WO2010070086A2 - Procédé de conversion enzymatique d'alcanes - Google Patents

Procédé de conversion enzymatique d'alcanes Download PDF

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Publication number
WO2010070086A2
WO2010070086A2 PCT/EP2009/067493 EP2009067493W WO2010070086A2 WO 2010070086 A2 WO2010070086 A2 WO 2010070086A2 EP 2009067493 W EP2009067493 W EP 2009067493W WO 2010070086 A2 WO2010070086 A2 WO 2010070086A2
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Prior art keywords
monooxygenase
cofactor
alkanes
carbon atoms
sequence
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PCT/EP2009/067493
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German (de)
English (en)
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WO2010070086A3 (fr
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Harald GRÖGER
Edyta Burda
Ulrich Schwaneberg
Jan Marienhagen
Karlheinz Drauz
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Evonik Degussa Gmbh
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Publication of WO2010070086A2 publication Critical patent/WO2010070086A2/fr
Publication of WO2010070086A3 publication Critical patent/WO2010070086A3/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
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0071—Oxidoreductases (1.) acting on paired donors with incorporation of molecular oxygen (1.14)
    • 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
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/24—Preparation of oxygen-containing organic compounds containing a carbonyl group
    • C12P7/26—Ketones

Definitions

  • the invention relates to the hydroxylation of alkanes and the production of ketones from alkanes by enzymatic reactions.
  • cyclic ketones are of great importance to the chemical industry, with particular attention paid to cyclohexanone, cyclooctanone, cyclodecanone and cyclododecanone.
  • cyclohexanone there are various synthetic access routes starting from different basic chemicals. Particularly attractive is the selective direct conversion of cyclohexane to cyclohexanone using oxygen.
  • cyclododecanone also called cyclododecanone
  • cyclododecanone is considered to be a commercially attractive building block in the production of perfumes, UV absorbers and the monomers laurinlactam and dodecanedicarboxylic acid for the production of nylon-12 or nylon-6.12.
  • Cyclooctanone also called cyclooctanone
  • cyclododecanone consists in the aerial oxidation of the corresponding cycloalkane in the presence of boric acid to cycloalkylborate, followed by a subsequent hydrolysis of the borate to cycloalkanol and followed again by dehydration of the cycloalkanol.
  • a description of this technical process, for example for the synthesis of cyclododecanone can be found inter alia in T. Schiffer, G. Oenbrink, "cyclododecanol, cyclododecanone and laurolactam" in Ullmann's Encyclopedia of Industrial
  • the object underlying the present invention is to provide a novel process for the preparation of ketones from alkanes, which does not have the above-described disadvantages of the prior art.
  • This object is achieved by a process in which the conversion of an alkane into the desired ketone is carried out by enzymatic reaction in the presence of a monooxygenase, alcohol dehydrogenase and a suitable cofactor in an aqueous reaction medium in the presence of molecular oxygen.
  • the cofactor used is accepted by both enzyme components (both monooxygenase and alcohol dehydrogenase).
  • NAD (P) H-dependent enzyme components are used.
  • alkanes are generally compounds selected from the group consisting of straight or branched chain, saturated and monounsaturated hydrocarbons having 1 to 20 carbon atoms, in particular 6 to 12
  • Carbon atoms and cyclic hydrocarbons optionally substituted with 1 to 5 carbon atoms, saturated or mono- or polyunsaturated, mononuclear or polynuclear, in which the ring or rings has a total of 6 to 20 carbon atoms, preferably mononuclear, saturated hydrocarbons with 8 , 10 or 12 carbon atoms used.
  • the aqueous reaction system may be single-phase or two-phase and optionally organic solvents such.
  • organic solvents especially isopropanol, dimethyl sulfoxide (DMSO) or methyl tert-butyl ether (MTBE), or emulsifiers.
  • the alkane component for example a cycloalkane
  • the alkane is hydroxylated using and consuming molecular oxygen (O 2) to form the corresponding alcohol (eg cycloalkanol).
  • O 2 molecular oxygen
  • the reduced form of a cofactor eg NAD (P) H
  • P oxidized
  • NAD (P) + oxidized
  • the reaction can also be carried out by isolating the alcohol as a product if no alcohol dehydrogenase suitable for the second reaction step from the alkanol to the alkanone is used.
  • no alcohol dehydrogenase suitable for the second reaction step from the alkanol to the alkanone is used.
  • the process has proven particularly advantageous for the conversion of cycloalkanes to cycloalkanones, with the process for the production of cyclohexanone, cyclooctanone, cyclodecanone and cyclododecanone being used very preferably.
  • the preparation of cyclooctanone (Examples 3 and 5) and cyclodecanone (Example 4) using the method of the invention is described.
  • the process according to the invention is generally at 0 -
  • Monooxygenases Selected Representatives The skilled person is free in the choice of monooxygenase.
  • Preferred monooxygenases are so-called cytochrome P450 monooxygenases (heme monooxygenases).
  • cytochrome P450 monooxygenases which are also recombinantly available and well expressed by means of a bacterial or eukaryotic host organism, are preferably used.
  • the host organism used is preferably Escherichia coli, although other proven host organisms can be used in an advantageous manner.
  • monooxygenases examples include the monooxygenases derived from Bacillus megaterium (in particular the enzyme CYP102A1, also referred to as P450 BM-3) and Thermus thermophilus (in particular the enzyme CYP175A1) and in this case very preferably corresponding mutants suitable for the hydroxylation (Schmid, J. Pleiss, V. Urlacher, Chemistry News 2004, 52, 767-772).
  • the monooxygenase from Bacillus megaterium is described, for example, in D. Appel, S. Lutz-Wahl, P. Fischer, U. Schwaneberg, RD Schmid, J. Biotechnol. 2001, 88, 167-171, U. Schwaneberg, A.
  • a very preferred mutant here is the monooxygenase from P450 BM-3, in which
  • P450 BM-3 mutant F87V This enzyme (hereinafter this polypeptide is referred to as "P450 BM-3 mutant F87V"; the sequence SEQ ID NO: 2 corresponds to this polypeptide) is described in W.T. Sulistyaningdyah, J.
  • Alcohol dehydrogenases Selected representatives
  • alcohol dehydrogenase is free in the choice of alcohol dehydrogenase and will be based on such representatives, which are particularly suitable for the oxidation of the respective alkanol component and in this case by high specific enzyme activities and a dependence on the cofactors NADH and / or NADPH distinguished.
  • preferred alcohol dehydrogenases are the alcohol dehydrogenase from Lactobacillus kefir, described in W. Hummel, M. -R. KuIa, EP 456107, 1991, C.W. Bradshaw, W.
  • the genes can be selected for transformation of the host organism used to produce the encoded enzymes.
  • a polynucleotide encoding a polypeptide that is at least 90%, 95%, or 99% identical to the sequence shown in SEQ ID NO: 2 is used, with the amino acid at position as compared to the wild-type sequence 87 is substituted for another proteinogenic amino acid (eg Phe ⁇ VaI) and the polypeptide has the activity of a monooxygenase.
  • Preferred is a 100% identity with SEQ ID NO: 2.
  • the invention is also a
  • polynucleotide having the sequence from SEQ ID NO: 1 b) polynucleotide having a sequence corresponding to SEQ ID NO: 1 within the scope of the degeneracy of the genetic code c) polynucleotide having a sequence which corresponds to the complementary sequences to point a) or b ) hybridized under stringent conditions,
  • the invention also provides further mutants of SEQ ID NO: 2 which have been produced by deletion, transition, transversion or insertion at a maximum of 5 positions, which have a higher activity and / or stability and / or selectivity in comparison to the wild type.
  • SSC buffer at a temperature of about 50 0 C - 68 ° C are used.
  • probes can also hybridize with polynucleotides that have less than 70% identity to the sequence of the probe. Such hybrids are less stable and are removed by washing under stringent conditions. This can be achieved, for example, by lowering the salt concentration to 2 ⁇ SSC and optionally subsequently 0.5 ⁇ SSC (The DIG System Users Guide for Filter Hybridization, Boehringer Mannheim, Mannheim, Germany, 1995), a temperature of about 50 ° C. - 68 ° C is set. It may be possible to lower the salt concentration to 0.1 x SSC. By gradually increasing the salt concentration to 2 ⁇ SSC and optionally subsequently 0.5 ⁇ SSC (The DIG System Users Guide for Filter Hybridization, Boehringer Mannheim, Mannheim, Germany, 1995), a temperature of about 50 ° C. - 68 ° C is set. It may be possible to lower the salt concentration to 0.1 x SSC. By gradually
  • Hybridization temperature in steps of about 1 - 2 0 C from 50 ° C to 68 ° C polynucleotide fragments can be isolated, for example, at least 70% or at least 80% or at least 90% to 95% or at least 96% to 99% identity to the sequence possess the probe used. It is also possible to isolate polynucleotide fragments which have complete identity with the sequence of the probe employed. Further instructions for hybridization are available on the market in the form of so-called kits (eg DIG Easy Hyb from Roche Diagnostics GmbH, Mannheim, Germany, Catalog No. 1603558). In the method according to the invention, isolated enzymes but also whole-cell catalysts are used, with the use of recombinant whole-cell catalysts being quite preferred. In addition, both isolated enzymes and whole-cell catalysts can also be used in immobilized form, with the skilled person being free to choose the immobilization method.
  • kits eg DIG Easy Hyb from Roche Diagnostics GmbH, Mannheim, Germany, Catalog No. 1603558.
  • the cells used according to the invention which at least partially contain the enzymes required, preferably the monooxygenase and the alcohol dehydrogenase, can easily be separated off after the reaction. Also, the use of such (recombinant) cells is more economically attractive compared to isolated enzymes for the access of others
  • the reaction of the alkanes is preferably with quiescent cells. This refers to cells that are viable, but do not multiply under given conditions, and which have been transformed with the coding for the required enzymes nucleotide sequences.
  • Another object of the invention is the provision of in the selected host strains in general autonomously replicable vectors which are compatible with each other and contain at least one gene coding for one of the enzymes according to the invention.
  • Vector DNA can be introduced into eukaryotic or prokaryotic cells by known transformation techniques. Preference is given to vectors which contain nucleotide sequences coding for two enzymes, in particular z. For monooxygenase and alcohol dehydrogenase.
  • nucleotide sequences coding for monooxygenase and alcohol dehydrogenase on a vector.
  • the nucleotide sequence for the cofactor is typically located in the genomic DNA of the host organism.
  • a typical preparation of a whole-cell catalyst containing sufficient amounts of the cofactor formed in the recombinant strain for biotransformations see for example: H. Gröger, F. Chamouleau, N. Orologas, C. Rollmann, K. Drauz, W. Hummel, A. Weckbecker, O. May, Angew. Chem. 2006, 118, 5806-5809; Angew. Chem. In t. Ed. 2006, 45, 5677-5681.
  • the procedure is to clone a highly expressible or highly active gene into a low copy vector, lower expression genes on a higher copy vector and / or with a strong promoter.
  • the host cells are transformed with these vectors in such a way that compared to the starting organism they contain at least one additional copy of the nucleotide sequences coding for the two enzymes (monooxygenase and alcohol dehydrogenase).
  • the copy number of the corresponding genes can be increased, or the promoter and regulatory region or ribosome binding site located upstream of the structural gene can be mutated.
  • expression cassettes act, which are installed upstream of the structural gene.
  • genes or gene constructs may either be present in different copy number plasmids or be integrated and amplified in the chromosome. Alternatively, overexpression of the genes in question can be achieved by changing the composition of the medium and culture.
  • the overexpression leads to an increase in the intracellular activity or concentration of the corresponding enzymes.
  • the increase is generally at least 10 to 500%, in particular 50 to 500% or 100 to 500%, up to a maximum of 1000 or 2000% compared to the concentration or activity of the enzyme in the transformation-based organism (start organism) ,
  • the expression of the gene or the catalytic properties of the enzyme proteins can be reduced or eliminated. If necessary, both measures can be combined.
  • the reduction of gene expression can be achieved by appropriate
  • Signaling structures of gene expression include repressor genes, activator genes, operators, promoters, attenuators, ribosome binding sites, the start codon, and terminators. Details can be found on the
  • Mutations include transitions, transversions, insertions and deletions.
  • Suitable mutations in the genes can be incorporated into suitable strains by gene or allelic replacement.
  • the invention also relates to recombinant
  • Microorganisms in which a monooxygenase according to the invention and a suitable alcohol dehydrogenase are present in overexpressed form are present in overexpressed form.
  • such cells whole-cell catalysts
  • such cells typically still contain the cofactor NAD (P) H required for the biotransformation.
  • the cell walls are permeable by chemical or physical measures for the absorption of the substrates and delivery of the products.
  • the substrates are generally used in a concentration of> 0 to 700 g / L, preferably> 50 to 500 g / L, most preferably> 100 to 300 g / L.
  • the skilled person is free to choose in the way in which the substrate is added. In this case, for example, the entire amount of substrate already be submitted at the beginning of the reaction or alternatively the total amount or a subset of
  • Concentration is preferably understood to mean the ratio of the total amount of the substrate used / total amount of the aqueous reaction medium.
  • Another object of the invention are recombinant microorganisms in which only one mutant monooxygenase is present. These strains contain a polynucleotide sequence as shown in SEQ ID NO: 1 and are used for the hydroxylation of said alkanes (e.g., cycloalkanes). In these strains, no alcohol dehydrogenase is overexpressed.
  • the cofactor necessary for the reaction can in any case also be added to the reaction mixture if the cells do not produce it in sufficient quantity.
  • the cofactor can be added both in reduced form (eg NAD (P) H) and in oxidized form (NAD (P) + ).
  • the reaction is carried out either by addition of the reduced form of the cofactor (eg NAD (P) H) as described in Examples 3 and 4 or alternatively starting from the oxidized form and an additive which is the formation of the first Reduction step required reduced form of the cofactor.
  • the additive is preferably an alcohol (in particular isopropanol) which is oxidized in the presence of the alcohol dehydrogenase present and in which the oxidized form reduces the cofactor (eg NAD (P) + ) to the reduced form (eg NAD (P) H) (see Example 5).
  • This expression culture is incubated at 30 ° C. in a shaking incubator (250 rpm) until, at a spectrophotometrically determined cell density of 0.8-1.0 (wavelength: 578 nm), the expression of the monooxygenase gene on the plasmid by addition of isopropyl- ⁇ -D thiogalactopyranoside (concentration: 100 ⁇ M) is induced.
  • the medium is also supplemented with the heme precursor 5-aminolevulinic acid (final concentration: 500 ⁇ M). After 20 hours of expression, the E.
  • coli cells with expressed monooxygenase protein are harvested by centrifugation and the cells in PBS buffer (2 g NaCl, 0.2 g KCl, 1.44 g Na 2 HPO 4 , 0.24 g KH 2 PO4, pH 7, 4) once. After resuspension in phosphate buffer (50 mM, pH 7.5), the cells are lysed by ultrasound.
  • the monooxygenase proteins can be purified by anion exchange chromatography as previously described (U. Schwaneberg, U., A. Sprauer, C. Schmidt-Dannert, and RD Schmid. J. Chromatogr. 848, 149-159).
  • Example 2 Enzyme activities of the monooxygenase with the sequence ID NO. 2
  • the enzyme activity is determined spectrophotometrically at a wavelength of 340 nm by measuring the consumption of NADPH by oxidation to NADP + on the basis of a work protocol known from the literature (E. Burda, W. Hummel, H. Gröger, Angew Chem., 2008, 120, 9693) determined in the presence of the respective cycloalkane as substrate mM ⁇ 1 cm ⁇ 1 ).
  • spectrophotometric determination of the enzyme activity are first in a cuvette (1 mL) 690 ⁇ L phosphate buffer (pH 7.0, 50 mM), 10 .mu.l of a DMSO solution of cycloalkane (100 mM) and 100 .mu.L enzyme solution of the monooxygenase with the sequence ID NO. 2 (partially purified, lyophilized, NADPH-dependent). The reaction is then started after 5 minutes by adding 200 ⁇ l of a solution of NADPH (NADPH: 0.8 mM, phosphate buffer: pH 7.0, 50 mM) and measuring the consumption of NADPH. The relative activities were determined by comparing the spectrophotometrically obtained enzyme activities (in U / mg) with the enzyme activity obtained for the substrate cyclohexane (as a reference experiment with the relative activity 100%).
  • Reaction started by adding 0.01 mmol of the cofactor NADPH (6.5 mg). After shaking the reaction mixture with the aid of a thermomixer for 67 hours at a reaction temperature of 25 ° C, add 1 mL of dichloromethane and extract. Subsequently, the organic phase is freed from the solvent under reduced pressure and the conversion is determined directly from the crude product obtained using 1 H NMR spectroscopy. The conversion is 50% based on the formation of cyclooctanone, wherein the amount of cyclooctanol formed is ⁇ 5%.
  • Example 5 Oxidation of cyclooctane to cyclooctanone with isopropanol as additive and NADP + as cofactor

Abstract

L'invention concerne un procédé de production de cétones par oxydation enzymatique d'alcanes, consistant à faire réagir les alcanes en présence d'une mono-oxygénase, d'une alcool-déshydrogénase et d'un cofacteur adapté aux deux enzymes, dans un milieu réactionnel aqueux, en présence d'oxygène moléculaire.
PCT/EP2009/067493 2008-12-18 2009-12-18 Procédé de conversion enzymatique d'alcanes WO2010070086A2 (fr)

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DE102008054918.5 2008-12-18
DE102008054918A DE102008054918A1 (de) 2008-12-18 2008-12-18 Verfahren zur enzymatischen Umsetzung von Alkanen

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Cited By (1)

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WO2024004921A1 (fr) * 2022-06-27 2024-01-04 天野エンザイム株式会社 Polypeptide, oxygénase, et applications de son utilisation

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