• 专利附录
  • 专利说明
  • 权利要求
  • 类似技术
  • 同族专利
  • 引用文献
  • 法律状态
  • 优先权
    • 专利摘要:

    公开号:SU1246897A3
    申请号:SU813375844
    申请日:1981-12-21
    公开日:1986-07-23
    发明作者:Граблей Сузанне；Заубер Клаус
    申请人:Хехст Аг (Фирма)；
    IPC主号:
    专利说明:

    IS
    20
    1, 124689
    The invention relates to the production of amino acids, namely to the method of obtaining L-2-α-4-non-methylphosphonic acid by enzymatic means.
    The aim of the invention is to increase the yield of the isomer of L-phosphinotricin.
    The method is carried out as follows.
    An aqueous solution of the N-arylacetylene derivative of general formula 10 is prepared.
     ABOUT
    and
    SNZ-R-CH 2-CH2-Sh-BN-CO CH-Ag
     HE COOH
    where Ar is phenyl,
    and enzymatic hydrolysis by acylase, which is used as penicillin-C-acylase, derived from Escherichia coli AMCC 11105. Then, after the end of the process, from the resulting mixture consisting of L-2-amino-4-methylphosphine oil Acids (L-FTC), N-phenyl-acetyl-D-2-ammonium-4-methyl-phosphinobutyric acid - (N-phenylacet-1-B-FTC) and phenylacetic acid can be selected for L-FTC that have a high degree of purity.
    Example 1. Take 10 g (33.4 mmol) of K-phenylacetyl-B, L-FTC and suspended in a small amount of double-distilled water. The pH of the suspension is then adjusted by adding 1N. sodium hydroxide solution to 7, 8, after which distilled water is added to obtain 500 mp of solution.
     15 mg of penicillin-C-adylase is added to it as a lyophilisate, derived from Escherichia coli AMCC 11105, and the resulting reaction mixture is kept at room temperature for 40 hours, after which a sample is taken and stained - hydrin content of free amino acids. In this case, a conversion rate of 45 is about 50%. Then the mixture is adjusted to pH 2.0 with concentrated hydrochloric acid. 3.0, filtered, and the resulting clear substrate solution was passed through a 50 column cut, filled with 150 g of Daycata (R) 50 W X 2 (H-form).
    After that, the column is washed. Until it leaves a neutral and chlorine-free eluate, .4 then with a 0.8N solution of hydrogen chloride mixed with ethyl alcohol
    S
    0
    89
    0

    five
    0 5 0
    five
     ..2.
    and the free amino acid in the form of hydrochloride is washed out from the column with water.
    From one stripped off the eluate receive pure hydrochloride TFTC with so pl. 199-200 ° C. The yield is 3.3 g (15.2 mmol) 45.4%).
     From hydrochloride by treatment with propylene oxide, a free crystalline b-amino acid with tlsh is obtained. 217-219 ° and a specific angle of rotation of + 28 °.
    Example 2. Take 60 g (200.5 mm: ol) N-phenylacetyl-D, L-FTC and mixed with a small amount of water. Then the solution of sodium hydroxide is adjusted to a pH of 8.0, then water is added to a volume of 1.0 l of suspension, and mixed with fixed penicillin-C-acylase (activity approximately 80 V / g). The resulting reaction mixture was stirred with 1.5 g, and then the water-insoluble catalyst was separated by filtration. The resulting filtrate is passed through a column filled with 750 g of a strongly acidic cation-exchange resin.
    Further processing of the solution is carried out according to example 1.
    The result is 20 g (92 mmol 46%) of hydrochloride with so pl. 199-201 ° C, specific rotation angle 23.3 ° and molar rotation f 50, 7.
    After treatment of hydrochloride with propylene oxide, the free L-FTP is obtained. 216-217 ° C, the specific angle of rotation + 28.5 ° and molar rotation 1 | and 51.6 °.
    Example 3. For the purpose of studying the stability associated with the penicillin-C-acylase carrier used in Example 2 with respect to N-phenyl-acetic-B b-FTC ,. 100 mg of the fixed enzyme is mixed with 10 ml of a 5% aqueous solution of M-phenyl-acetyl-B, L-FTC (the pH of the suspension is stabilized at 7.8 by adding phosphate buffer). The mixture is stirred at room temperature. After 24 hours, the substrate solution is filtered, the enzyme is separated, and again mixed with the substrate solution.
    The enzyme activity is measured by the content of free FTC after 45 minutes and after 22.5 hours by staining the samples.
    NINGHID ZINOM.
    Significant decrease in stability. associated with a carrier penicillin31246897
    -G-amylase, was not detected after 8 weeks. In each case, after 45 minutes from the start of the reaction, about 20% hydrolyzed, and after 22.5 hours, about 50% calculated on the racemic level used. pH
    050
    nat
    alive
    1M
    50
    Example 4. Collagen membranes are taken to obtain fixed penicillin C-amylase, they are activated by the Kule method, and then moistened with 2 ml of penicillin C-amylase solution containing O, 1 mol of potassium phosphate
    Editor A. Shandor Order 4030/60
    Compiled by M. Andreev
    Tehred G.Gerber Proofreader G. Reshetnik,
    Circulation 490. Subscription VNIZHI State Committee of the USSR
    for inventions and discoveries 113035, Moscow, Zh-35, Raushsk nab., 4/5
    Production and printing company, Uzhgorod, Projecto st., A
    four

    The membranes in this mixture are kept for 4 hours at 4 ° C and then washed.
    pH 8.0, 0.25 mol of acetate wipe, and
    05024% aqueous azide solution
    on three .
    live
    1 M solution of sodium chloride and
    50 mmol kal1ifos fatah buffer (pH
    equal to 7.0).
    The resulting material was reacted in the manner described in npi-mepe 2 with 60 g of N-phenacetyl-D-L-FTC. The result is L-FTC with the same level of optical purity as the L-FTC hydrochloride in example 2.
    权利要求:
    Claims (2)
    [1]
    1 1246897.
    [2]
    2
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    同族专利:
    公开号 | 公开日
    OA06973A|1983-07-31|
    IL64623D0|1982-03-31|
    AU547636B2|1985-10-31|
    PT74188A|1982-01-01|
    AT14597T|1985-08-15|
    DD201907A5|1983-08-17|
    DE3171623D1|1985-09-05|
    PL234314A1|1982-07-05|
    US4389488A|1983-06-21|
    CA1172981A|1984-08-21|
    DK571481A|1982-06-24|
    MA19362A1|1982-07-01|
    BR8108346A|1982-10-13|
    JPS57138394A|1982-08-26|
    CS224638B2|1984-01-16|
    EP0054897A2|1982-06-30|
    ES8207584A1|1982-10-01|
    PT74188B|1983-11-08|
    AU7875181A|1982-07-01|
    EP0054897B1|1985-07-31|
    ZW30581A1|1982-07-14|
    DE3048612A1|1982-07-01|
    IL64623A|1985-04-30|
    JPH0218072B2|1990-04-24|
    EP0054897A3|1982-09-08|
    DE3048612C2|1982-12-02|
    ZA818859B|1982-11-24|
    ES508034A0|1982-10-01|
    HU189552B|1986-07-28|
    引用文献:
    公开号 | 申请日 | 公开日 | 申请人 | 专利标题
    GB1369462A|1971-11-23|1974-10-09|Beecham Group Ltd|Enzymic resolution of racemic n-acyl-dl-amino acids|
    JPS6247520B2|1978-10-02|1987-10-08|Meiji Seika Co|
    US4226941A|1979-09-27|1980-10-07|Meiji Seika Kaisha, Ltd.|Process for the optical resolution of d,l-2-amino-4-methylphosphinobutyric acid|DE3334849A1|1983-09-27|1985-04-04|Hoechst Ag, 6230 Frankfurt|METHOD FOR RACEMIZING OPTICALLY ACTIVE AMINO ACIDS|
    DE3435156A1|1984-09-25|1986-04-03|Boehringer Mannheim Gmbh, 6800 Mannheim|METHOD FOR PRODUCING THE STEREOISOMERS OF 1-AMINO-ALKYLPHOSPHONIC ACIDS OR 1-AMINOALKYLPHOSPHINIC ACIDS|
    DE3724722A1|1987-07-25|1989-02-16|Hoechst Ag|IMPROVED METHOD FOR THE ENZYMATIC PRODUCTION OF L-2-AMINO-4-METHYLPHOSPHINOBUTTERIC ACID|
    DE3817191A1|1988-05-20|1989-11-30|Hoechst Ag|METHOD FOR RACEMIZING OPTICALLY ACTIVE D-2-N-PHENACETYLAMINO-4-METHYLPHOSPHINOBUTTERIC ACID|
    DE3817956A1|1988-05-27|1989-12-07|Hoechst Ag|METHOD FOR THE PRODUCTION OF L-AMINO ACIDS CONTAINING PHOSPHORUS AND ITS ESTERS AND N-DERIVATIVES|
    US5081024A|1988-09-05|1992-01-14|Nissan Chemical Industries, Ltd.|Process for producing optically active amino acids|
    DE3903446A1|1989-02-06|1990-10-18|Hoechst Ag|METHOD FOR ENZYMATICALLY SEPARATING 2-AMINO-4-METHYLPHOSPHINOBUTTERIC ACID DERIVATIVES|
    US5057607A|1990-06-08|1991-10-15|Eli Lilly And Company|Enantiomerically selective biocatalyzed acylation|
    TW353663B|1991-04-06|1999-03-01|Hoechst Ag|Process for the preparation of phosphorus-containing L-amino acids, their derivatives and intermediates for this process|
    DE4422045A1|1994-06-26|1996-01-04|Hoechst Schering Agrevo Gmbh|Process for the enzymatic cleavage of 2-amino-4-methylphosphinobutanoic acid derivatives|
    AT497538T|2002-02-26|2011-02-15|Syngenta Ltd|METHOD FOR THE SELECTIVE MANUFACTURE OF MALE OR FEMALE-STERILE PLANTS|
    CN110343676B|2018-04-03|2020-06-23|上海弈柯莱生物医药科技有限公司|L-glutamate dehydrogenase mutant and application thereof|
    CN108484665B|2018-04-16|2020-06-23|浙江工业大学|Method for separating and extracting L-glufosinate-ammonium from enzyme conversion solution|
    CN111979208A|2019-05-23|2020-11-24|弈柯莱生物科技股份有限公司|L-glutamate dehydrogenase mutant and application thereof|
    CN110343734B|2019-06-14|2021-03-23|浙江工业大学|L-glufosinate-ammonium chemoenzymatic production method|
    法律状态:
    优先权:
    申请号 | 申请日 | 专利标题
    DE3048612A|DE3048612C2|1980-12-23|1980-12-23|"Process for the enzymatic separation of L-2-Ami no-4-methylphosphinobutyric acid"|
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