CN109384811B - Preparation method of L-glufosinate-ammonium - Google Patents
Preparation method of L-glufosinate-ammonium Download PDFInfo
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- 238000002360 preparation method Methods 0.000 title claims description 6
- 238000000034 method Methods 0.000 claims abstract description 29
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims abstract description 13
- 102000004879 Racemases and epimerases Human genes 0.000 claims abstract description 12
- 108090001066 Racemases and epimerases Proteins 0.000 claims abstract description 12
- -1 glufosinate-ammonium amide Chemical class 0.000 claims abstract description 11
- 108010024026 Nitrile hydratase Proteins 0.000 claims abstract description 10
- 102000004190 Enzymes Human genes 0.000 claims abstract description 6
- 108090000790 Enzymes Proteins 0.000 claims abstract description 6
- 230000003301 hydrolyzing effect Effects 0.000 claims abstract description 5
- 238000006460 hydrolysis reaction Methods 0.000 claims abstract description 4
- NGVDGCNFYWLIFO-UHFFFAOYSA-N pyridoxal 5'-phosphate Chemical compound CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O NGVDGCNFYWLIFO-UHFFFAOYSA-N 0.000 claims description 12
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical group OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 claims description 7
- 235000007682 pyridoxal 5'-phosphate Nutrition 0.000 claims description 6
- 239000011589 pyridoxal 5'-phosphate Substances 0.000 claims description 6
- 229960001327 pyridoxal phosphate Drugs 0.000 claims description 6
- 239000005515 coenzyme Substances 0.000 claims description 3
- 125000004108 n-butyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 claims description 3
- 125000004169 (C1-C6) alkyl group Chemical group 0.000 claims description 2
- 239000008346 aqueous phase Substances 0.000 claims description 2
- 125000003118 aryl group Chemical group 0.000 claims description 2
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 claims description 2
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 2
- IAJOBQBIJHVGMQ-UHFFFAOYSA-N 2-amino-4-[hydroxy(methyl)phosphoryl]butanoic acid Chemical compound CP(O)(=O)CCC(N)C(O)=O IAJOBQBIJHVGMQ-UHFFFAOYSA-N 0.000 abstract description 20
- 230000008569 process Effects 0.000 abstract description 7
- 230000009471 action Effects 0.000 abstract description 6
- 238000005580 one pot reaction Methods 0.000 abstract description 4
- 230000007062 hydrolysis Effects 0.000 abstract description 3
- 230000006340 racemization Effects 0.000 abstract description 2
- 238000006243 chemical reaction Methods 0.000 description 24
- 239000000543 intermediate Substances 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 11
- 230000000694 effects Effects 0.000 description 9
- IAJOBQBIJHVGMQ-BYPYZUCNSA-N glufosinate-P Chemical compound CP(O)(=O)CC[C@H](N)C(O)=O IAJOBQBIJHVGMQ-BYPYZUCNSA-N 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- LOUPRKONTZGTKE-WZBLMQSHSA-N Quinine Chemical compound C([C@H]([C@H](C1)C=C)C2)C[N@@]1[C@@H]2[C@H](O)C1=CC=NC2=CC=C(OC)C=C21 LOUPRKONTZGTKE-WZBLMQSHSA-N 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 239000004009 herbicide Substances 0.000 description 4
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 3
- LOUPRKONTZGTKE-UHFFFAOYSA-N cinchonine Natural products C1C(C(C2)C=C)CCN2C1C(O)C1=CC=NC2=CC=C(OC)C=C21 LOUPRKONTZGTKE-UHFFFAOYSA-N 0.000 description 3
- 230000002363 herbicidal effect Effects 0.000 description 3
- 239000003456 ion exchange resin Substances 0.000 description 3
- 229920003303 ion-exchange polymer Polymers 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 235000001258 Cinchona calisaya Nutrition 0.000 description 2
- 239000005561 Glufosinate Substances 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 102000003929 Transaminases Human genes 0.000 description 2
- 108090000340 Transaminases Proteins 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000003444 phase transfer catalyst Substances 0.000 description 2
- 229960000948 quinine Drugs 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- IAJOBQBIJHVGMQ-SCSAIBSYSA-N (2R)-glufosinate Chemical compound C[P@@](O)(=O)CC[C@@H](N)C(O)=O IAJOBQBIJHVGMQ-SCSAIBSYSA-N 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241001147838 Paenarthrobacter nicotinovorans Species 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000011914 asymmetric synthesis Methods 0.000 description 1
- 238000010364 biochemical engineering Methods 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- KMPWYEUPVWOPIM-UHFFFAOYSA-N cinchonidine Natural products C1=CC=C2C(C(C3N4CCC(C(C4)C=C)C3)O)=CC=NC2=C1 KMPWYEUPVWOPIM-UHFFFAOYSA-N 0.000 description 1
- KMPWYEUPVWOPIM-LSOMNZGLSA-N cinchonine Chemical compound C1=CC=C2C([C@@H]([C@H]3N4CC[C@H]([C@H](C4)C=C)C3)O)=CC=NC2=C1 KMPWYEUPVWOPIM-LSOMNZGLSA-N 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 231100000053 low toxicity Toxicity 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000007040 multi-step synthesis reaction Methods 0.000 description 1
- 229910000510 noble metal Inorganic materials 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 150000003242 quaternary ammonium salts Chemical class 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07F—ACYCLIC, CARBOCYCLIC OR HETEROCYCLIC COMPOUNDS CONTAINING ELEMENTS OTHER THAN CARBON, HYDROGEN, HALOGEN, OXYGEN, NITROGEN, SULFUR, SELENIUM OR TELLURIUM
- C07F9/00—Compounds containing elements of Groups 5 or 15 of the Periodic Table
- C07F9/02—Phosphorus compounds
- C07F9/28—Phosphorus compounds with one or more P—C bonds
- C07F9/30—Phosphinic acids [R2P(=O)(OH)]; Thiophosphinic acids ; [R2P(=X1)(X2H) (X1, X2 are each independently O, S or Se)]
- C07F9/301—Acyclic saturated acids which can have further substituents on alkyl
-
- 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
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/55—Design of synthesis routes, e.g. reducing the use of auxiliary or protecting groups
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- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
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- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses a method for catalyzing and hydrolyzing cheap and easily-obtained glufosinate-ammonium intermediate by using biological enzyme to obtain single-configuration L-glufosinate-ammonium in one pot. The hydrolysis process comprises the following specific steps: under the action of non-selective nitrile hydratase, racemic glufosinate-ammonium intermediate is subjected to racemization to obtain glufosinate-ammonium amide racemate; step two: and (3) selectively hydrolyzing the L-type glufosinate-ammonium amide intermediate by using L-amidohydrolase to obtain L-type glufosinate-ammonium, and racemizing the unhydrolyzed D-type glufosinate-ammonium amide intermediate under the action of ACL racemase to continuously convert the unhydrolyzed D-type glufosinate-ammonium amide intermediate into the L-type glufosinate-ammonium intermediate. The single L-type glufosinate-ammonium is finally obtained through the DKR process; step three: l-type glufosinate-ammonium is hydrolyzed under the action of dilute hydrochloric acid to obtain L-glufosinate-ammonium.
Description
Technical Field
The invention belongs to the technical field of biological pharmacy and biochemical engineering, and particularly relates to a preparation method of L-glufosinate-ammonium.
Background
Glufosinate-ammonium was developed successfully in 80 s by Herst company, belongs to phosphonic acid herbicides, is a glutamine synthesis inhibitor, is a biocidal contact herbicide, is a broad-spectrum, low-toxicity and non-selective herbicide, is also a herbicide tolerant to second transgenic crops in the world, and has a very wide application prospect.
Currently, glufosinate-ammonium is generally marketed as a racemic mixture. If the glufosinate product can be used as a pure optical isomer of the L-configuration (formula)
) The using amount of the glufosinate-ammonium can be reduced by 50%, and the method has great significance for improving atom economy, reducing using cost and relieving environmental pressure.
Currently, the following methods are mainly used for the synthesis of L-glufosinate-ammonium.
Resolution of racemate
1. Chemical resolution
Hoechst corporation (US5767309) resolved racemic glufosinate using quinine as a chiral resolving agent. The process needs to use expensive chiral resolving agent quinine, and the theoretical yield of the resolution is only 50%, so that the industrial value of the route is lower; in addition, the steps of resolution are very complicated, and the steps of salification, induced crystallization, salt dissolution and the like are required, so that great inconvenience is brought to industrial production;
2. biological resolution
Chinese patent (CN104558033A) reports the preparation of optically pure L-glufosinate by selective hydrolysis of racemic glufosinate-N-carboxylic anhydride with an arthrobacter nicotinovorans ester hydrolase. Although the method can obtain optically pure L-glufosinate-ammonium, the total yield is low, so that the industrial value is low. The reaction equation is as follows:
(II) asymmetric Synthesis
1. Japanese scientists reported in 1991 (J. org. chem,1991,56, 1783-:
this method has several disadvantages: part of intermediates have strong water solubility and are difficult to separate and purify; the asymmetric reduction of the double bond requires expensive noble metals and ligands, which is uneconomical; the product has low enantioselectivity (only 84% ee) and the overall yield of the reaction is low (only 26.7%). Therefore, the industrial application of this method is difficult.
2. Chinese patent (CN105603015A) reports that L-glufosinate-ammonium is prepared by biological transaminase catalysis, and the general reaction equation is as follows:
this method has several disadvantages: substrate synthesis is difficult, and the reaction requires a plurality of cofactors such as transaminase, coenzyme and amine donor, and is not advantageous in cost.
3. Chinese patent (CN104558033A) reports that addition of methyl ethyl phenyl phosphonate and benzylidene glycine is catalyzed by a chiral phase transfer catalyst (cinchonine chiral quaternary ammonium salt derivative). The adduct is hydrolyzed by hydrochloric acid to obtain L-glufosinate-ammonium, and the total reaction equation is as follows:
the method needs a large amount of chiral phase transfer catalysts with high price, and has low total yield of reaction, higher total cost and no industrialized application prospect.
And (III) starting from chiral amino acid, and preparing the L-glufosinate-ammonium through multi-step synthesis.
In 1996 (Chinese Chemical Letters,2006,17,177-179) it was reported that L-glufosinate was prepared by a multistep Chemical synthesis starting from methionine, the general reaction equation of which is as follows:
the method needs expensive methionine as a starting material, and has the advantages of long reaction synthesis route, low total yield, high cost and no industrial application prospect.
Disclosure of Invention
Aiming at the defects of the prior art, the invention provides a simple and feasible novel method for synthesizing L-glufosinate-ammonium, and the chiral L-glufosinate-ammonium has the following structural formula:
the invention discloses a method for catalyzing and hydrolyzing cheap and easily-obtained glufosinate-ammonium intermediate by using biological enzyme to obtain single-configuration L-glufosinate-ammonium by one-pot reaction, which has the following reaction formula:
the intermediate is reacted with a catalyst
In the aqueous phase, the enzyme is catalyzed to obtain
Optionally re-hydrolyzing (when R is not H), and one-pot reacting to obtain L-glufosinate-ammonium
Wherein R is selected from H or a phosphonic acid protecting group.
The above hydrolysis process involves a Dynamic Kinetic Resolution (DKR) process, the reaction formula is as follows:
specifically, the method comprises the following steps:
the method comprises the following steps: under the action of non-selective nitrile hydratase, racemic glufosinate-ammonium intermediate is subjected to racemization to obtain glufosinate-ammonium amide racemate;
step two: and (3) selectively hydrolyzing the L-type glufosinate-ammonium amide intermediate by using L-amidohydrolase to obtain L-type glufosinate-ammonium, and racemizing the unhydrolyzed D-type glufosinate-ammonium amide intermediate under the action of ACL racemase to continuously convert the unhydrolyzed D-type glufosinate-ammonium amide intermediate into the L-type glufosinate-ammonium intermediate. The single L-type glufosinate-ammonium is finally obtained through the DKR process;
step three: l-type glufosinate-ammonium is hydrolyzed under the action of dilute hydrochloric acid to obtain L-glufosinate-ammonium.
The process of the present invention finally enables L-glufosinate to be obtained in an overall yield of up to 87% with an enantioselectivity (Ee) of 98%.
Wherein Ee is L-glufosinate/[ L-glufosinate + D-glufosinate ].
In the above reaction, the phosphonic acid protecting group is selected from C1-C6 alkyl and aryl, preferably ethyl, n-butyl and phenyl.
Preferably, pyridoxal phosphate is added as a coenzyme of ACL racemase during the reaction;
preferably, the enzymes are added in the order nitrile hydratase, L-amidohydrolase and ACL racemase, or pyridoxal phosphate, nitrile hydratase, L-amidohydrolase and ACL racemase;
preferably, the nitrile hydratase is available from Suzhou navigation Biotechnology Ltd under the product number YH 1603;
preferably, the ACL racemase is purchased from suzhou pilotage biotechnology limited under the product number YH 1507;
preferably, the L-amidohydrolase is obtained from Suzhou pilotage Biotech, Inc. under the product number YH 1411;
the preparation method is simple to operate, is a continuous one-pot reaction, and does not need to separate any intermediate; the method is carried out in a water phase, does not need any organic solvent, and is very green and environment-friendly. In addition, the method greatly reduces the production cost and is easy to realize industrialization.
Detailed Description
The present invention will be described in further detail with reference to examples, but is not limited thereto.
It should be noted that the chiral L-glufosinate-ammonium described in examples 1-3 has the following structural formula:
the reaction path is as follows:
example 1 (R ═ Et)
Intermediate glufosinate-ammonium 760mg (4mmol) was dissolved in 40ml of pbs buffer (0.2M, pH 8.0). To the reaction solution were added pyridoxal phosphate 20mg, nitrile hydratase 50mg (purchased from suzhou piloting biotechnology limited, product No. YH1603, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, L-amidohydrolase 38mg (purchased from suzhou piloting biotechnology limited, product No. YH1411, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, and ACL racemase 76mg (purchased from suzhou piloting biotechnology limited, product No. YH1507, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, in this order. After the addition, the temperature of the system was raised to 30 ℃ and the reaction was completed after 8 hours. 20ml of concentrated hydrochloric acid was added to the reaction system, and the mixture was refluxed for 1 hour. After the reaction, the aqueous hydrochloric acid solution was concentrated to dryness and purified by ion exchange resin to obtain 629mg of L-glufosinate-ammonium in 87% yield and Ee 98%.
Example 2 (R ═ n-Bu)
Intermediate 872mg (4mmol) of glufosinate-ammonium was dissolved in 40ml of a solution of pbs buffer (0.2M, pH 8.0). To the reaction solution were added pyridoxal phosphate 20mg, nitrile hydratase 50mg (purchased from suzhou piloting biotechnology limited, product No. YH1603, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, L-amidohydrolase 38mg (purchased from suzhou piloting biotechnology limited, product No. YH1411, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, and ACL racemase 87mg (purchased from suzhou piloting biotechnology limited, product No. YH1507, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, in this order. After the addition, the temperature of the system was raised to 30 ℃ and the reaction was completed after 8 hours. 20ml of concentrated hydrochloric acid was added to the reaction system, and the mixture was refluxed for 1 hour. After the reaction, the aqueous solution of hydrochloric acid was concentrated to dryness and purified by ion exchange resin to obtain 593mg of L-glufosinate-ammonium with a yield of 82% and Ee 97%.
Example 3 (R ═ H)
The intermediate glufosinate-ammonium 648mg (4mmol) was dissolved in 40ml of pbs buffer (0.2M, pH 8.0). To the reaction solution were added pyridoxal phosphate 20mg, nitrile hydratase 50mg (purchased from suzhou piloting biotechnology limited, product No. YH1603, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, L-amidohydrolase 38mg (purchased from suzhou piloting biotechnology limited, product No. YH1411, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, and ACL racemase 65mg (purchased from suzhou piloting biotechnology limited, product No. YH1507, only one of which was given here to illustrate the effects of the present invention) dissolved in 1ml of water, in this order. After the addition, the temperature of the system was raised to 30 ℃ and the reaction was completed after 8 hours. After the reaction, the aqueous solution was concentrated to dryness and purified by ion exchange resin to obtain 513mg of L-glufosinate-ammonium with a yield of 71% and Ee 95%.
It is to be understood that the above examples are illustrative only for the purpose of clarity of description and are not intended to limit the embodiments. Other variations and modifications will be apparent to persons skilled in the art in light of the above description. It is not necessary or necessary to exhaustively enumerate all embodiments herein, and obvious variations or modifications can be made without departing from the scope of the invention.
Claims (8)
1. A preparation method of L-glufosinate-ammonium is characterized in that an intermediate is prepared
In the aqueous phase, the enzyme is catalyzed to obtain
Optionally hydrolyzing again, and making into L-glufosinate-ammonium
Wherein R is selected from H or a phosphonate protecting group, including nitrile hydratase, L-amidohydrolase, and ACL racemase.
2. The method of claim 1, wherein the phosphonic acid protecting group is selected from the group consisting of C1-C6 alkyl and aryl.
3. The phosphonic acid group-protecting group according to claim 2, characterized in that said phosphonic acid group-protecting group is selected from ethyl, n-butyl, phenyl.
4. The method according to claim 1, wherein the enzyme further comprises pyridoxal phosphate, a coenzyme for ACL racemase.
5. The method of claim 1, wherein the nitrile hydratase is available from Soviea Biotech, Inc. under the reference YH 1603.
6. The method of claim 1, wherein the L-amidohydrolase is obtained from Soviea pilot Biotech, Inc. under the reference YH 1411.
7. The method of claim 1, wherein the ACL racemase is available from suzhou piloting biotechnology limited under the reference YH 1507.
8. The method of claim 1, wherein the hydrolysis reaction is carried out in a dilute hydrochloric acid solution.
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| CN112391438B (en) * | 2019-08-13 | 2023-01-13 | 四川利尔生物科技有限公司 | Production method of L-glufosinate-ammonium or salt thereof |
| CN113462730B (en) * | 2020-03-31 | 2023-08-25 | 江苏扬农化工股份有限公司 | Method for preparing L-glufosinate-ammonium by double enzyme-linked method |
| EP4063374A4 (en) * | 2020-10-14 | 2023-09-27 | Lier Chemical Co., Ltd. | Method for preparing l-glufosinate |
| CN112940031B (en) * | 2021-02-01 | 2022-08-02 | 河北威远生物化工有限公司 | N-naphthyl-acetyl-glufosinate-ammonium, synthesis method thereof and synthesis method for synthesizing L-glufosinate-ammonium by using N-naphthyl-acetyl-glufosinate-ammonium |
| CA3240868A1 (en) * | 2021-12-13 | 2023-06-22 | Lei Zhou | L-glufosinate derivative, composition comprising same, preparation method therefor and use thereof |
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|---|---|---|---|---|
| US5618728A (en) * | 1994-06-26 | 1997-04-08 | Hoechst Schering Agrevo Gmbh | Process for the enzymatic cleavage of 2-amino-4-methyl-phosphinobutyramide derivatives |
| CN103275896A (en) * | 2013-05-27 | 2013-09-04 | 浙江工业大学 | Bacillus cereus and application for Bacillus cereus in preparation for L-glufosinate via microbial transformation |
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