WO1995007359A1 - Procede de conversion catalysee par voie enzymatique de composes organiques - Google Patents

Procede de conversion catalysee par voie enzymatique de composes organiques Download PDF

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Publication number
WO1995007359A1
WO1995007359A1 PCT/EP1994/003038 EP9403038W WO9507359A1 WO 1995007359 A1 WO1995007359 A1 WO 1995007359A1 EP 9403038 W EP9403038 W EP 9403038W WO 9507359 A1 WO9507359 A1 WO 9507359A1
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Prior art keywords
ester
process according
enzyme
alcohol
acid
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PCT/EP1994/003038
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English (en)
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Maria Christina De Zoete
Frederik Van Rantwijk
Roger Arthur Sheldon
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Technische Universiteit Delft
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Priority to AU76964/94A priority Critical patent/AU7696494A/en
Publication of WO1995007359A1 publication Critical patent/WO1995007359A1/fr

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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
    • 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
    • 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
    • C12P13/02—Amides, e.g. chloramphenicol or polyamides; Imides or polyimides; Urethanes, i.e. compounds comprising N-C=O structural element or polyurethanes

Definitions

  • the present invention relates to a process for carrying out enzymatically catalyzed conversions of organic compounds.
  • the present invention provides a process for carrying out enzymatically catalyzed conversions of organic compounds, wherein an ester of an organic acid is reacted with ammonia in a liquid organic phase in the presence of a hydrolytic enzyme.
  • This conversion reaction with ammonia is referred to herein as ammonolysis, and leads to the obtainment of amides.
  • the organic acid ester is a carboxylic acid ester.
  • the invention may also be applied to conversions of, e.g., phosphoric and sulfonic acid esters.
  • the conversion according to the invention can be generally represented as follows:
  • the carboxylic acid (RCOOH) corresponding to the ester in question may be a simple carboxylic acid (such as a straight- or branched-chain alkanoic or alkenoic acid) or a carboxylic acid of more complex structure. Thus, it may, for example, be selected among substituted and unsubstituted aliphatic, cycloaliphatic (alicyclic), aromatic and heterocyclic carboxylic acids, including aliphatic and cycloaliphatic carboxylic acids containing aromatic and/or heterocyclic rings. Aliphatic or cycloaliphatic (alicyclic) carboxylic acids of the types in question, as well as substituents therein, may further be saturated or unsaturated (i.e. contain ethylenic and/or acetylenic double bonds). Carboxylic acids belonging to the above- mentioned types and containing two or more carboxylic acid (carboxy) functionalities are also or relevance in the context of the present invention.
  • esters of simple carboxylic acids are to be found among esters of saturated 0,-0*,, carboxylic acids, e.g. propionic, butyric, isobutyric, valeric, isovaleric, caproic (hexanoic), heptanoic, caprylic (octanoic), nonanoic and decanoic acids.
  • carboxylic acids e.g. propionic, butyric, isobutyric, valeric, isovaleric, caproic (hexanoic), heptanoic, caprylic (octanoic), nonanoic and decanoic acids.
  • esters of carboxylic acids of somewhat more complex structure may be mentioned esters of the chiral acids 2-(6-methoxy-2- naphthyl) propionic acid (an enantiomer of which is marketed as an antiinflammatory/analgesic drug under the name, inter alia, of "Naproxen”), 2-(4- isobutylphenyl) propionic acid (the racemic form of which is marketed as an antiinflammatory drug under the name, inter alia, of "Ibuprofen”) and trans- (4- methoxyphenyl)glycidic acid (derivatives of which are useful, for example, in the synthesis of a vasodilatory drug marketed under the name, inter alia, of "Diltiazem”).
  • the ester function (alcohol component) in the organic acid ester employed in the process of the invention can be derived from a wide variety of substituted and unsubstituted alcohols, including lower aliphatic alcohols such as methanol, ethanol, propanol and higher homologues with, e.g., 4, 5, 6 or more carbon atoms, and may in this connection contain aromatic rings (such as substituted or unsubstituted phenyl or naphthyl rings) and/or heterocyclic rings (e.g. substituted or unsubstituted pyridyl rings).
  • lower aliphatic alcohols such as methanol, ethanol, propanol and higher homologues with, e.g., 4, 5, 6 or more carbon atoms
  • aromatic rings such as substituted or unsubstituted phenyl or naphthyl rings
  • heterocyclic rings e.g. substituted or unsubstituted pyridyl rings
  • a substituted ethanol such as 2-chloroethanol provides a quite reactive ester function. More generally, it appears that the more reactive ester functions, notably when using lipases as enzymes, will be derived from relatively lipophilic alcohols, including moderately long-chain (e.g. C 8 -C 12 ) alkanols.
  • RCO 2 R' may also be attached to each other.
  • the starting material is a lactone, and the reaction product then obtained is a hydroxy-substituted amide.
  • a carboxylic acid ester RCO 2 R' to be used as starting material for the ammonolysis procedure can be prepared enzymatically (i.e. using an enzyme - e.g. an esterase or a lipase - as catalyst) from the acid (RCOOH) in question and the alcohol (R'OH) in question, whereafter the ester obtained is subjected to the present ammonolysis using the same or a different enzyme.
  • an enzyme - e.g. an esterase or a lipase - as catalyst
  • the ester obtained is subjected to the present ammonolysis using the same or a different enzyme.
  • the alcohol itself can then serve as solvent at the same time.
  • the water which is released during the ester formation should be removed, preferably continuously, from the reaction medium in order to maximise the degree of ester formation and, notably, the subsequent conversion of the resulting ester to the amide.
  • This variant of the process of the invention has a number of important advantages: Firstly, e.g., the ester formed need not be separated from the reaction medium (although it may, of course, if so desired), and it is therefore possible [cf. the working examples provided herein (vide infra)] to carry out the ester synthesis in situ (i.e. in the reaction vessel system subsequently used for the ammonolysis reaction) prior to performing the ammonolysis procedure, i.e. to carry out the entire sequence of reactions (i.e.
  • hydroxy- substituted amides can be prepared without requiring the presence of a separate alcohol.
  • hydrolytic enzymes can be used as catalytic components in the practice of the present conversions. Enzymes belonging to the group of the esterases and in particular of the lipases have been found to be particularly suitable. Proteases have, however, also proved to be well suited for certain purposes, such as the ammonolysis of protected (notably N-protected) amino acid esters. These enzymes are commercially available, sometimes immobilized on a support. If they are not provided in supported form by the supplier, it is generally preferable that they be immobilized on a support before use in the process of the invention, since it is then easier to separate the enzyme from the reaction medium afterwards and to obtain the desired reaction product.
  • the preparation of the supported enzyme can be carried out by any appropriate known technique. A suitable technique is disclosed, for instance, in WO 90/15868.
  • Lipases As examples of suitable enzymes for use in accordance with the invention, the following can be mentioned: Lipases:
  • lipase SP 435 (a supported form of Candida antarctica lipase B, disclosed in EP 0 287 634), available from Novo Nordisk A/S, Denmark, under the name NovozymTM 435;
  • lipase SP 398 and lipase SP 523 both available from Novo Nordisk A/S;
  • lipase SP 524 (from Rhizomucor miehei), available in supported form from Novo Nordisk A/S;
  • lipoprotein lipase from Pseudomonas, available from Boehringer Mannheim GmbH, Germany, catalogue No. 734 286;
  • porcine pancreas lipase (type II, 70 units/mg), available from Sigma Chemical Company, St. Louis, USA; and
  • Amano PS lipase unimmobilized preparation available from Amano, Japan (possibly cross-linked, since it displays low solubility in water);
  • protease SP 539 available from Novo Nordisk A/S
  • Subtilisin A available from Novo Nordisk A/S.
  • the reaction medium i.e. the liquid organic phase
  • the reaction medium may contain one or more organic solvents.
  • Solvents are required only in certain cases where one of the starting materials or one of the reaction products is a solid substance.
  • a solvent such as an alcohol, for instance tert-butyl alcohol.
  • an excess of the alcohol in question can often serve as solvent, optionally in combination with one or more other suitable solvents.
  • solvents suitable for use in the process of the invention are solvents which are of moderate to low polarity, display limited to low miscibility with water and are good solvents for ammonia (i.e. substantially anhydrous ammonia).
  • Solvents meeting these requirements are to be found, for example, among alcohols, suitably certain lower aliphatic alcohols, and in particular tertiary aliphatic alcohols such as tert-butyl alcohol, tert-amyl alcohol and the like, which are sterically relatively hindered with respect to nucleophilic reaction of the oxygen atom of the alcoholic hydroxy group and therefore have relatively little tendency to compete as nucleophiles with ammonia (in ammonolysis) or with ester-forming alcohols (in ester formation from an acid and an alcohol).
  • Secondary alcohols and in some cases primary alcohols, which generally speaking are less sterically hindered in this respect than corresponding tertiary alcohols, may nevertheless be satisfactory solvents for certain embodiments of the process of the invention.
  • Other types of organic solvents which appear to be suitable for use in the context of the invention include, e.g., certain ethers.
  • the concentration of the starting material (s) to be converted is between 3 and 50%, calculated on the basis of the liquid organic phase. However, higher concentrations are quite possible, and concentrations of, e.g., up to about 60% or even about 70% appear to be feasible.
  • the typical procedure will then be to add the enzyme - preferably immobilized on a support - to the reaction medium, which will typically be a solution (as discussed above).
  • the amount of enzyme to be used is partly determined by the extent to which the enzyme is active towards effecting the conversion contemplated. This can easily be determined experimentally by methods well known per se. For some enzymes, the required amount of enzyme is larger, sometimes even considerably larger, than for others. For any selected enzyme, of course, the extent of conversion can also be increased by prolonging the reaction time.
  • the reaction may then be carried out by allowing ammonia to act on the reaction medium.
  • ammonia for this purpose, gaseous ammonia at atmospheric pressure (obtained, e.g. from a "lecture bottle” or the like) can be bubbled through the reaction medium.
  • ammonia can also be allowed to act under pressure, so that the reaction velocity can be increased.
  • liquid ammonia may in some cases be advantageous, especially if ester substrates of low thermal stabilitity are involved.
  • a saturated solution of ammonia in tert-butyl alcohol prepared by bubbling ammonia gas through the solvent for a moderately extended period of time.
  • a saturated solution at ambient temperature contains approximately 2.5 mol of ammonia per liter, and it may suitably be used directly to perform the ammonolysis in an essentially closed system; alternatively, the saturated solution may be diluted with tert-butyl alcohol to achieve a desired concentration of ammonia lower than the saturation concentration.
  • An ammonia concentration of less than 2.5 mol/l is advantageous for the stability of certain lipases and proteases.
  • the conversion is typically carried out at room temperature (i.e. ambient temperature), although a higher temperature may be employed to increase the velocity, or a lower temperature to improve the selectivity and/or (as mentioned above) to minimize thermal degradation of thermolabile reaction components.
  • a temperature in the range of about 15-50°C will generally be suitable. Temperatures in the range of about 20-40°C, e.g. 20-25°C, will often be very suitable for the ammonolysis procedure, whereas it may be appropriate to employ a rather higher temperature, such as a temperature in the range of about 25-50°C, e.g. around 40°C, for enzyme-catalyzed ester formation from an acid and an alcohol.
  • the overall reaction conditions can be classified as particularly mild.
  • the enzyme can be separated from the reaction medium, typically by filtration, whereafter the filtrate can be subjected to further treatment using conventional techniques in order to obtain the intended product.
  • the first to be mentioned is the provision of a process for preparing amides under very mild conditions. This is of importance in cases where it is desired to perform conversions on very sensitive molecules which are not resistant to the temperature at which amides are formed in previously known chemical procedures.
  • the present process can be carried out at room temperature (or at least at a temperature not deviating greatly therefrom), and the other conditions are also such that even rather unstable starting materials are not at risk of being broken down or undergoing other undesired conversions.
  • the ammonolysis procedure of the present invention exhibits high stereoselectivity when the starting material is a racemate, i.e. one of the enantiomers is converted with a high selectivity.
  • the invention thus provides a process for separating the enantiomers from each other.
  • the asymmetry (chirality) can reside in the acid component or in the alcohol component or even in both. It is both surprising and of great importance that the present ammonolysis has a higher enantioselectivity than the enzymatically catalyzed hydrolysis which is employed on an industrial scale, for instance in the preparation of one enantiomer of the drug substance Ibuprofen (vide supra) in pure form.
  • the present ammonolysis procedure can be used for carrying out regioselective and/or enantioselective conversions in compounds containing, for example, two ester groups, so that only one of those ester groups is converted to amide, whilst the other one is maintained in unmodified condition.
  • ACCURELTM is an AKZO trade name for a particulate polypropene. The different types of ACCUREL are described in a datasheet on ACCUREL systems from AKZO, Fibers and Polymers Division, obtainable from Enka AG, Postfach D- 8753 Obenburg, Germany.
  • the immobilization of the enzymes on ACCUREL EP 100 was performed by the method described in Example 3 of WO 90/15868, utilizing an enzyme-to-support ratio of 1 :1.
  • the amounts of enzyme specified in the Examples relate to the total amount of enzyme + support.
  • HPLC NovapakTM C18; mobile phase 60/40 acetonitrile/water; NaOAc/HOAc 0.01 M; pH 4.5.
  • reaction mixture After 24 hours (100% conversion; 95% octanamide; 5% octanoic acid) the reaction mixture was processed further.
  • the isolation was carried out as follows.
  • the enzyme was filtered off and washed with 1 ,2-dichloroethane.
  • the washing liquid and the filtrate were combined, and 1 ,2- dichloroethane and tert-butyl alcohol were evaporated under vacuum.
  • the resulting crude octanamide was then recrystallized from 40/60 petroleum ether at -20°C.
  • the solid octanamide was filtered off and washed with cold 40/60 petroleum ether.
  • This protocol is important when the starting material is a chiral acid, since in that case an enantioselective conversion takes place twice in succession.
  • E is the “enantiomeric ratio” and is calculated according to the formula given in “Biotransformations in Organic Chemistry” Kurt Faber, Springer Verlag, 1992, page 15 33.
  • the enantioselectivity in the reaction [given as enantiomeric excess (ee) of ⁇ - methylbenzyl alcohol] was determined by GC using a chiral GC column material (Astec ChiraldexTM G-TA).
  • amino acid esters can be converted to amino acid amides by ammonolysis; amide compounds of this type are important, for example, in the enzymatic synthesis of penicillins such as Ampicillin and Amoxicillin (see, e.g, WO
  • the reaction is catalyzed by, for example, lipases and proteases.
  • lipases there is a strong preference for the use of unprotected amino acid esters
  • proteases there is a preference for protected (N-protected) amino acid esters, for instance N-benzyloxycarbonyl-protected esters.
  • the present example illustrates the use of lipases and proteases, respectively, in the enantioselective ammonolysis

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Abstract

L'invention concerne un procédé permettant de réaliser des conversions catalysées par voie enzymatique de composés organiques. Ledit procédé consiste à faire réagir un ester d'acide organique dans une phase organique liquide avec de l'ammoniac en présence d'une enzyme hydrolytique telle que la lipase, l'estérase ou la protéase. Ce procédé permet de préparer de manière hautement énantiosélective et rentable des énantiomères d'amides, d'esters et/ou d'alcools à partir d'un produit de départ racémique dans des conditions de réaction très douces.
PCT/EP1994/003038 1993-09-10 1994-09-12 Procede de conversion catalysee par voie enzymatique de composes organiques WO1995007359A1 (fr)

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AU76964/94A AU7696494A (en) 1993-09-10 1994-09-12 A process for carrying out enzymatically catalyzed conversions of organic compounds

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NL9301574A NL9301574A (nl) 1993-09-10 1993-09-10 Werkwijze voor het uitvoeren van enzymatisch gekatalyseerde omzettingen van organische verbindingen.
NL9301574 1993-09-10

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Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0759426A2 (fr) * 1995-08-17 1997-02-26 Bayer Ag Procédé pour la préparation d'aryl-1-alkylamines optiquement actives
EP0795609A2 (fr) * 1996-03-15 1997-09-17 Tanabe Seiyaku Co., Ltd. Procédé de préparation de composés trans-3-phénylglycidamidiques optiquement actifs
US5847122A (en) * 1996-02-23 1998-12-08 Tanabe Seiyaku Co., Ltd. Process for preparing 1,5-benzothiazepine derivative
WO1999007875A1 (fr) * 1997-08-07 1999-02-18 Tanabe Seiyaku Co., Ltd. Procede permettant de preparer des composes de (2r,3s)-3-(phenyle substitue ou non substitue)-glycidamide par amidation asymetrique
WO2000058490A1 (fr) * 1999-03-29 2000-10-05 Technische Universiteit Delft Synthese d'amide primaire d'acides carboxyliques avec une lipase
FR2900926A1 (fr) * 2006-05-15 2007-11-16 Ppg Sipsy Soc Par Actions Simp Procede de synthese d'ester de l'acide trans-4-amino-cyclohexanecarboxylique
WO2010118498A1 (fr) * 2009-04-14 2010-10-21 Her Majesty The Queen In Right Of Canada As Represented By The Minister Of Natural Resources Biotraitement de pétrole pour empêcher la corrosion en raffinerie

Non-Patent Citations (8)

* Cited by examiner, † Cited by third party
Title
CHEMICAL ABSTRACTS, vol. 70, no. 17, 28 April 1969, Columbus, Ohio, US; abstract no. 74630x, S.E.BRESLER ET AL.: "Mechanisms of the tryptic hydrolysis of ester and amide bonds." page 40; *
CHEMICAL ABSTRACTS, vol. 97, no. 11, 13 September 1982, Columbus, Ohio, US; abstract no. 87938m, D.PETKOV: "Enzyme peptide synthesis and semisynthesis: kinetic and thermodynamic aspects." page 378; *
INT.CONF.CHEM.BIOTECHNOL.BIOL.ACT.NAT.PROD.,(PROC.),1ST, vol. 2, 1981, pages 469 - 479 *
MARIA JESUS GARCIA ET AL.: "Chemoenzymatic aminolysis and ammonolysis of beta-ketoesters", TETRAHEDRON LETTERS., vol. 34, no. 38, 17 September 1993 (1993-09-17), OXFORD GB, pages 6141 - 6142 *
MOL.BIOL., vol. 3, no. 1, 1969, USSR, pages 15-28 *
SUSANA PUERTAS ET AL.: "Lipase catalyzed aminolysis of ethyl propiolate and acrylic esters.Synthesis of chiral acrylamides.", TETRAHEDRON, (INCL. TETRAHEDRON REPORTS), vol. 49, no. 19, 1993, OXFORD GB, pages 4007 - 4014 *
VICENTE GOTOR ET AL.: "A simple procedure for the preparation of chiral amides.", TETRAHEDRON LETTERS., vol. 29, no. 52, 1988, OXFORD GB, pages 6973 - 6974 *
VICENTE GOTOR ET AL.: "Enzymatic aminolysis and transamidation reactions", TETRAHEDRON, (INCL. TETRAHEDRON REPORTS), vol. 47, no. 44, 1991, OXFORD GB, pages 9207 - 9214 *

Cited By (14)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0759426A2 (fr) * 1995-08-17 1997-02-26 Bayer Ag Procédé pour la préparation d'aryl-1-alkylamines optiquement actives
EP0759426A3 (fr) * 1995-08-17 1999-06-30 Bayer Ag Procédé pour la préparation d'aryl-1-alkylamines optiquement actives
US5847122A (en) * 1996-02-23 1998-12-08 Tanabe Seiyaku Co., Ltd. Process for preparing 1,5-benzothiazepine derivative
EP0795609A2 (fr) * 1996-03-15 1997-09-17 Tanabe Seiyaku Co., Ltd. Procédé de préparation de composés trans-3-phénylglycidamidiques optiquement actifs
EP0795609A3 (fr) * 1996-03-15 1999-02-17 Tanabe Seiyaku Co., Ltd. Procédé de préparation de composés trans-3-phénylglycidamidiques optiquement actifs
WO1999007875A1 (fr) * 1997-08-07 1999-02-18 Tanabe Seiyaku Co., Ltd. Procede permettant de preparer des composes de (2r,3s)-3-(phenyle substitue ou non substitue)-glycidamide par amidation asymetrique
WO2000058490A1 (fr) * 1999-03-29 2000-10-05 Technische Universiteit Delft Synthese d'amide primaire d'acides carboxyliques avec une lipase
FR2900926A1 (fr) * 2006-05-15 2007-11-16 Ppg Sipsy Soc Par Actions Simp Procede de synthese d'ester de l'acide trans-4-amino-cyclohexanecarboxylique
WO2007132119A1 (fr) * 2006-05-15 2007-11-22 Ppg-Sipsy Procede in situ ou 'one pot' d'hydrogenation et d'amination reductrice.
WO2010118498A1 (fr) * 2009-04-14 2010-10-21 Her Majesty The Queen In Right Of Canada As Represented By The Minister Of Natural Resources Biotraitement de pétrole pour empêcher la corrosion en raffinerie
US20120028341A1 (en) * 2009-04-14 2012-02-02 Heerze Louis D Petroleum bioprocessing to prevent refinery corrosion
EP2419493A1 (fr) * 2009-04-14 2012-02-22 Her Majesty The Queen In Right Of Canada As Represented By The Minister Of Natural Resources Canada Biotraitement de pétrole pour empêcher la corrosion en raffinerie
EP2419493A4 (fr) * 2009-04-14 2014-09-24 Her Majesty The Queen In Right Of Canada As Represented By The Minister Of Natural Resources Canada Biotraitement de pétrole pour empêcher la corrosion en raffinerie
US9404051B2 (en) 2009-04-14 2016-08-02 Her Majesty The Queen In Right Of Canada As Represented By The Minister Of Natural Resources Petroleum bioprocessing to prevent refinery corrosion

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NL9301574A (nl) 1995-04-03

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