbonyl group of the D-form of N-substituted carbonyl form such as parin, methionine, phenylalanine, etc., and has high optical purity of D-amino acid.
  • Rhodococcus' mouth Dokuros 2 0 3 0-2 strain is inoculated with a platinum loop into a ⁇ 18 mm test tube containing 5 ml of culture medium with the following composition. With shaking for 48-72 hours
  • Pimerobacter simplex 1 595--1 strain was inoculated into a ⁇ 18 mm test tube containing 5 ml of the following culture medium in a platinum loop and shake-cultured at 25 ° C for 48 to 72 hours. did.
  • the culture was performed according to the above procedure except that the culture temperature was 30 and the culture time was 72 hours.
  • the results measured according to the analysis conditions described in Example 2 are as follows.
  • the amide carbonyl reaction The optically active form of D-amino acid and N-substituted L-amino is derived from N-substituted carbonyl-D-amino acid and Z or a salt thereof, which can be easily chemically synthesized by performing The acid can be selectively produced in a simple process and under mild conditions.
  • substituted carbonyl group degrading enzyme used in the present invention efficiently decomposes only the substituted carbonyl group of the D-substituted N-substituted carbonyl compound such as parin, methionine, and phenylalanine, and has a high optical purity. Produces amic acid.

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Analytical Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

Un procédé de production d'un D-aminoacide et d'un N-(carbonyle substitué)-L-aminoacide par hydrolyse microbienne d'un N-(carbonyle substitué)-DL-aminoacide, ledit procedé consistant à effectuer une résolution optique se faisant par traitement d'un N-(carbonyle substitué)-DL-aminoacide répondant à la formule générale [1] et/ou un sel dudit acide avec une cellule de culture d'une bactérie choisie dans les espèces Rhodococcus et Pimelobacter. L'invention concerne également un produit de traitement obtenu selon ce procédé. Dans ladite formule, R représente hydrogène ou alkyle C1-C10 éventuellement halogéné ou phényle; et R1 représente alcanoyle C¿1?-C10 éventuellement halogéné ou benzoyle.
PCT/JP1993/000910 1992-07-03 1993-07-02 Procede de production d'un d-aminoacide optiquement actif Ceased WO1994001577A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP4/200324 1992-07-03
JP20032492A JPH0622789A (ja) 1992-07-03 1992-07-03 光学活性なｄ−アミノ酸の製造法

Publications (1)

Publication Number Publication Date
WO1994001577A1 true WO1994001577A1 (fr) 1994-01-20

Family

ID=16422407

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/JP1993/000910 Ceased WO1994001577A1 (fr) 1992-07-03 1993-07-02 Procede de production d'un d-aminoacide optiquement actif

Country Status (2)

Country Link
JP (1) JPH0622789A (fr)
WO (1) WO1994001577A1 (fr)

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8598685B2 (en) 2009-09-04 2013-12-03 Sumitomo Electric Industries, Ltd. GaN single crystal substrate and method of manufacturing thereof and GaN-based semiconductor device and method of manufacturing thereof

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS645488A (en) * 1987-06-29 1989-01-10 Daicel Chem Novel d-aminoacylase and production thereof
JPH02234677A (ja) * 1989-03-07 1990-09-17 Dai Ichi Pure Chem Co Ltd 酸性ｄ―アミノ酸に作用するｄ―アミノアシラーゼ及びその製造法
JPH0394696A (ja) * 1988-09-05 1991-04-19 Nissan Chem Ind Ltd 光学活性体の製造方法

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS645488A (en) * 1987-06-29 1989-01-10 Daicel Chem Novel d-aminoacylase and production thereof
JPH0394696A (ja) * 1988-09-05 1991-04-19 Nissan Chem Ind Ltd 光学活性体の製造方法
JPH02234677A (ja) * 1989-03-07 1990-09-17 Dai Ichi Pure Chem Co Ltd 酸性ｄ―アミノ酸に作用するｄ―アミノアシラーゼ及びその製造法

Also Published As

Publication number Publication date
JPH0622789A (ja) 1994-02-01

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