EP1848809A2 - Utilisation d'emulsions pit dans des reactions biocatalytiques - Google Patents

Utilisation d'emulsions pit dans des reactions biocatalytiques

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Publication number
EP1848809A2
EP1848809A2 EP06706695A EP06706695A EP1848809A2 EP 1848809 A2 EP1848809 A2 EP 1848809A2 EP 06706695 A EP06706695 A EP 06706695A EP 06706695 A EP06706695 A EP 06706695A EP 1848809 A2 EP1848809 A2 EP 1848809A2
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EP
European Patent Office
Prior art keywords
use according
emulsions
linkage
enzymes
reaction
Prior art date
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EP06706695A
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German (de)
English (en)
Inventor
Albrecht Weiss
Eric Dubreucq
Jean-Pierre Molitor
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Cognis IP Management GmbH
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Cognis IP Management GmbH
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Publication of EP1848809A2 publication Critical patent/EP1848809A2/fr
Withdrawn legal-status Critical Current

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Classifications

    • 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
    • C12P13/002—Nitriles (-CN)
    • C12P13/004—Cyanohydrins

Definitions

  • the present invention relates to the use of emulsions prepared by the PIT process as a reaction medium for biocatalytic reactions.
  • biocatalytic methods for synthesis are described, for example, in K. Drauz and H. Waldmann, Enzymes Catalysis in Organic Synthesis, WILEY-VCH, Volumes I to III, 2002; U.T. Bornscheuer, RJ. Kazlauskas in Hydrolases in Organic Synthesis.
  • the technical implementation of biocatalytic processes is described by A. Liese, K. Seelbach and C. Wandrey in Industrial Biotransformations, WILEY-VCH, 2002.
  • biocatalysts enzymes and microorganisms in the form of whole cells or in the form of active cell components. It is often disadvantageous that the solvents used adversely affect the reactivities of the catalysts used - enzymes or whole microorganisms and their cell constituents. Thus, the solvents can lead to denaturation of the biocatalysts and thus reduce the biocatalyst performance or destroy completely.
  • a large interface between the hydrophilic and the hydrophobic phase is necessary.
  • a large surface is created when the smallest possible droplets of a phase, for example, by stirring or homogenizing are generated.
  • biocatalytic reactions are often the availability and stability of the catalysts involved in the process. Enzymes or microorganisms which are stabilized by immobilization, for example by microencapsulation and can be used repeatedly, are already known from the prior art. In order for the biocatalysts to be used for commercial applications, new biocatalysts with suitable stability are frequently being sought. More modern methods make use of e.g. the "directed evolution" to develop the desired profile of the biocatalysts.
  • the reaction of hydrophobic compounds can already be carried out by the use of water in oil (W / O) microemulsions, as described by Orlich and Schomaeker in Enzyme Microb. Technol .; 2001; 28; 1; 42-48 for the lipase from Candida rugosa.
  • W / O water in oil
  • the object of the present invention was therefore to provide a system for biocatalyzed reactions in which solvents which can damage the biocatalyst can be avoided and yet substances can be reacted which dissolve poorly in aqueous systems.
  • the reaction should proceed under mild mixing conditions in order to limit or avoid the negative effects already described above.
  • the substrate concentrations should be able to be varied, but the high interface and thus the concentrations of oil and water remain constant so far that they have no great influence on the reaction and on the activity of the enzyme.
  • these systems should be inexpensive and recyclable and not or only slightly affect the biocatalyst in its stability. This should also be such enzymes can be used, which show too poor stability in classically used organic solvent systems.
  • the invention relates to the use of O / W emulsions as a reaction medium for biocatalytic reactions, containing at least water, emulsifiers and a ⁇ lpha- se, wherein the emulsion is prepared by the PIT method and has a droplet size of 50 to 400 nm.
  • Emulsions are disperse preparations of at least two non-dissolvable liquids, one of which is aqueous.
  • Emulsifiers or emulsifier systems are used to homogenize immiscible oil / water phases by emulsification. Without the influence of stabilizing emulsifiers, the phases would separate again because of their different polarities.
  • the amphiphilic emulsifiers sit at the interfaces between the finely divided droplets and the coherent phase and prevent their coalescence through steric or electrostatic shielding.
  • Emulsifiers are compounds that combine hydrophilic and lipophilic building blocks in their molecular structure.
  • Emulsifiers or emulsifier systems are often characterized by the HLB (number) value, which makes a statement on the hydrophilic-lipophilic balance.
  • HLB number
  • emulsifiers or emulsifier systems with comparatively highly hydrophilic proportions lead to high HLB values and in their practical application generally to the water-based O / W emulsions with disperse oil phase.
  • E-emulsifiers or emulsifier systems with comparatively highly lipophilic fractions lead to comparatively lower HLB values and thus to the W / O invert emulsion with closed oil phase and disperse water phase.
  • the location of the PIT depends on many factors, for example the type and the phase volume of the oil component, the hydrophilicity and the structure of the emulsifiers and the composition of the emulsifier system.
  • Essential for the fineness of the PIT emulsion is its production process.
  • the water and oil phases are mixed with the emulsifiers and then heated to a temperature above the PIT.
  • the conductivity must fall to zero.
  • the emulsion is then cooled back to the starting temperature (usually room temperature, approx. 20 ° C).
  • the formation of the emulsion used according to the invention takes place only when the PIT is exceeded and the subsequent drop below the PIT.
  • PIT emulsions are particularly finely divided, which form a microemulsion phase with low interfacial tension between oil and water or a lamellar liquid-crystalline phase in the phase inversion.
  • the decisive step is always the reverse inversion on cooling.
  • the emulsions according to the invention are distinguished in particular by their fineness.
  • the droplet size is 50 to 400 ⁇ m.
  • the droplet size is preferably in the range from 70 to 300 nm, in particular in the range from 80 to 250 nm and particularly preferably in the range from 90 to 160 nm.
  • a distribution according to Gauss is assumed. The measurement is carried out, for example, by light scattering or absorption.
  • These finely divided emulsions retain their homogeneity through Brownian motion. This Brownian motion is a thermal random motion of particles ⁇ 5 ⁇ m. It is the driving force of diffusion and hinders both sedimentation and flotation.
  • a big advantage is that energy-consuming stirring processes can be reduced. It leads to an improved diffusion of substrate and enzyme and to reduced energy costs.
  • the substrate concentrations can be varied without having to change the droplet size.
  • a high substrate concentration can be achieved without a coalescence of the droplets occurring.
  • the low surface tension increases the transfer rate of the molecules at the oil / water interface.
  • the high reproducibility and stability of the PIT emulsions enable biochemical studies on enzymes and their reactivity as well as the possibility to further optimize already known reaction conditions and activities for enzymes.
  • the emulsions according to the invention are distinguished by the fact that they exhibit sufficient stability during the reaction phase during the use according to the invention. This implies that disintegration of the emulsion prepared by the PIT process is not detrimental to the desired reaction and is desired in a preferred embodiment. This has the advantage that a simplified processing of the products can be achieved.
  • the PIT emulsions contain, in addition to water, an oil phase which contains compounds from the group of mineral oils and fatty acid alkyl esters a) or of the native oils of vegetable origin and their oleochemical derivatives b).
  • Groups a) and b) are hydrophobic compounds which are insoluble or only sparingly soluble in water and which may preferably be the starting materials, ie substrates for the products desired by biocatalytic catalysis but may also be used as auxiliaries. These are essentially fatty acid esters, fatty alcohol ethers, fatty alcohol esters, and fatty acid polyol esters.
  • Suitable esters of group a) are derived in particular from saturated, unsaturated, linear or branched fatty acids having a total of 7 to 23 carbon atoms. These are therefore compounds of the formula (I)
  • R 1 is an alkyl radical having 6 to 22 C atoms and R 2 is an alkyl radical having 1 to 4 C atoms, with methyl and ethyl radicals being particularly preferred.
  • methyl esters Most advantageous is the use of methyl esters.
  • the methyl esters of the formula (I) can be obtained in a customary manner, for example by transesterification of triglycerides with methanol and subsequent distillation become.
  • Suitable fatty acids are caproic, heptane, caprylic, perlagonic, capric, undecane, lauric, tridecane, myristic, pentadecane, palmitic, heptadecane, stearic, nonadecan, Arachin and behenic acid.
  • Unsaturated representatives are, for example, lauroelein, myristolein, palmitoleic, petroselaidin, oil, elaidin, ricinoleic, linoleic, conjugated linoleic acid (CLA), in particular the cis9, transl-CLA or the translO, cis12- CLA, linoleic, linolenic, conjugated linoleic gadoleic, arachidonic and erucic acid. Mixtures of the methyl esters and / or ethyl esters of these acids are also suitable.
  • PIT emulsions which contain methyl esters and / or ethyl esters from the group of methyl oleate, methylpamitate, methyl stearate, methyl pelargonate, ethyl oleate, ethyl pamitate, ethyl stearate and / or ethyl pelargonate.
  • methyl esters and / or ethyl esters based on natural fatty acid mixtures such as, for example, from linseed, coconut, palm, palm kernel, olive, castor oil, rapeseed, soybean or sunflower oils (in the case of rape seed and sunflower oils Sunflower oil each new and old varieties) are obtained.
  • Suitable compounds of group b) are native oils of plant origin and their oleochemical derivatives. These are essentially mineral oils, fatty acid esters, fatty acid ethers, fatty alcohol ethers, fatty alcohol esters, fatty acid polyol esters such as preferably triglycerides and triglyceride mixtures, the glycerol in each case being completely esterified with longer-chain fatty acids. Particularly suitable vegetable oils are selected from the group peanut, coconut and / or sunflower oil.
  • emulsifiers or emulsifier systems used.
  • the emulsifiers used are preferably nonionic emulsifiers, in particular ethoxylated fatty alcohols and fatty acids.
  • a two-component emulsifier system comprising a hydrophilic emulsifier (A) and a hydrophobic coemulsifier (B).
  • Suitable hydrophilic nonionic emulsifiers (A) are substances which have an HLB value of about 8 to 18.
  • the HLB value hydrophilic-lipophilic balance
  • L is the weight fraction of the lipophilic groups, i. is the fatty alkyl or fatty acyl groups in percent in the ethylene oxide addition products.
  • R 3 is -O- (CH 2 CH 2 O) n -H (II)
  • R 3 is a linear or branched, saturated or unsaturated alkyl radical having 6 to 24 carbon atoms and n is a number from 1 to 50. Particular preference is given to those compounds of the formula (II) in which n is a number from 1 to 35 and in particular from 1 to 15. Particular preference is furthermore given to those compounds of the formula (II) in which R 3 is an alkyl radical having 16 to 22 carbon atoms.
  • the compounds of the formula (II) are obtained in a manner known per se by reacting fatty alcohols with ethylene oxide under pressure, if appropriate in the presence of acidic or basic catalysts.
  • Typical examples are caproic alcohol, capryl alcohol, 2-ethylhexyl alcohol, capric alcohol, lauryl alcohol, isotridecyl alcohol, myristyl alcohol, cetyl alcohol, palmoleyl alcohol, stearyl alcohol, isostearyl alcohol, oleyl alcohol, elaidyl alcohol, petroselinyl alcohol, linolyl alcohol, linolenyl alcohol, elaeostearyl alcohol, arachyl alcohol, gadoleyl alcohol, behenyl alcohol, erucyl alcohol and brassidyl alcohol and their technical mixtures, eg incurred in the high-pressure hydrogenation of technical methyl esters based on fats and oils or aldehydes from the Roelen oxo synthesis and as
  • Fatty acid ethoxylates which are also suitable as emulsifier component (A), preferably follow the formula (III),
  • R 4 is a linear or branched alkyl radical having 12 to 22 carbon atoms and m is a number from 5 to 50 and preferably 12 to 35.
  • Typical examples are adducts of 10 to 30 moles of ethylene oxide with lauric acid, isotridecanoic acid, myristic acid, palmitic acid, palmitoleic acid, stearic acid, isostearic acid, oleic acid, elaidic acid, petroselinic acid, linoleic acid, linolenic acid, elaeostearic acid, arachidic acid, gadoleic acid, behenic acid and erucic acid, and the like technical mixtures which are obtained, for example, in the pressure splitting of natural fats and oils or in the reduction of aldehydes from Roelen's oxosynthesis.
  • addition products of 10 to 30 moles of ethylene oxide are used to fatty acids having 16 to 18 carbon atoms.
  • Partial glycerides which are suitable as emulsifier component (B), preferably follow the formula (IV), CH 2 O (CH 2 CH 2 O) x -COR 5
  • COR 5 is a linear or branched acyl radical having 12 to 22 carbon atoms and x, y and z are in total 0 or numbers of 1 to 50, preferably 15 to 35.
  • Typical examples of suitable for the purposes of the invention partial glycerides are lauric acid monoglyceride, KokosfettTexremonoglycerid, Palmitinklaremonoglycerid, stearic acid monoglyceride, Isostearinklaremonoglycerid, ⁇ lklaremonoglycerid, conjugated Linolklare- monoglycerides and Talgfettklaremonoglycerid and their adducts with 5 to 50 and preferably 20 to 30 moles of ethylene oxide.
  • monoglycerides or technical mono / Diglyceridgemische are used with predominantly Monoglyceridanteil of formula (IV), in which COR 5 is a linear acyl radical having 16 to 18 carbon atoms.
  • emulsifier mixtures which contain the components (A) and (B) in a weight ratio of 10:90 to 90:10, preferably 25:75 to 75:25 and especially 40:60 to 60:40.
  • Suitable further emulsifiers are, for example, nonionic surfactants from one of the following groups:
  • alkyl mono- and oligoglycosides having 8 to 22 carbon atoms in the alkyl radical and their ethoxylated analogs
  • Adducts of 15 to 60 moles of ethylene oxide with castor oil and / or hydrogenated castor oil Adducts of 15 to 60 moles of ethylene oxide with castor oil and / or hydrogenated castor oil; Polyol and in particular polyglycerol esters such as e.g. Polyglycerol polyricinoleate or
  • Polyglycerol poly-12-hydroxy are also suitable are mixtures of compounds of several of these classes of substances;
  • the addition products of ethylene oxide and / or of propylene oxide to glycerol mono- and diesters and sorbitan mono- and diesters of fatty acids or castor oil are known, commercially available products. These are homolog mixtures whose average degree of alkoxylation corresponds to the ratio of the amounts of Ethylene oxide and / or propylene oxide and substrate, with which the addition reaction is carried out corresponds.
  • the PIT emulsions used according to the invention preferably contain from 20 to 90% by weight of water, in particular from 30 to 80% by weight and very particularly preferably from 30 to 60% by weight.
  • the oil phase itself is preferably contained in amounts of from 10 to 80% by weight, in particular from 40 to 70% by weight.
  • the oil phase preferably contains exclusively the components a) or b) or mixtures of these components.
  • the emulsifiers or emulsifier systems are preferably present in amounts of from 1 to 25% by weight, in particular in amounts of from 5 to 20 and particularly preferably in amounts of from 5 to 15% by weight.
  • the emulsions used in the invention have vorzugswei- se to phase inversion temperatures in the range of 20 to 95 ° C and especially from 30 to 95 0 C.
  • the emulsions used according to the invention are developed according to the properties of the educts by the correct selection and composition of oil component and emulsifiers. Preference is given to using emulsions which comprise fatty acid alkyl esters or fatty alcohol ethers and an emulsifier mixture based on ethoxylated hydroxyfatty acid triglycerides.
  • the biocatalysts used according to the invention are enzymes or whole cells or cell parts. They are able to react catalytically at interfaces.
  • the biocatalysts are preferred as isolated enzymes.
  • enzymes from the group of lyases and / or oxidoreductases are used which can be used either alone or in combination with a plurality of enzymes.
  • Lyases are in the IUBMB classification representatives of the 4th main group of enzymes. There are four important subclasses (CC, CO, CN 3 CS lyases, EC 4.1 to 4.4). Lyases non-hydrolytically cleave or add certain groups from their substrate, leaving a double bond or adding groups to double bonds.
  • the oxidoreductases are the first of the 6 main groups of enzymes that catalyze Red ⁇ x reactions.
  • the subgroup depends mostly on the type of electron donor and is divided into subgroups again according to the type of electron acceptor.
  • the systematic names are formed according to the pattern: DonoriAcceptor oxidoreductase.
  • Preferred in the context of the invention are lyases selected from the group formed by hydroxynitrilases, nitrilases, nitrile hydratases, oxynitrilases, carboxylases and aldolases.
  • the oxidoreductases are preferably selected from the group formed by dehydrogenase, hydroxylase, laccase, lipoxygenase, reductase, oxidase, peroxidase and oxygenase.
  • enzymes in the sense of biocatalysts are hydroxynitrile lyases.
  • Suitable enzymes are lyases and / or oxidoreductases of organisms selected from the group formed by Alcaligenes, Aspergillus, Aeromonas aerophila, Bacillus, Candida Chromobacterium viscosum, Fusarium solani, Geotrichum candidum, Hevea. Issatchenkia orientalis (Candida krusei), Kluyveromyces marxianus (C. kefyr, C.pseudotropicalis), Linum, Manihot.
  • lyases and / or oxidoreductases of organisms selected from the group formed by Alcaligenes, Aspergillus, Aeromonas aerophila, Bacillus, Candida Chromobacterium viscosum, Fusarium solani, Geotrichum candidum, Hevea. Issatchenkia orientalis (Candida krusei), Kluyveromyces marxianus (C. kefyr, C.
  • Mucor javanicus Nocardia, Penicilium camenberti, Penicilium roqueforti, Pichia, Pseudomonas, Pseudomonas, Prunus, Rhizomucor, Rhizopus, Sorghum and Thermomyces and mixtures thereof.
  • the enantioselective enzymes are particularly preferred.
  • the lyases are of plant origin. They can be isolated from all components of the plants, preferably both from the leaves, the stem or stalk, as well as the fruit.
  • the oxidoreductases are preferably of microbial origin.
  • the enzymes to be used according to the invention can be used in various forms. In principle, all dosage forms of enzymes customary to the person skilled in the art can be used. According to the invention, the term “enzyme” also includes the terms protein and enzyme protein According to the invention, both the enzyme protein and the total protein which comprises the function of the protein according to the invention in a part of the protein sequence are preferably used.
  • the enzyme preparation used is either immobilized on a carrier material and / or in solution, in particular in aqueous solution, and reused in so-called “repeated batches.” Also preferred are crystallized enzymes, so-called CLECs, for example W 2
  • the proportion of active enzyme in the respective technical enzyme preparations varies from manufacturer to manufacturer. The proportion is, however, on average between 1 and 10% active enzyme.
  • the enzymes to be used according to the invention are used in a further embodiment of the invention having an activity of 20-5000 U / ml aqueous phase, calculated as pure enzyme or as an enzyme preparation, in particular the activities to be employed are 30-3000 U / ml aqueous phase.
  • the biocatalytic reactions are preferably C-C linkages, C-N linkage, C-O linkage or C-S linkage.
  • Preferred within the meaning of the invention are enantioselective reactions which lead to chiral compounds with an enantiomeric purity of 98-99 ee.
  • the chiral compounds can be obtained by the use of enantioselective enzymes.
  • the preparation of chiral compounds is preferred for the purposes of the invention.
  • the biocatalytic reactions using the PIT emulsion according to the invention produce fine chemicals as intermediates for cosmetic and / or pharmaceutical products and / or as intermediates for use in agro-areas.
  • the fine chemicals are cyanhydrins, in particular enantiomerically pure cyanohydrins.
  • the preparation of enantiomerically pure cyanohydrins in both the (S) and (R) configurations opens up many possibilities for stereoselective sequential reactions such as hydrolysis to chiral hydroxy acids.
  • the O / W emulsions according to the invention containing at least water, emulsifiers and an oil phase and prepared by the PIT process are outstandingly suitable for use as reaction medium for biocatalytic reactions. From this, a further object of the invention can be derived directly. It is a process for biocatalytic C [BOND] C bonds, CN linking, CO linking or CS linking, in which O / W emulsions are used as the reaction medium, which are prepared by the PIT process.
  • the emulsions used for the process according to the invention correspond in their constituents, conditions and further embodiments to the emulsions which have already been described in detail for the use of these O / W emulsions.
  • the process according to the invention preferably produces fine chemicals as intermediates for cosmetic and / or pharmaceutical products and / or as intermediates for use in agro-areas.
  • cyanohydrins are produced.
  • the PIT emulsions comprising the substrate are added to the reaction vessel which immobilizes or does not immobilize the biocatalysts and optionally contains further auxiliaries and additives.
  • the details of this process in particular the amount of biocatalyst and the metered emulsion, arise from the nature of the biocatalyst and the selected PIT emulsion and can be adapted by the skilled person to the specific circumstances.
  • a phase separation can be achieved and the product in the oil phase can be easily separated from the aqueous phase.
  • separation and reuse of the enzyme is provided.
  • the fineness of the oil droplets results in a large surface area between the oil and water phases, allowing for rapid contact and reaction rate between the biocatalysts and the oil phase containing the substrates.
  • reaction conditions of the biocatalytic reaction according to the invention depend on the optimum reaction range of the selected enzymes and on the emulsions used. In particular, these are conditions in which, inter alia, the reaction temperature between 4 and 50 ° C, preferably a temperature between 15 and 40 ° C, in particular a temperature of 20 ° C is selected.
  • the temperature can be reduced to temperatures between 0 ° and 20 ° C to reduce side reactions. In these cases, a temperature between 3 ° C to 15 ° C is preferred.
  • R-oxynitrilase EC 4.1.2.10, R-mandelonitrile lyase, R-acetone-cyanohydrine lyase
  • Prusius amygdalus 38 U / ml solution FLUKA
  • R - (+) - Madelonitrile > 99% Aldrich; Benzaldehyde (> 99%, redistilled, Aldrich); KCN (analytical grade, FLUKA) sodium phosphate (prolabo); Eumulgin HRE 40 (from Cognis); Methyl oleate (ex Cognis); Cetiol OE (CETIOL® OE 1 INCI: dicaprylyl ether from Cognis); Ultra-pure water (Milipore MiIIiQ +); Ethanol (Carlo Erba).
  • Two PIT emulsions were prepared. One contains benzaldehyde dissolved in methyloleate, the other contains benzaldehyde dissolved in cetiol OE. The final composition was: 0.5 g methyloleate or cetiol OE / 0.5 g eumulgin HRE 40 / 0.4 ml benzaldehyde / 1.4 ml water.
  • the PIT emulsion was further diluted by adding 1 ml of water. Both emulsions remain stable at 4 ° C for weeks. For each experiment, fresh emulsions were prepared to avoid the degradation of benzaldehyde.
  • the reaction medium was formed by: 1.2 ml of phosphate buffer (pH 5.7, 50 mM); 0.4 ml cyanide solution, (5 g KCN in 10 ml water); 0.2 ml PIT emulsion; 0.2 ml (7.6 U) of enzymes or 0.2 ml of buffer.
  • the reactions were carried out in closed (Teflon layer) 4 ml Wheaton vials without stirring except for the random sample.
  • the reaction rate was the Benzaldehydumwandlung 0.30 micromol / ml / h in the presence of benzaldehydes / Cetiol systems at 4 0 C and 0.14 micromol / ml / h with benzaldehyde / methyloleates at 4 0 C.

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Abstract

L'invention concerne l'utilisation d'émulsions huile dans eau en tant que milieu de réaction pour des réactions biocatalytiques, contenant au moins de l'eau, un émulsifiant ainsi qu'une phase huileuse, caractérisée en ce que l'émulsion est produite selon le procédé PIT, et une taille de goutellettes comprise entre 50 et 400 nm. Les enzymes insérées correspondent à des lyases et/ou à des oxydoréductases.
EP06706695A 2005-02-16 2006-02-07 Utilisation d'emulsions pit dans des reactions biocatalytiques Withdrawn EP1848809A2 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102005007174A DE102005007174A1 (de) 2005-02-16 2005-02-16 Verwendung von PIT-Emulsionen in biokatalytischen Reaktionen
PCT/EP2006/001041 WO2006087119A2 (fr) 2005-02-16 2006-02-07 Utilisation d'emulsions pit dans des reactions biocatalytiques

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EP1848809A2 true EP1848809A2 (fr) 2007-10-31

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US (1) US20080227170A1 (fr)
EP (1) EP1848809A2 (fr)
JP (1) JP2008530991A (fr)
DE (1) DE102005007174A1 (fr)
WO (1) WO2006087119A2 (fr)

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Publication number Priority date Publication date Assignee Title
DE102007034258A1 (de) * 2007-07-21 2009-01-22 Universität Dortmund Verfahren zur Aufarbeitung von koaleszenzgehemmten Emulsionen aus Ganzzell-Biotransformationen mit Kohlendioxid
EP2060251B1 (fr) * 2007-11-17 2011-03-23 Cognis IP Management GmbH Procédé de fabrication de concentrés de matière active

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AT406961B (de) * 1997-12-29 2000-11-27 Dsm Fine Chem Austria Gmbh Enzymatisches verfahren zur herstellung von (s)-cyanhydrinen
DE19923785A1 (de) * 1999-05-25 2000-11-30 Cognis Deutschland Gmbh Verwendung von PIT-Emulsionen in Fermentationsverfahren
US7510831B2 (en) * 2001-10-26 2009-03-31 Genencor International, Inc. Trichoderma reesei phytase enzymes, nucleic acids encoding such phytase enzymes, vectors and host cells incorporating same and methods of making and using same
AT411065B (de) * 2001-12-27 2003-09-25 Dsm Fine Chem Austria Gmbh Verfahren zur herstellung von heterocyclischen (r)- und (s)-cyanhydrinen
AT411064B (de) * 2001-12-27 2003-09-25 Dsm Fine Chem Austria Gmbh Verfahren zur herstellung von enantiomerenangereicherten cyanhydrinen unter verwendung von acetalen oder ketalen als substrate
DE10337451A1 (de) * 2003-08-14 2005-03-17 Cognis Deutschland Gmbh & Co. Kg Verwendung von PIT-Emulsionen in enzymatischen Reaktionen

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Title
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JP2008530991A (ja) 2008-08-14
WO2006087119A3 (fr) 2007-03-22
WO2006087119A2 (fr) 2006-08-24
DE102005007174A1 (de) 2006-08-24
US20080227170A1 (en) 2008-09-18

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