• 专利附录
  • 专利说明
  • 权利要求
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    • 专利摘要:
    METHOD OF OBTAINING LOW O-L-AMINO ACIDS FROM THE RELATED Lower ot-ketr acids in the presence of a specific dehydrogenase specific for the substrate, ammonium salts and nicotinamide dyudine dinucleotide (NADVHAflH) with one-time regeneration of the process In the process, an ultrafiltration membrane reactor with an average pore size of 1-3 μm is placed in a solution of formate dehydrogenase and specific to the initial lower oi. a-ketoacid dehydrogenase containing NAD VHAHH at a concentration of 3.55-3.92 1 1 mol / l, which is associated with poly (ethylene glycol) with an average molecular weight of 10,000, is continuously fed with an aqueous solution containing 100-500 mmol / l of the initial cA-- ketbic acid as a water-soluble salt and an aqueous solution of ammonium formate as the ammonium salt with a concentration of 400–800 mmol / l, the pressure difference on both sides of the membrane / L supporting 0.2-0.5 bar, and continuous V the flow of filtrate containing the target product 2 is jerked out of the reactor through the membrane.
    公开号:SU1069622A3
    申请号:SU802954169
    申请日:1980-07-24
    公开日:1984-01-23
    发明作者:Вандрей Кристиан；Вихманн Рольф；Лойхтенбергер Вольфганг；Кула Мария-Регина；Бюкманн Андреас
    申请人:Дегусса Аг (Фирма)；Гезельшафт Фюр Биотехнологише Форшунг Мбх (Гбф) (Фирма)；
    IPC主号:
    专利说明:

    O5
    SO F
    yu yu
    The invention relates to the improvement of the production of lower d-t, amino acids used in pharmacology, pyadic activity, and also as starting compounds in peptide synthesis.
    The closest to the proposed method is the preparation of lower o.1. Amino acids, which consists in introducing the initial corresponding d-keto acid with a substrate of dehydrogenase specific to the substrate in the presence of a 0.1 M aqueous solution of ammonium salt (for example, ammonium phosphate), nicotinamide adenine nucleotide (NAD / NADH with simultaneous regeneration of .HAflH from NAD with methanol, ethanol or ethoxyethanol in the presence of alcohol dehydrogenase. At the same time, the concentration of nicotinamide adenine dinucleotide comp l is approximately 1 mmol / l, the concentration of the initial D-kotokisloty 10 mmol / L, yields of desired products 4,4-93,1% (excluding stage of separation from nicotinamide, and enzymes that phospha ammonium) 1.
    The disadvantage of this method is the complexity of the process, associated with the need to separate the target products from nicotinamide adenine dinucleotide, keto acid dehydrogenase and alcohol dehydrogenase. As a result, these enzymes are inactivated, and Nikitinamide adenine dinucleotide can be partially destroyed, which makes it almost impossible to reuse these components.
    The aim of the invention is to simplify the process of enzymatic production of lower ot-1, -amino acids from the corresponding lower oi-keto acids.
    This goal is achieved by the method of obtaining lower o-b-amino acids from the corresponding lower o (α-keto acids), which means that a solution of formate dehydrogenase and specific to the initial lower one is placed in a reactor with ultrafiltration membrane, the average pore size is 1-3 µm. The oC-ketoxylate dehydrogenase containing VAD / NADH at a concentration of 3.553, 92 mmol / l, which is bound to polyethylene glycol with an average molecular weight of 10,000, is continuously fed an aqueous solution containing 100-500 mmol / l of the starting oi-keto acid in water type soluble salt, and an aqueous solution of ammonium formate as an ammonium salt with a concentration of 400-800 mmol / l, the pressure difference on both sides of the membrane being maintained within 0.2-0.5 bar, and continuously withdrawn from the reactor through the membrane flow
    filtrate containing target .product.
    As a rule, the correlation between formate dehydrogenase and substrate-specific dehydrogenase activities is in the range of 1: (1-5).
    As a rule, the nickel mobilization of ashdtsin from a cleotide on polyethylene-. glycol is carried out by treating the coenzyme with ethyleneimine followed by concentration of the obtained amino acid of aminoethyl derivative with carboxypropyl polyethylene glycol with water soluble carbohydrates, after which the immobilized product is reduced to the corresponding derivative: f NADH, converted by D-production into N-derivative, in the m production. if necessary, they are oxidized to the corresponding derivative of NAD1. At the base of this, the coenzyme concentration is usually 0.1 to 10 mmol / l, preferably 1 to 7 mmol / l.
    The concentration of ammonium formate should preferably be equal to the concentration of the starting α-keto acid, or at least not lower than the last
    The pH of the reaction mixture during the process is usually kept in the range of 5–9.
    As a rule, target products are isolated using limestone methods, for example, using anion exchange resins. The implementation of the proposed method obviates the process of obtaining lower oC-ti-amino acids from the corresponding lower oC-keto acids and consists in a simpler separation of the target products from the initial ones, for example using anion-exchange resins; in the possibility of repeated reuse of expensive components - Formate dehydrogenase, specific with respect to the initial c-keto acid of the dehydrogenase, nicotinamide adenine dinucleotide in the continuity of the process; in a smaller volume. | the reaction mixture (by increasing the concentrations).
    Example. Thermostatically controlled 10c reactor with a flat membrane equipped with a magnetic stirrer and a membrane for ultrafiltration with a diameter of 62 mm with a nominal exclusion limit of 3QOO (supplier company Amikon, Witten, type DM 5) are washed for sterilization with an aqueous formaldehyde solution at a feed rate of 20 ml. / h using a dosing pump for about 5 hours. Then, for about 5 more hours, the formaldehyde solution is displaced by distillation with water, and then also at a feed rate of 20 MP / H for about 2.5 hours.
    pass a substrate solution filtered through a sterile filter (0.2 µm) containing 500 mmol / l sodium salt of pyruvic acid, 400 mmol / l and 50 mmol / l of sodium phosphate monosubstituted and brought to pH 8 at sodium hydroxide . After that, instead of a substrate solution, 10 ml of a solution of nicotinamide adenine dinucleotide containing 3.66 mmol / l HAJrt emitted with polyethylene glycol with an average mol. weighing 10,000 and 50 mmol / l of phosphate buffer solution. To establish a pH of 8. Then the cyecTpja-J5 solution is again applied.
    the same composition with a speed of 20 ml / h.
    Then, 100 mg of formate dehydrogenate 20 (activity of 6.74 µmol / mg per minute with formate as a substrate, and pH 8) in the form of an aqueous glycerin solution (50% by weight of glycerin ), 10 mg formate dehydro- 75
    Nasa / ml and 1.62 MV b-alanine dehydrogenase (activity 415 μmol / mg per minute with pyruvate as substrate, 40 s and pH 8) in the form of an aqueous solution in ammonium sulfate (2.4 mol / l ammonium sulfate, 5 mg 30 b alanine dehydrogenase / ml) using a syringe. With this composition, the ratio between the activities of formate dehydrogenase and L-alanine dehydrogenase is CH. The conversion process of the ZZ is continuously monitored when the flow-through filtrate mounted in the flow
    cuvettes floor of the rimeter. The differential pressure at the membrane initially reaches 0.2 bar, then gradually increases to 0.5 bar and remains constant after that. During the working period of about 50 hours, 175 mmol of L-alanine is obtained. The maximum conversion rate reaches-45 et of 6.45 mmol L-alanine / h.
    108 mmol of L-alanine are obtained. from 1 mg L-alanine dehydrogenase or 1.75 mmol L-alanine based on 1 MJf formate dehydrogenase. -d Target product yield 35%, optical purity 100%.
    PRI mme R 2. Sterilization of a 10 gg membrane reactor with a flat membrane (membrane with a nominal exclusion limit of 5000, supplier company Amikon, Witten, type UM 5), maintained at. conducted in the same manner as in example 1.-60
    At a feed rate of 20 ml / h, a sterile filtered solution containing 400 mmol / l of pyruvic acid sodium salt, 400 mmol / l form-65 is fed for about 2.5 h.
    ammonium miata and 50 mmol / l monosubstituted, sodium phosphate and adjusted to pH 8 with sodium hydroxide. After that, instead of the substrate solution, at a feed rate of 4 ml / h, a mixture of 7 ml of the cocozyme solution (in accordance with Example 1) and 138 mg of formate dehydrogenase (activity 0.85 µmol / mg per minute with formate as a substrate, and. pH 8) in the form of an aqueous glycerin solution (50% by weight of glycerin), 10 mg formate dehydrogenase / ml}. Thereafter, 2.78 mg of L-alanine dehydrogenase (activity 233 μmol / mg per minute with pyruvate as a substrate, 25c and pH 8) in the form of an aqueous solution in ammonium sulfate (2.4 mol / l of ammonium sulfate, 5 mg of L-alanine dehydrogenase / ml) using a syringe. The ratio between the formate dehydrogenase and L-alanine dehydrogenase activities reaches 1: 4. 48 mmol of L-alanine is obtained within 59 hours, which corresponds to 17.3 GUMOL L- alanine based on 1 mg of L-alanine dehydrogenase or 0.35 mmol of L-alanine based on 1 mg formate dehydrogenase. Target product yield 10.2%, optical purity 100%.
    Example H. A 10 ml sterilization of a flat membrane reactor (a membrane with a nominal exclusion limit of 5000, supplier Amykon, Witte, type UM 5) thermostatically controlled at 25 ° C was carried out as described in Example 1.
    At a feed rate of 20 ml / h, it is sterile for about 2.5 hours. filtered solution containing 400 mmol / l. pyruvic acid sodium salt, 800 mmol / l ammonium formate and 50 mmol / l sodium phosphate monosodium phosphate and adjusted to pH 8 with sodium hydroxide. After that, instead of a substrate solution, a mixture of 10 ml of coesisim solution (according to Example 1) and 85 mg of forate dehydrogenase (activity 0.85 µmol / mg per minute with formate as a substrate, and pH 8) are introduced at a speed of 4 ml / h. in the form of an aqueous glycerin solution (50% by weight of glycerin), 10 mg formate dehydrogenase / ml. After that, 0: 94 mg of L-alanine dehydrogenase (activity 233 µmol / mg per minute per pyruvate as a substrate, 25 C and pH 8) is introduced into the reaction space through a side opening with a Pomoid syringe 0, in the form of an aqueous solution of ammonium sulfate (2, 4 mol / l sulfa. That ammonium, 5 mg of L-alanine dehydrogenase / ml). The ratio between the activities reaches 1: 2.2. For 140 h, 92 mmol of L-alanine is obtained, which corresponds to 98 mmol of L-alanine based on 1 mg of L-alanine rogenase or 1.08 mmol of L-alanine based on 1 mg of Formiatehydrohydrochloride. The yield of the target product is 8.2%, the optical purity of 100%. PRI me R 4. Thermostatically controlled, at 25 ° C, a 11.3 ml flat membrane reactor equipped with a magnetic stirrer and a 62 mm ultrafiltration membrane with a nominal elimination limit of 5pOO (supplier Amikon, Vitten, type UM 5) It is washed for sterilization with a dosing pump installed at a feed rate of 20 ml / h for about 5 hours with an aqueous solution of 70% ethyl alcohol and replaced with distilled water. Thereafter, a sterile filter (0.2 mmk) filtered substrate solution containing 100 mmol / l of 2-oxo4 methylpentanoic acid sodium salt and 400 mmol / l of ammonium formate, and a pH of 8 is set with caustic soda solution. Then, 11.77 ml, respectively, 35.2 mg of formate dehydrogenase (activity 4.06 μmol / mg) is metered into the substrate current between the metering substrate and the sterile filter. per minute in the case of formate as a substrate - at 25 ° C and pH 8) in the form of One polyethylene glycol solution (40 wt.% ethylene glycol with an average mole, mass 400; 3 mg formate dehydrogenase / ml); In addition, 1.6 ml are injected in the same way, respectively, 6.72 mg leucine dehydrogenase (activity 10.46 μmol / mg per minute in the case of the sodium salt of 2-oxo-4-methylpentanoic acid as a substrate, 400 mmol / l ammonium formate, 25 ° C and pH B) in the form of an aqueous solution of phosphate.cali (10 mmol / l, pH 7) i the following 5 h dispensed substrate solution. After this, the substrate feed rate is set at. 11.3 ml / h and 2.88 ml of a coenzyme solution is added to the enzyme, which contains 3.92 mmol / l of NADH, associated with polyethylene glycol with an average mol. weighing 10,000 in the form of an aqueous solution, in which pH is set at 8 using sodium hydroxide solution. The ratio of formate dehydrogenase to leucine dehydrogenase activities is 1: 2. The process is monitored with a flowmeter of the polarimeter integrated in the flow filtrate. The differential pressure above the membrane gradually rises to about 35 bar and then remains constant. Within 205 hours (8.5 days), 202 mmol of L-leucine is obtained. The maximum process rate is 1.12 mmol L-leucine per hour. The yield of the target product is 87.2%, the optical purity is 100%. ExampleB Thermostatically controlled reactor at 25 ° C with a volume of 10 ml with a Sh1os membrane, which is equipped with a magnetic stirrer and an ultrafiltration membrane with a diameter of 62 mm and a nominal exclusion limit of 5000 (production company Amikon, Witten, type UM 5), using the feed rate set at 20 The ml / h dosing pump for approximately 5 hours is sterilized with a 70% aqueous solution of ethanol to sterilize. Then, over the next 5 hours, the ethanol is displaced with distilled water. After that, at a feed rate of 20 ml / h, the substrate solution filtered through a sterile filter (0.2 μm), which contains 100 mmol / l of 2-oxo4-methylpentanoic acid sodium salt, 400 mmol / l of formate is fed for about 2.5 h ammonium and 50 mmol / l of sodium phosphate monosubstituted, and the pH is adjusted to 8 with sodium hydroxide solution. Then, instead of the substrate solution, 7 are metered, | ml of coenzyme solution, which contains 3.80 mmol / l of NADH bound with polyethylene glycol of average mole, weight 10,000, and 50 mmol / l of phosphate buffer with pH B. Thereafter, 6J., 5 formate dehydrogenase is metered (activity 2.60 μmol / mg per minute with formate as a substrate, 25 ° C and pH 8) in the form of an aqueous solution of glycerol (50 weight,% glycerol; 10 ml formate dehydrogenase / ml), Subsequently, the substrate solution is dispensed in the manner described. After about 5 hours, the flow of the substrate is reduced to 2 ml / h. Then, 31.6 mg of leucine dehydrogenase (activity 11.48 µmol / mg per minute in the case of the sodium salt of 2-oxo-4-methylpentanic acid as a substrate, at a concentration of 4 pO mmol / is added to the reaction volume in front of the membrane through the side opening with a syringe) l ammonium formate, 25 ° C and pH 8) in the form of an aqueous solution of potassium phosphate (10. mmol / l 4.2 mg of leucine dehydrogenase / ml). The ratio of the activities of formate dehydrogenase and leucine dehydrogenase is 1S2.3. The process is controlled by means of a polarimeter flow cell built into the filtrate of the filtrate. The differential pressure above the membrane is set at
    710696228
    0.35 bar and then remains constant m-. the process has a potency of 0.20 mmol. For 1152 h 48 days L), obtain L-leucine a / h. The yield of the target product is 150 mmol of L-leucine. The maximum speed is 65 D% optical purity 100%.
    权利要求:
    Claims (1)
    [1]
    METHOD FOR PRODUCING LOW. “/ - L — AMINO ACIDS from the corresponding lower oC keto acids in the presence of a specific dehydrogenase substrate, ammonium salt and nicotinamide adenine dinucleotide (NAD + / NADH) while regenerating NADH from NAD)) is distinguished. The reason is that, in order to simplify the process, a solution of formate dehydrogenase specific with respect to the initial lower οί-keto acid dehydrogenase containing NAD is placed in a reactor with an ultrafiltration membrane, the average pore size of which is 1-3 microns t / NADH at a concentration of 3.55-3.92 mmol / L, which is associated with polyethylene glycol with an average molecular weight of 10,000, is continuously fed an aqueous solution containing 100-500 mmol / L of the starting ci-keto acid in the form of a water-soluble salt and an aqueous solution ammonium formate as an ammonium salt end centration 400-800 mmol / l, wherein the pressure difference on both sides of the membrane is maintained 0.2-0.5 bar, and continuously withdrawn from the reactor via the membrane a filtrate stream containing the desired product * »SU ..,. 1,069,622
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    法律状态:
    优先权:
    申请号 | 申请日 | 专利标题
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