WO2010098629A2 - 메칠머캅탄과 디메칠설파이드의 혼합물을 사용하여 메치오닌 생산능을 증가시키는 방법 - Google Patents
메칠머캅탄과 디메칠설파이드의 혼합물을 사용하여 메치오닌 생산능을 증가시키는 방법 Download PDFInfo
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- WO2010098629A2 WO2010098629A2 PCT/KR2010/001250 KR2010001250W WO2010098629A2 WO 2010098629 A2 WO2010098629 A2 WO 2010098629A2 KR 2010001250 W KR2010001250 W KR 2010001250W WO 2010098629 A2 WO2010098629 A2 WO 2010098629A2
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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
- C12P13/12—Methionine; Cysteine; Cystine
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- the present invention relates to a method for enhancing the L-methionine and organic acid production efficiency.
- Methionine is one of the essential amino acids in vivo and is widely used in feed and food additives. It is also used as a synthetic raw material for fluids and pharmaceuticals. Methionine acts as a precursor to compounds such as choline (lecithin) and creatine, and is also used as a synthetic material for cysteine and taurine. It also serves to provide sulfur. S-adenosyl-methionine is derived from L-methionine and serves to provide methylation in vivo and is involved in the synthesis of various neurotransmitters in the brain.
- Methionine and / or S-adenosyl-L-methionine play a variety of roles in vivo, such as inhibiting fat accumulation in the liver and arteries and alleviating depression, inflammation, liver disease, myalgia (Jeon BR et al. , J Hepatol. , 2001 Mar; 34 (3): 395-401).
- the chemical synthesis of methionine utilizes a method of producing L-methionine through the reaction of hydrolyzing 5- ( ⁇ -methylmercaptoethyl) hydantoin (5- ( ⁇ -methylmercaptoethyl) -hydantoin).
- methionine produced through such chemical synthesis has a disadvantage that L- and D-forms are produced in a mixed form. Accordingly, the present inventors have developed a technology for selectively producing L-methionine using a biological method and have applied for a patent (WO2008 / 013432).
- This method is simply named as a two-stage process and consists of a process for producing L-methionine precursor by fermentation and a process for converting the L-methionine precursor to L-methionine by an enzyme.
- the L-methionine precursor preferably includes O-acetylhomoserine and O-succinyl homoserine.
- the succinic acid is used as a raw material for paints, cosmetics, and medicines, and acetic acid is very useful industrially, such as in the preparation of vinyl acetate, dyeing, aspirin and other medicines and photographic fixatives.
- the enzyme conversion process of the two-step process uses an enzyme having the activity of cystathionine gamma synthase, O-succinyl homoserine sulfidylase and O-acetylhomoserine sulfidylase, and O- which is a precursor of L-methionine.
- L-methionine and organic acids are produced by enzymatic reaction of acetyl homoserine or O-succinyl homoserine with methylmercaptan.
- Methylmercaptan exists as a gas at room temperature, is insoluble in water, and has a high solubility in alkaline solution. Since the enzymatic conversion reaction for producing L-methionine occurs in aqueous solution, it is expected that the methylmercaptan can have a higher solubility in aqueous solution, thereby greatly improving methionine productivity.
- the present inventors have made efforts to find a method for increasing the solubility of methylmercaptan in the enzymatic conversion process in order to maximize L-methionine productivity.
- the mixed methylmercaptan and dimethyl are mixed in an appropriate ratio.
- the present invention was completed by improving the conversion of L-methionine and organic acid from L-methionine precursor by using a sulfide mixed solution, and confirming that L-methionine can be produced at a higher yield than the conventional method.
- An object of the present invention is to add methionine by adding another sulfur compound dimethylsulfide to the methylmercaptan, a sulfur compound, used as a substrate in an enzymatic conversion reaction using O-acetyl homoserine or O-succinyl homoserine, which is a precursor of L-methionine. It is to provide a method for improving the conversion rate.
- the present invention is an aspect
- reaction solution comprising a mixed solution of methylmercaptan and dimethylsulfide and an enzyme converting the methionine precursor to methionine, O-acetyl homoserine or O-succinyl homoserine, which is a methionine precursor, and
- two-stage process refers to one step of producing O-acetyl homoserine or O-succinyl homoserine through glucose fermentation using a fermentation strain prepared by the method disclosed in WO2008 / 013432; It refers to a method for producing L-methionine comprising two steps of producing L-methionine by converting the O-acetyl homoserine or O-succinyl homoserine with methylmercaptan to convert the enzyme into a methionine.
- the present invention in one aspect,
- methionine precursor O-acetyl homoserine or O-succinyl homoserine; A conversion enzyme that converts the methionine precursor to methionine; And preparing a reaction solution including a mixed solution of methylmercaptan and dimethyl sulfide; And,
- Stirring in step 2) may be performed at 500 to 1000 rpm, preferably 600 to 900 rpm, more preferably 700 to 800 rpm.
- the method of the present invention may further comprise the step of terminating the enzyme conversion reaction, in the specific embodiment of the present invention was terminated by treatment with 2N HCl.
- the method of the present invention may further comprise the step of purifying the methionine present in the reaction solution.
- the methionine purification process may include 1) separating the cells from the enzyme conversion reaction solution, 2) decolorizing and filtering the reaction solution from which the cells are separated, and 3) crystallizing the filtrate. .
- Separating the cells may be performed using a high speed centrifuge or a membrane filter.
- Decolorizing / filtering the reaction solution from which the cells are separated may use activated carbon, but is not limited thereto.
- the present inventors attempted to increase the reactivity of methylmercaptan by adding a third substance to the reaction solution containing methylmercaptan. As a result, in the present invention, it was confirmed that the conversion efficiency was increased when the reaction was induced by partially mixing dimethylsulfide (DMS: Dimethylsulfide) with methylmercaptan as a third substance.
- DMS dimethylsulfide
- the conversion reaction was not performed with dimethylsulfide alone, but by mixing dimethylsulfide with methylmercaptan, it was confirmed that the conversion was increased compared to the case where methylmercaptan was used alone (Table 1, Table 4 and FIG. 2). In addition, it was confirmed that the reaction rate of the enzyme was also faster than the case of using methylmercaptan alone as the pH drop rate by acetic acid, which is a byproduct produced by mixing with dimethyl sulfide (see FIG. 1). In addition, the conversion rate was increased while continuously supplying the mixed solution (see Table 2), or even when the culture scale was changed to a large size, and the conversion rate was increased compared with the case of supplying alone (see Table 3). Thus, the method of the present invention may be usefully used to improve the conversion rate from O-acetyl homoserine or O-succinyl homoserine to L-methionine.
- the conversion reaction from methionine precursor to methionine using an enzyme having methionine conversion activity is performed as in the following scheme.
- the CH 3 S- residue of methylmercaptan is substituted with succinate or acetate residue of O-succinyl homoserine or O-acetyl homoserine to produce methionine.
- methylmercaptan (CH 3 SH) can be added in various forms.
- the methylmercaptan is either a gaseous methylmercaptan gas or a liquid methylmercaptan, and both sodium methylmercaptan solutions may be used.
- the sodium methylmercaptan solution and the methylmercaptan gas exhibit the same reaction characteristics on the water-soluble reaction liquid. Therefore, as described above, methylmercaptan may be directly used or dissolved in caustic soda, and may be used in the form of sodium methylmercaptan solution.
- methylmercaptan exists as a gas at room temperature, methylmercaptan is dissolved in caustic soda. It is more preferable to use in the form of the sodium methylmercaptan solution.
- enzymes with methionine conversion activity include cystathionine gamma synthase, O-succinylhomoserine sulfhydrylase and O-acetylhomoserine sulfidylase (O -acetylhomoserine sulfhydrylase) can be used one or more selected from the group consisting of.
- Enzymes having methionine conversion activity used in the methionine production reaction in the reaction are Escherichia sp. , Pseudomonas sp. , Leptospira sp., Corynebacterium sp.
- Saccharomyces sp. Chromobacterium sp., Nocardia sp., Bradyrhizobium sp., High homonas Hyphomonas sp.), in methyl Rhodococcus (Methylococcus sp.), genus Bacillus as methyl (Methylobacillus sp.), nitro consumption eggplant in (Nitrosomonas sp.), keurep when Ella in (Klesiella sp.), Bacillus (Bacillus sp .), Shigella sp., Colwellia sp., Salmonella sp., Yeast or yeast or fungi.
- microorganism strains belonging to the genus Pseudomonas, Nocadia , and Chromobacterium more preferably P. aurogenosa , Cystathionine gamma synthase, O-succi, derived from microbial strain belonging to N. Farcinica , P. putida , C. Violaceum
- P. aurogenosa P. aurogenosa
- Cystathionine gamma synthase O-succi, derived from microbial strain belonging to N. Farcinica , P. putida , C. Violaceum
- One or more enzymes selected from the group consisting of nilhomoserine sulfidylase and O-acetylhomoserine sulfidylase can be used.
- microorganism strains belonging to the genus Leptospira, Chromobacterium and Hypomonas more preferably Leptospira meeri ( L. meyeri), Pseudomonas Ke rugi labor (P. aurogenosa), hypo Pseudomonas Yep Tunisia Titanium (H. Neptunium), chromotherapy tumefaciens non come syum (C.
- Violaceum derived from a microorganism strain belonging to the cis tachioh non-gamma synthase, O- succinyl
- One or more enzymes selected from the group consisting of nilhomoserine sulfidylase and O-acetylhomoserine sulfidylase can be used.
- O-acetyl homoserine or O-succinyl homoserine which is a substrate used in the L-methionine production conversion reaction, is prepared as described in WO2008 / 013432, which is a conventional patent document. It was produced by fermenting the microorganism strains, and purified from the cultured fermentation broth using O-acetyl homoserine or O-succinyl homoserine as a substrate by methanol precipitation method.
- the enzyme used in the L-methionine production conversion reaction is chromobacterium viola ( Chromobacterium violaceum O-succinyl homoserine sulfidylase and hypomonas neptunium ( Hyphomonas Neptunium O-acetylhomoserine sulfidylase gene derived from the) was fermented, and the cells were recovered and crushed as described in WO2008 / 013432, which is a conventional patent document.
- a conversion reaction solution was prepared by mixing an enzyme having methionine conversion activity with O-acetyl homoserine or O-succinyl homoserine, which is a substrate recovered by the above method.
- Dimethylsulfide was mixed with methylmercaptan, which is used as another substrate, in an appropriate ratio, and then converted into a reaction solution.
- the mixing ratio of methylmercaptan and dimethylsulfide is a ratio of methylmercaptan: dimethylsulfide from 1: 0.0.5 (mol: mol) to 1: 1 (mol: mol), preferably 1: 0.20. (mol: mol) to 1: 1 (mol: mol), more preferably 1: 0.25 (mol: mol) to 1: 0.5 (mol: mol).
- dimethyl sulfide is preferably used in a ratio of 5% to 25%, more preferably 20% to 25% relative to the molar concentration of methylmercaptan.
- the present invention provides a methionine prepared by the above method.
- the methionine may be in the form of a dry powder or a solution dissolved in an aqueous solution after purification through a separate purification process.
- a method of converting an L-methionine precursor to L-methionine using a mixture of methylmercaptan and dimethylsulfide can produce L-methionine in a higher yield than the conventional method. It can be widely used in various fields such as feed and food additives, medical and raw materials of medicines.
- the present invention may increase the methionine production rate and increase the purity of the product L- methionine and organic acid compared to the case of using methylmercaptan alone in the conversion reaction. Furthermore, the productivity of methionine can be improved to achieve the economic effect of reducing the investment cost for the reaction equipment.
- 1 is a diagram comparing the change in enzyme conversion reaction rate according to the supply of methylmercaptan solution or dimethylsulfide mixed solution in a 1 L batch reactor with a change in pH.
- Figure 2 is a diagram showing the relative activity according to the mixing ratio of methylmercaptan solution (SMM) and dimethylsulfide (DMS).
- Dimethyl sulfide was mixed in the methylmercaptan solution in an appropriate ratio during the conversion reaction, and the conversion rate was compared with the conversion reaction of O-acetyl homoserine to methionine.
- Methylmercaptan exists as a gas at room temperature, and sodium methyl mercaptan (CH 3 S-Na, 2.14M, 15%, in the state of Tokyo chemical industry in Japan) by adding methylmercaptan to caustic soda solution. May exist.
- the experiment was performed using a sodium methylmercaptan 2.14 M solution.
- Sodium methylmercaptan 2.14 M solution was collectively referred to as methylmercaptan solution.
- a methylmercaptan solution and a dimethylsulfide solution 13.38M, 99%, French arkema
- the conversion reaction solution was prepared by adding 50 ⁇ l of the conversion enzyme solution to 1 ml of O-acetyl homoserine (500 mM) solution, and the enzyme cofactor pyridoxal 5'-phosphate (Sigma, USA) at a concentration of 0.1 mM.
- O-acetyl homoserine solution was used by dissolving O-acetyl homoserine purified from the fermentation broth in a phosphate buffer at pH 7.5.
- Fermented strains were CJM-BTJA / pCJ-metXlme-CL strain produced by the method disclosed in WO2008 / 013432.
- the CJM-BTJA / pCJ-metXlme-CL strain was inoculated in a 5L fermenter and incubated for 50-100 hours by a fed batch fermentation method.
- O-acetyl homoserine was purified from the cultured fermentation broth using methanol precipitation method.
- the conversion enzyme fermented the strain E. coli W3110 transformed with pCJ-MetZ-CL derived from Hyphomonas Neptunium , and recovered and disrupted the cells as described in WO2008 / 013432. Used.
- Enzymatic reaction was started by adding each methylmercaptan and dimethylsulfide mixed liquid to the prepared conversion reaction liquid. At this time, the amount of methylmercaptan and dimethylsulfide mixed solution was adjusted so that the final amount of methylmercaptan amount was 0.04 mM.
- the reaction temperature was reacted under stirring at 33 ° C. and 800 rpm for 10 minutes. After completion of the reaction, the reaction was terminated by adding 0.2N HCl solution. The concentration of the product methionine was analyzed by HPLC analysis. Analysis conditions were based on the analysis conditions specified in WO2008 / 013432.
- the methionine conversion (%) of O-acetyl homoserine was calculated by calculating the moles of methionine produced from the moles of substrate (mol / L) used in the reaction. % Conversion was calculated as 100% when 1 mol of methionine was produced from 1 mol of O-acetyl homoserine and methylmercaptan. The analysis results are shown in Table 1 below.
- the reaction was performed using 500 mL of 700 mM O-acetyl homoserine in a 1 L batch reactor.
- the enzyme conversion reaction was performed while continuously supplying a methylmercaptan solution or a mixed solution of methylmercaptan solution and dimethylsulfide 1: 0.25 (mol: mol) at a flow rate of 3.0 mL / min for 60 min.
- the amount of methylmercaptan contained in each solution was adjusted to be the same.
- Reaction temperature was set to 33 degreeC and stirring was 700 rpm.
- Conversion enzyme solution was prepared in the same manner as in the above and the Example was added to 10 mL and the enzyme cofactor pyridoxal phosphate (pyridoxal 5'-phosphate) was added at a concentration of 0.1 mM. The amount of methionine produced after about 3 hours was measured using HPLC. The results are shown in Table 3 below.
- the conversion rate of the enzyme reaction in which O-succinyl homoserine is converted to methionine was compared by dimethyl sulfide added amount in the methylmercaptan solution in the same 1.5 mL tube scale.
- the amount of dimethylsulfide added was mixed so that the ratio of methylmercaptan solution to dimethylsulfide was 1: 0, 1: 0.25, 1: 0.35, 1: 1 (mol: mol), respectively.
- the conversion reaction solution was prepared by adding 50 ⁇ l of conversion enzyme solution to 1 ml of O-succinyl homoserine (500 mM) solution and pyridoxal 5'-phosphate, an enzyme cofactor, at a concentration of 0.1 mM.
- the O-succinyl homoserine solution was used by dissolving O-succinyl homoserine purified from the fermentation solution in phosphate buffer at pH 7.5.
- CJM-BTJ / pCJ-metA-CL strain prepared as described in WO2008 / 013432 was inoculated in a 5L fermenter and incubated for 50 to 100 hours by a fed batch fermentation method.
- O-succinyl homoserine was purified from the cultured fermentation broth using methanol precipitation.
- the conversion enzyme fermented E. coli W3110 strain transformed with pCJ-MetZ-CL derived from Chromobacterium violaceum , and recovered and disrupted the cells as described in WO2008 / 013432.
- the enzyme dose was 0.05 mL.
- the enzymatic reaction was initiated by adding 0.02 mL of a mixed solution of methylmercaptan solution and dimethyl sulfide in various mixing ratios to the prepared reaction solution. Each solution was adjusted to contain the same amount of methylmercaptan.
- the reaction temperature was reacted under stirring at 33 ° C. and 800 rpm for 10 minutes. After completion of the reaction, the reaction was terminated by adding 0.2N HCl solution.
- the product methionine concentration was analyzed by HPLC analysis. The results are shown in Table 4.
- the present invention can provide a method for increasing the conversion rate to methionine, so it is a very useful invention for feed, food additives and pharmaceutical industry.
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Abstract
Description
Claims (11)
- 메치오닌 전구체인 O-아세틸 호모세린 또는 O-숙시닐 호모세린 상기 메치오닌 전구체를 메치오닌으로 전환하는 전환효소; 및 메칠머캅탄과 디메칠설파이드의 혼합액을 포함하는 반응용액을 제조하는 제1단계; 및상기 반응용액을 교반하면서, 효소 전환 반응을 수행하는 제2단계를 포함하는 메치오닌 생산방법.
- 제 1항에 있어서, 상기 메칠머캅탄은 메칠머캅탄 가스 또는 소디움 메칠머캅탄 용액인, 메치오닌 생산방법.
- 제 1항에 있어서, 상기 메칠머캅탄과 디메칠설파이드의 혼합비율은 메칠머캅탄:디메칠설파이드가 1:0.05 내지 1:1의 비율인, 메치오닌 생산방법.
- 제 3항에 있어서, 상기 메칠머캅탄과 디메칠설파이드의 혼합비율은 메칠머캅탄:디메칠설파이드가 1:0.20 내지 1:1의 비율인, 메치오닌 생산방법.
- 제 4항에 있어서, 상기 메칠머캅탄과 디메칠설파이드의 혼합비율은 메칠머캅탄:디메칠설파이드가 1:0.25 내지 1:0.5의 비율인, 메치오닌 생산방법.
- 제 1항에 있어서, 상기 메치오닌 전환활성을 가진 효소는 시스타치오닌 감마 신타아제(cystathionine gamma synthase), O-숙시닐호모세린 설피드릴라아제(O-succinylhomoserine sulfhydrylase) 및 O-아세틸호모세린 설피드릴라아제(O-acetylhomoserine sulfhydrylase)로 이루어진 군으로부터 선택되는 1종 이상인, 메치오닌 생산방법.
- 제 1항에 있어서, 상기 방법은 효소 전환 반응을 종료하는 단계를 추가로 포함하는, 메치오닌 생산방법.
- 제 1항에 있어서, 상기 방법은 상기 효소 전환 반응에 의해 형성된 반응액에 존재하는 메치오닌을 정제하는 단계를 추가로 포함하는, 메치오닌 생산방법.
- 제 8항에 있어서, 상기 메치오닌을 정제하는 방법은 하기 단계를 포함하는, 메치오닌 생산방법:1) 효소 전환 반응액으로부터 균체를 분리하는 단계; 2) 상기 균체가 분리된 반응액을 탈색 및 여과하는 단계; 및 3) 상기 여과액을 결정화하는 단계.
- 제 1 내지 제 9항 중 어느 한 항의 방법으로 제조된 메치오닌.
- 제 10항에 있어서, 상기 메치오닌은 분말 또는 용액 상태인, 메치오닌.
Priority Applications (6)
Application Number | Priority Date | Filing Date | Title |
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JP2011551987A JP5481497B2 (ja) | 2009-02-27 | 2010-02-26 | メチルメルカプタンとジメチルスルフィドの混合物を使用してメチオニン生産能を増加させる方法 |
EP10746468.7A EP2402453B1 (en) | 2009-02-27 | 2010-02-26 | Method for increasing methionine productivity using a mixture of methyl mercaptan and dimethyl sulfide |
DK10746468.7T DK2402453T3 (en) | 2009-02-27 | 2010-02-26 | Process for Increasing Methionine Productivity Using a Mixture of Methylmercaptan and Dimethyl Sulfide |
ES10746468.7T ES2618407T3 (es) | 2009-02-27 | 2010-02-26 | Procedimiento para aumentar la productividad de metionina usando una mezcla de metil mercaptano y sulfuro de dimetilo |
US13/203,521 US9024063B2 (en) | 2009-02-27 | 2010-02-26 | Method for increasing methionine productivity using a mixture of methyl mercaptan and dimethyl sulfide |
CN201080009632.4A CN102333881B (zh) | 2009-02-27 | 2010-02-26 | 使用甲硫醇和二甲硫醚的混合物增加蛋氨酸产率的方法 |
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KR1020090016604A KR101048593B1 (ko) | 2009-02-27 | 2009-02-27 | 메칠머캅탄과 디메칠설파이드의 혼합물을 사용하여 메치오닌 생산능을 증가시키는 방법 |
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EP (1) | EP2402453B1 (ko) |
JP (1) | JP5481497B2 (ko) |
KR (1) | KR101048593B1 (ko) |
CN (1) | CN102333881B (ko) |
DK (1) | DK2402453T3 (ko) |
ES (1) | ES2618407T3 (ko) |
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Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2012087038A2 (ko) | 2010-12-21 | 2012-06-28 | 씨제이제일제당 (주) | 신규 o-아세틸호모세린 설피드릴라아제 또는 이의 변이체 및 이를 이용한 메치오닌 전환 방법 |
WO2013029690A1 (en) * | 2011-09-02 | 2013-03-07 | Arkema France | Preparation process of l-methionine |
JP2014501116A (ja) * | 2010-12-29 | 2014-01-20 | シージェイ チェイルジェダン コーポレーション | L−メチオニン及び関連産物の生産方法 |
CN108026550A (zh) * | 2015-09-30 | 2018-05-11 | 阿肯马法国公司 | 用于制备l-甲硫氨酸的方法 |
WO2019004780A2 (ko) | 2017-06-30 | 2019-01-03 | 씨제이제일제당 (주) | 신규한 o-숙시닐 호모세린 트랜스퍼라제 변이체 및 이를 이용한 o-숙시닐 호모세린의 제조방법 |
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Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2008013432A1 (en) | 2006-07-28 | 2008-01-31 | Cj Cheiljedang Corporation | Microorganism producing l-methionine precursor and method of producing l-methionine and organic acid from the l-methionine precursor |
WO2008103432A1 (en) | 2007-02-23 | 2008-08-28 | Schering Corporation | Engineered anti-il-23p19 antibodies |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US2775616A (en) * | 1956-12-25 | Preparation of methionine from a-aming- | ||
KR100651220B1 (ko) * | 2004-06-29 | 2006-11-29 | 씨제이 주식회사 | L-메씨오닌 생산 균주 및 상기 균주를 이용한l-메씨오닌의 생산방법 |
BRPI0612900A8 (pt) * | 2005-07-18 | 2022-07-19 | Basf Ag | Métodos para produzir metionina, para aperfeiçoar o uso de dmds para produção de metionina, e, para identificar um alelo mutante, composição, produto contendo metionina, microorganismo, gene isolado, o-acetil-homosserina sulfidrilase mutante ou enzimas de o-succinil-homosserina sulfidrilase, e organismo |
RU2008109855A (ru) * | 2005-08-18 | 2009-09-27 | Эвоник Дегусса ГмБх (DE) | Микроорганизмы с повышенной эффективностью синтеза метионина |
-
2009
- 2009-02-27 KR KR1020090016604A patent/KR101048593B1/ko active IP Right Grant
-
2010
- 2010-02-26 PL PL10746468T patent/PL2402453T3/pl unknown
- 2010-02-26 DK DK10746468.7T patent/DK2402453T3/en active
- 2010-02-26 CN CN201080009632.4A patent/CN102333881B/zh active Active
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- 2010-02-26 WO PCT/KR2010/001250 patent/WO2010098629A2/ko active Application Filing
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Patent Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2008013432A1 (en) | 2006-07-28 | 2008-01-31 | Cj Cheiljedang Corporation | Microorganism producing l-methionine precursor and method of producing l-methionine and organic acid from the l-methionine precursor |
WO2008103432A1 (en) | 2007-02-23 | 2008-08-28 | Schering Corporation | Engineered anti-il-23p19 antibodies |
Non-Patent Citations (2)
Title |
---|
JEON BR ET AL., J HEPATOL., vol. 34, no. 3, March 2001 (2001-03-01), pages 395 - 401 |
See also references of EP2402453A4 |
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JP2017123845A (ja) * | 2010-12-29 | 2017-07-20 | シージェイ チェイルジェダン コーポレーション | L−メチオニン及び関連産物の生産方法 |
US9752167B2 (en) | 2010-12-29 | 2017-09-05 | Cj Cheiljedang Corporation | Methods for production of L-methionine and related products |
JP2014501116A (ja) * | 2010-12-29 | 2014-01-20 | シージェイ チェイルジェダン コーポレーション | L−メチオニン及び関連産物の生産方法 |
EP2658986A4 (en) * | 2010-12-29 | 2016-08-10 | Cj Cheiljedang Corp | PROCESS FOR PREPARING L-METHIONINE AND RELATED PRODUCTS |
JP2014521358A (ja) * | 2011-09-02 | 2014-08-28 | アルケマ フランス | L−メチオニンの製造方法 |
WO2013029690A1 (en) * | 2011-09-02 | 2013-03-07 | Arkema France | Preparation process of l-methionine |
CN108026550A (zh) * | 2015-09-30 | 2018-05-11 | 阿肯马法国公司 | 用于制备l-甲硫氨酸的方法 |
CN108026550B (zh) * | 2015-09-30 | 2022-10-04 | 阿肯马法国公司 | 用于制备l-甲硫氨酸的方法 |
US10378031B2 (en) | 2015-10-13 | 2019-08-13 | Cj Cheiljedang Corporation | O-acetylhomoserine sulfhydrylase variant and method for producing L-methionine using same |
WO2019004780A2 (ko) | 2017-06-30 | 2019-01-03 | 씨제이제일제당 (주) | 신규한 o-숙시닐 호모세린 트랜스퍼라제 변이체 및 이를 이용한 o-숙시닐 호모세린의 제조방법 |
WO2019004779A2 (ko) | 2017-06-30 | 2019-01-03 | 씨제이제일제당 (주) | 신규한 o-숙시닐 호모세린 트랜스퍼라제 변이체 및 이를 이용한 o-숙시닐 호모세린의 제조방법 |
US10982245B2 (en) | 2017-06-30 | 2021-04-20 | Cj Cheiljedang Corporation | O-succinyl homoserine transferase mutant and method for producing O-succinyl homoserine using same |
US11142779B2 (en) | 2017-06-30 | 2021-10-12 | Cj Cheiljedang Corporation | O-succinyl homoserine transferase variant and method of producing O-succinyl homoserine using the same |
WO2021125896A1 (ko) | 2019-12-20 | 2021-06-24 | 씨제이제일제당 (주) | 내막 단백질의 변이체 및 이를 이용한 목적 산물 생산 방법 |
Also Published As
Publication number | Publication date |
---|---|
WO2010098629A3 (ko) | 2010-12-09 |
ES2618407T3 (es) | 2017-06-21 |
MY152999A (en) | 2014-12-31 |
US20120123158A1 (en) | 2012-05-17 |
US9024063B2 (en) | 2015-05-05 |
JP2012518432A (ja) | 2012-08-16 |
DK2402453T3 (en) | 2017-03-13 |
PL2402453T3 (pl) | 2017-09-29 |
EP2402453A4 (en) | 2013-11-20 |
CN102333881B (zh) | 2014-03-12 |
CN102333881A (zh) | 2012-01-25 |
JP5481497B2 (ja) | 2014-04-23 |
EP2402453B1 (en) | 2016-12-14 |
KR101048593B1 (ko) | 2011-07-12 |
KR20100097782A (ko) | 2010-09-06 |
EP2402453A2 (en) | 2012-01-04 |
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