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    • 专利摘要:
    The invention relates to a process for the enzymatic production of mercaptans from disulphides, and in particular methyl mercaptan from dimethyl disulfide.
    公开号:FR3041635A1
    申请号:FR1559257
    申请日:2015-09-30
    公开日:2017-03-31
    发明作者:Georges Fremy；Arnaud Masselin
    申请人:Arkema France SA；
    IPC主号:
    专利说明:

    PROCESS FOR PRODUCTION OF MERCAPTANS BY ENZYMATIC HYDROGENOLYSIS OF DISULFIDE
    The present invention relates to a process for the production by enzymatic catalysis of mercaptans, in particular methyl mercaptan, from disulphides, in particular dimethyl disulphide, and with the aid of reducing organic compounds.
    Mercaptans are of great use in many fields, for example as flavors, odorants for gas, chain transfer agents in polymerization, raw materials for the pharmaceutical or cosmetic industry, for the synthesis of antioxidants , extreme pressure or anti-wear additives for lubrication. These examples are in no way limiting the uses of mercaptans known today and which can be prepared by the method of the invention.
    In particular, the first of the mercaptans, methyl mercaptan (CH3SH), is of great industrial interest, particularly as a raw material for the synthesis of methionine essential amino acid widely used in animal feed. Methyl mercaptan is also a raw material that is widely used for the synthesis of many other molecules.
    The mercaptans can be synthesized by numerous methods such as the sulfhydration of alcohols, the catalytic or photochemical addition of hydrogen sulphide to unsaturated organic compounds, the substitution with hydrogen sulphide of halides, epoxides or organic carbonates, and others.
    In particular, methyl mercaptan is currently produced in large volume industrially from methanol and hydrogen sulfide according to reaction (1): CH 3 OH + H 2 S + CH 2 SH 2 + H 2 O (I) disadvantages of requiring methanol (CH3OH), of synthesizing hydrogen sulphide (H2S, from hydrogen and sulfur for example, hence the need to synthesize hydrogen as well) and lead to by-products of dimethyl ether type (CH3OCH3), dimethyl sulfide (CH3SCH3) and cracking products and water, which implies many steps of purification of methyl mercaptan.
    [0007] The description of processes based on these reactions, for example, in patent applications such as WO2013092129, WO2008118925, WO2007028708, WO2006015668, WO2004096760 is described.
    It may be economically interesting (to avoid the synthesis of methanol) to want to produce methyl mercaptan from carbon monoxide, hydrogen and hydrogen sulfide according to the following synthesis scheme (2): CO + However, these processes have the disadvantages of requiring synthesis gas (CO / H 2) and thus of steam reforming a hydrocarbon source. to have the right proportions between CO and H2 thus to be able to adjust the ratio CO / H2 with the so-called reaction of the "gas with the water" (CO + H2O -► CO2 + H2), and to synthesize the hhS.
    These processes also generally result in high levels of CO2 as a by-product, as well as methane, dimethylsulfide and water. Descriptions of these methods are provided by way of example in patent applications such as US2010286448, US2010094059, US2008293974, US2007213564.
    Still other methods have been described and combine different reactions such as: • Formation of CS2 and FhS from methane and sulfur (3): CH4 + 4 S -> CS2 + 2 H2S (3) Hydrogenation of CS2 (4): CS2 + 3 H2 - CH3SH + H2S (4) It is also possible to use the excess H2S of reactions (3) and (4) in reactions with methanol. (reaction 1) or synthesis gas (reaction 2) to give again methyl mercaptan.
    These methods obviously combine the disadvantages described for the reactions (1) and (2) with the additional difficulty of having excess hydrogen to perform the reaction (4). Descriptions of these methods can be found in patent applications such as US2011015443 or, more specifically, in reaction (4), in WO2010046607.
    The patent application WO200196290 proposes a method for synthesizing methylmercaptan directly from methane and H2S with hydrogen coproduction. This direct reaction between methane and H2S is done using pulsed plasma with corona discharge. This application does not describe any example of synthesis, it may seem difficult to imagine a process of industrial synthesis of methyl mercaptan on a large scale with this technology. In addition, this process requires the synthesis of H2S if it is not available.
    The patent application EP0649837 proposes a method for synthesizing methyl mercaptan by catalytic hydrogenolysis, with transition metal sulfides, dimethyl disulfide with hydrogen. This process, although efficient, requires relatively high temperatures of the order of 200 ° C to obtain productivities of interest industrially.
    Those skilled in the art also know that it is possible to prepare methyl mercaptan by acidification of an aqueous solution of sodium methylmercaptide (ChhSNa). This method has the major disadvantage of producing large amounts of salts, such as sodium chloride or sodium sulfate, depending on whether hydrochloric acid or sulfuric acid is used. These saline aqueous solutions are often very difficult to treat and traces of smelly products that remain make this method difficult to envisage on an industrial level.
    Processes for synthesizing mercaptans higher than methyl mercaptan also have many disadvantages. Thus the substitution of the alcohols with hydrogen sulphide requires temperatures and often high pressures, and leads to undesired by-products of the olefin, ether and sulphide type.
    The catalytic or photochemical addition of hydrogen sulfide to unsaturated compounds is generally carried out under slightly milder conditions than previously, but also leads to numerous by-products formed by isomerization of the raw material, by non-addition. regioselective or by double addition which gives sulphides. Finally, the substitution of halogenated derivatives leads to processes that generate a lot of effluents and saline discharges that are difficult to reconcile with industrial processes.
    The present invention aims to provide a new process for the preparation of mercaptans, in particular methyl mercaptan, which does not have the disadvantages described in the known processes of the prior art and previously detailed.
    More particularly, the present invention has as a first object the process for preparing a mercaptan of formula R-SH, comprising at least the steps of: a) preparing a mixture comprising: • a disulfide of formula RSS- R ', • a catalytic amount of amino acid carrying a thiol group or a peptide with a thiol group, • a catalytic amount of enzyme reductase corresponding to said amino acid carrying a thiol group or said peptide with a thiol group A catalytic amount of NADPH, b) addition of a reducing organic compound in stoichiometric amount relative to the disulfide and DMDS) with a catalytic amount of the corresponding enzyme dehydrogenase, c) conducting the enzymatic reaction, d) recovering the mercaptan of formula R-SH and mercaptan of formula R'-SH, e) separation and optional purification of mercaptan of formula R-SH and mercaptan of formula R'-SH.
    In the context of the present invention, any disulfide corresponding to the general formula R-S-S-R 'may be engaged in the mercaptan production process. In the general formula RSS-R ', R and R', which may be identical or different, represent, independently of one another, a linear, branched or cyclic hydrocarbon-based radical containing from 1 to 20 carbon atoms, said chain being saturated or carrying one or more unsaturations in the form of double (s) or triple (s) bond (s). R and R 'can also form together with the sulfur atoms which carry them a cyclic molecule comprising from 4 to 22 atoms, preferably from 5 to 10 atoms.
    According to a preferred aspect, the radicals R and R ', which may be identical or different, are chosen independently of one another from among the alkyl, cycloalkyl, aryl, alkylaryl and arylalkyl radicals comprising from 1 to 20 carbon atoms. carbon, preferably from 1 to 12 carbon atoms, more preferably from 1 to 6 carbon atoms, linear or branched, saturated or not, and optionally functionalized by one or more selected functions, in a nonlimiting manner and as examples among the alcohol, aldehyde, ketone, acid, amide, nitrile or ester functional groups, or the functions carrying sulfur, phosphorus, silicon or halogen.
    The disulfide of formula R-S-S-R 'is capable of being reduced, according to the process of the invention, to mercaptan of formula R-SH and to mercaptan of formula R'-SH. When R is different from R ', we speak of asymmetric disulfide, and when R and R' are identical, we speak of symmetrical disulfide. In the case of symmetrical disulfides R-S-S-R, the process of the invention leads to a mercaptan of formula R-SH. According to a very particularly preferred aspect of the invention, dimethyl disulfide (DMDS) is used in order to produce methyl mercaptan CHSSH.
    In the case of asymmetric disulfide RSS-R ', the process of the invention leads to a mixture of mercaptans of formulas R-SH and R'-SH which can be used as such or else subject to one or more separation operations well known to those skilled in the art, for example distillation.
    It is also possible to implement in the process of the invention mixtures of a plurality of disulfides, symmetrical and / or asymmetrical. Possible disulfide mixtures may include DSOs ("DiSulfide Oils" in English), said DSOs thus finding a valuation possibility quite interesting.
    According to the process of the invention, the mercaptans or products are generally recovered in solid, liquid and / or gaseous form.
    The production process according to the invention is based on the enzymatic reduction of disulfides, in particular dimethyl disulphide, with a reducing organic compound which is a hydrogen donor, as will be defined below, according to the following reaction, illustrated with dimethyl disulfide yielding methyl mercaptan, using glucose as reducing organic compound (hydrogen donor):
    It has now been found that this reaction is easily catalyzed by the enzymatic system using a thiol-containing amino acid or a peptide with a thiol group, for example glutathione, in the form of a complex (amino acid or peptide). corresponding reductase enzyme, regenerated by the organic hydrogen donor compound, as described in Figure 1 attached.
    Thus, according to the illustration of Figure 1, the peptide (glutathione represented example) reduces the disulfide (DMDS shown) to mercaptan (methylmercaptan shown) by converting disulfide bond peptide (glutathione disulfide shown). The reductase enzyme ("glutathione reductase" represented, EC 1.8.17 or EC 1.6.4.2) regenerates the peptide (glutathione) and this same enzyme is regenerated by a redox enzymatic complex well known to those skilled in the art, by for example the NADPH / NADP + complex (Nicotine adenine dinucleotide phosphate (reduced form and oxidized form)). In turn, NADP + is regenerated into NADPFI via the enzyme dehydrogenase corresponding to the reducing organic compound used (here the "glucose dehydrogenase" EC 1.1.1.47) by means of said reducing organic compound (represented by glucose) which provides hydrogen (hydrogen donor) by transforming into its oxidized form (here gluconolactone).
    According to a particularly suitable embodiment, the glutathione / glutathione disulfide system associated with the enzyme glutathione reductase allows according to the present invention to reduce the DMDS to methyl mercaptan.
    Glutathione is a tripeptide widely used in biology. This species in reduced form (glutathione) or oxidized (glutathione disulfide) forms a significant pair of oxidation-reduction in the cells. Thus glutathione is vital for removing heavy metals from organisms. Thus, for example, the application WO05107723 describes a formulation in which glutathione is used to form a chelating preparation, US Pat. No. 4,657,856 teaches that glutathione also makes it possible to destroy peroxides such as ΙΉ2Ο2 in H2O via glutathione.
    peroxidase. Finally, glutathione also makes it possible to reduce the disulfide bridges present in proteins (Rona Chandrawati, "Triggered Cargo Release by Encapsulated Enzymatic Catalysis in Capsosomes", Nano Lett., (2011), 11, 4958-4963).
    According to the process of the invention, a catalytic amount of amino acid carrying a thiol group or a peptide with a thiol group is used for the production of mercaptans from disulfides.
    Among the amino acids bearing thiol group usable in the process of the present invention, there may be mentioned, by way of non-limiting examples, cysteine and homocysteine. The oxidoreduction enzyme systems used which can regenerate the catalytic cycle in the same way are, in these cases, the cysteine / cystine reductase system EC 1.8.1.6, and homocysteine / homocysteine reductase.
    Among the peptides bearing thiol group usable in the process of the present invention, there may be mentioned, by way of non-limiting examples, glutathione and thioredoxin. The glutathione / glutathione reductase system described above can be replaced by the thioredoxin (CAS No. 52500-60-4) / thio-redoxin reductase (EC 1.8.1.9 or EC 1.6.4.5) system.
    Glutathione and the glutathione / glutathione reductase system are particularly preferred for the present invention, because of the ease of supply and the costs of these compounds.
    Among the reducing organic compounds which can be used in the context of the present invention, the hydrogen-donor compounds are very particularly preferred, and among these, the most suitable compounds are the organic reducing compounds which give rise to hydrogen bearing hydroxyl-functional groups, such as alcohols, polyols, sugars and the like.
    The enzyme used is an enzyme capable of dehydrogenating the hydrogen-bearing compound, for example an alcohol dehydrogenase. Glucose is a particularly suitable sugar for use in the process of the present invention with glucose dehydrogenase to give gluconolactone.
    In the process according to the invention only disulphide (s) and glucose are used in stoichiometric amount, all the other components (amino acid or peptide, NADPH and 2 enzymes) are used in catalytic amount.
    The advantages provided by the method of the invention are numerous. These advantages include the possibility of working in aqueous or hydro-organic solution under very mild conditions of temperature and pressure and under pH conditions close to neutrality. All these conditions are typical of a so-called "green" or "sustainable" process.
    Another advantage when the process employs dimethyl disulfide is that the methyl mercaptan product, which is in the gaseous state under the reaction conditions, leaves the reaction medium as it is formed. Methyl mercaptan can therefore be used directly at the outlet of the reactor in an application further downstream. It can also be easily liquefied by cryogenics for example if it is desired to isolate it. It may optionally accelerate its departure from the reaction medium by bubbling in a slight flow of nitrogen.
    Dimethyl disulphide (DMDS) can be produced at another site from methyl mercaptan and an oxidant such as oxygen, sulfur or hydrogen peroxide, for example, or from dimethyl sulfate. and sodium disulfide. The DMDS can also come from a source of "DiSulfide Oils" (DSO), as indicated above, and then purified for example by reactive distillation, as described in application WO2014033399. Note that DSO can also be used as is, without the need for purification between the different disulfides component. A mixture of mercaptans is then obtained by applying the process of the invention.
    When DMDS is used as a disulfide, the process according to the invention can then be considered as a method to avoid the transport of methyl mercaptan from its production site by existing industrial channels, to its site of use if they are different. Indeed, methyl mercaptan is a room temperature gas, toxic and highly malodorous which greatly complicates its transport already highly regulated unlike DMDS. The method described in the present invention can therefore be used to produce methyl mercaptan directly at the site of use of the latter.
    The DMDS being consumed in the reaction and the methyl mercaptan leaving the reaction medium as it is formed, only the dehydrogenation product of the reducing organic compound, for example gluconolactone, accumulates in the reaction medium in the reaction medium. the hypothesis of a continuous supply of glucose and DMDS. When the gluconolactone concentration exceeds saturation under the reaction conditions, the latter will precipitate and can then be isolated from the reaction medium by any means known to those skilled in the art.
    Gluconolactone may have several uses. It is for example used as a food additive known under the symbol E575. Gluconolactone hydrolyzes in aqueous acidic media to form gluconic acid also used as a food additive (E574). Gluconolactone is also used for the production of tofu (see CN103053703) for the food industry.
    Gluconolactone may especially and advantageously, in the sense that it represents the "waste" of the process according to the present invention, replace the glucose in a possible fermentation reaction to produce either bioethanol or any other molecule derived from fermentation of sugar or starch.
    Some bacteria can indeed use in fermentation gluconolactone as carbon source, as described by JP van Dijken, "Novel pathway for alcoholic fermentation of gluconolactone in the yeast Saccharomyces bulderi", J. Bacteriol., (2002), Vol. . 184 (3), 672-678.
    Still other sugars may be used in the process of the invention, and for example it is possible to replace the glucose / gluconolactone / glucose-dehydrogenase system by the following system: glucose-6-phosphate / 6-phosphoglucono -5-lactone / Glucose-6-phosphate dehydrogenase (EC 1.1.1.49).
    It is also possible in the process of the invention to use an alcohol instead of sugar, and thus use instead of the glucose / glucono-lactone / glucose dehydrogenase system, the following general system: alcohol / ketone or aldehyde / alcohol dehydrogenase (EC 1.1.1) and more particularly the isopropanol / acetone / isopropanol dehydrogenase system (EC 1.1.1.80).
    Indeed, this system makes it possible to obtain, when DMDS is used as disulfide, a mixture consisting of methyl mercaptan (MeSH) and acetone which leaves the reaction medium (thus no accumulation of any product). MeSH and acetone can be easily separated by simple distillation if desired. In the case of other disulfides, depending on the boiling point of the mercaptan formed and its solubility in the reaction medium, the acetone can easily be removed from the medium and the mercaptan can optionally decant from the reaction medium to be easily separated.
    In general, the temperature of the reaction is in a range from 10 ° C to 50 ° C, preferably between 15 ° C and 45 ° C, more preferably between 20 ° C and 40 ° C.
    The pH of the reaction may be between 6 and 8, preferably between 6.5 and 7.5. The pH of the reaction medium can be adjusted by means of a buffer. Most preferably, the pH of the phosphate buffer will be chosen at 7.3.
    The pressure used for the reaction can range from a reduced pressure relative to the atmospheric pressure to several bars (several hundred kPa), depending on the reagents used and the equipment used. In the case where the DMDS is used as a disulphide, a reduced pressure can indeed allow a faster degassing of methylmercaptan formed but has the disadvantage of increasing the saturation vapor pressures of water and DMDS, polluting a little more the methylmercaptan formed. Preferably, a pressure ranging from atmospheric pressure to 20 bar (2 MPa) will be used and even more preferably one will work under a pressure ranging from atmospheric pressure to 3 bar (300 kPa).
    The process according to the invention may be carried out batchwise or continuously in a glass or metal reactor depending on the operating conditions used and the reagents used.
    The ideal organic reductant / disulfide compound molar ratio is stoichiometry (molar ratio = 1) but may vary from 0.01 to 100 if the skilled person finds therein any interest such as continuous addition of the disulphide. while the reducing compound is introduced from the start into the reactor. Preferably, this molar ratio is chosen between 0.5 and 5 overall over the entire reaction.
    The elements present in catalytic amount in the mixture prepared in step a) above (amino acid bearing a thiol group or a thiol peptide, enzyme reductase, NADPH) are readily available in the or can be prepared according to techniques well known to those skilled in the art. These various elements can be in solid or liquid form and can very advantageously be dissolved in water to be used in the process of the invention. The enzymes used can also be grafted onto a support (in the case of supported enzymes).
    The aqueous solution of enzymatic complex comprising the amino acid or the peptide may also be reconstituted by methods known to those skilled in the art, for example by permeabilization of cells that contain these elements. This aqueous solution, a composition of which is given in the following Example 1, can be used in contents of between 0.01% and 20% relative to the total weight of the reaction medium. Preferably, a content of between 0.5% and 10% will be used.
    According to another aspect, the present invention relates to the use of an aqueous solution of enzymatic complex comprising an amino acid bearing a thiol function as defined above or a peptide carrying a thiol function such that defined above, for the synthesis of a mercaptan from a disulfide.
    The mixture prepared in step a) and comprising: • a disulphide of formula RSS-R ', • a catalytic amount of amino acid carrying a thiol group or a peptide with a thiol group, • a catalytic amount of enzyme reductase corresponding to said amino acid carrying a thiol group or said peptide with thiol group, and • a catalytic amount of NADPH, is new and as such is part of the present invention.
    The invention will be better understood with the following nonlimiting examples with respect to the scope of the invention. EXAMPLE 1 [0060] In a reactor containing 150 ml of 0.1 mol / l phosphate buffer at pH 7.30, 10 ml of glutathione enzymatic complex and 19.2 g (0.1 mol) of glucose are introduced. . The enzyme complex solution contains: 185 mg (0.6 mmol) glutathione, 200 U glutathione reductase, 50 mg (0.06 mmol) NADPH and 200 U glucose dehydrogenase. The reaction medium is brought to 25 ° C. with mechanical stirring. A first sample is taken t = 0. Subsequently, the dimethyl disulfide (9.4 g, 0.1 mol) is placed in a burette and added dropwise into the reactor, the reaction begins. A stream of nitrogen is placed in the reactor. A gas chromatographic analysis of the gases leaving the reactor essentially shows the presence of nitrogen and methyl mercaptan (some traces of water). These exit gases are trapped in 20% sodium hydroxide (sodium hydroxide) in water. The DMDS is introduced in 6 hours and the reaction is followed by potentiometric assay in argentimetry of the sodium salt of methyl mercaptan in the trap at the reactor outlet. The final analysis shows that DMDS was converted quantitatively to methyl mercaptan. In addition, a final analysis by gas chromatography of the reaction medium confirms the absence of DMDS, and by UPLC / mass there are traces of glucose and the almost exclusive presence of gluconolactone. EXAMPLE 2 [0061] To the reaction medium of Example 1, 19.2 g (0.1 mol) of glucose are reintroduced at once and 9.4 g (0.1 mol) of DMDS are added dropwise. in 6 hours. The reaction is monitored in the same manner as in Example 1 after changing the soda solution to 20% at the outlet of the reactor. The analyzes at the end of the reaction confirm the complete disappearance of DMDS completely converted to methyl mercaptan found as sodium salt in the sodium hydroxide solution. Only gluconolactone is analyzed and found in the reaction medium at the end of the reaction. This example shows the robustness of the catalytic system by its reproducibility.
    权利要求:
    Claims (11)
    [1" id="c-fr-0001]
    A process for preparing a mercaptan of formula R-SH, comprising at least the steps of: a) preparing a mixture comprising: a disulphide of formula RSS-R '; a catalytic amount of carrier amino acid a thiol group or a peptide with a thiol group, • a catalytic amount of enzyme reductase corresponding to said amino acid carrying a thiol group or said peptide with a thiol group, • a catalytic amount of NADPH, b) addition of a thiol group, a reducing organic compound in stoichiometric amount relative to the disulfide and DMDS) with a catalytic amount of the corresponding enzyme dehydrogenase, c) conducting the enzymatic reaction, d) recovering the mercaptan of formula R-SH and the mercaptan of formula R -SH, e) optionally separating and optionally purifying the mercaptan of the formula R-SH and / or the mercaptan of the formula R'-SH.
    [2" id="c-fr-0002]
    2. Process according to claim 1, in which R and R ', which may be identical or different, represent, independently of one another, a linear, branched or cyclic hydrocarbon-based radical containing from 1 to 20 carbon atoms, said chain being saturated or carrying one or more unsaturations in the form of double (s) or triple (s) bond (s), R and R 'may also form together with the sulfur atoms which carry them a cyclic molecule comprising 4 at 22 atoms, preferably from 5 to 10 atoms.
    [3" id="c-fr-0003]
    3. A process according to claim 1 or claim 2, in which the radicals R and R ', which may be identical or different, are chosen independently of one another from among the alkyl, cycloalkyl, aryl, alkylaryl and arylalkyl radicals comprising from 1 to 20 carbon atoms, preferably from 1 to 12 carbon atoms, more preferably from 1 to 6 carbon atoms, linear or branched, saturated or unsaturated, and optionally functionalized with one or more functions chosen from alcohol functional groups, aldehyde, ketone, acid, amide, nitrile, ester or the functions carrying sulfur, phosphorus, silicon or halogen.
    [4" id="c-fr-0004]
    4. Process according to any one of the preceding claims, in which the disulphide of formula R-S-S-R 'is dimethyl disulphide.
    [5" id="c-fr-0005]
    5. Process according to any one of the preceding claims, in which the thiol-bearing amino acid or the peptide carrying thiol group is chosen from cysteine, homocysteine, glutathione and thioredoxin.
    [6" id="c-fr-0006]
    6. A process according to any one of the preceding claims, wherein the reducing organic compound is a reducing organic hydrogen-donor compound carrying hydroxyl function, selected from alcohols, polyols, sugars and others.
    [7" id="c-fr-0007]
    The process of any of the preceding claims, wherein the reducing organic compound is selected from glucose, glucose-6-phosphate and isopropanol.
    [8" id="c-fr-0008]
    8. Process according to any one of the preceding claims, in which the pH of the reaction is between 6 and 8, preferably between 6.5 and 7.5.
    [9" id="c-fr-0009]
    9. Process according to any one of the preceding claims, in which the molar ratio of organic compound reducing agent / disulphide is between 0.01 and 100, preferably between 0.5 and 5 globally over the entire reaction, so quite preferred said molar ratio is 1.
    [10" id="c-fr-0010]
    10. Use of an aqueous solution of enzymatic complex comprising a thiol-functional amino acid or a peptide carrying a thiol function for the synthesis of a mercaptan from a disulfide.
    [11" id="c-fr-0011]
    11. Mixture comprising: • a disulphide of formula RSS-R ', • a catalytic amount of amino acid carrying a thiol group or a peptide with a thiol group, • a catalytic amount of enzyme reductase corresponding to said amino acid carrier of a thiol group or said peptide with a thiol group, and • a catalytic amount of NADPH.
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    引用文献:
    公开号 | 申请日 | 公开日 | 申请人 | 专利标题
    US4059636A|1976-05-04|1977-11-22|Phillips Petroleum Company|Mercaptans by catalytic cleavage of organic sulfides|
    US20050260250A1|2004-05-24|2005-11-24|Ott David M|Medicinal products incorporating bound organosulfur groups|
    JPH0214036B2|1985-04-24|1990-04-05|Ebara Sogo Kenkyusho Kk|
    FR2711366B1|1993-10-20|1995-12-15|Elf Aquitaine|Synthesis of methylmercaptan from dimethyldisulfide.|
    EP0770686A1|1995-10-25|1997-05-02|Societe Des Produits Nestle S.A.|Process for the production of thiols|
    DE102005043151A1|2005-09-10|2007-03-22|Degussa Ag|Process for the preparation of methyl mercaptan|
    BR112013016810B1|2010-12-29|2020-12-29|Cj Cheiljedang Corporation|methods for the production of l-methionine and related products|FR3041636B1|2015-09-30|2018-11-16|Arkema France|PROCESS FOR THE PRODUCTION OF MERCAPTANS BY ENZYMATIC HYDROGENOLYSIS OF DISULFIDES USING HYDROGEN|
    CN113058621B|2019-12-12|2022-02-15|中国科学院大连化学物理研究所|Reduced coenzyme and analogue regeneration catalyst thereof, preparation method and application|
    WO2021197632A1|2020-04-03|2021-10-07|Wacker Chemie Ag|Biocatalyst as a core component of an enzyme-catalyzed redox system for the biocatalytic reduction of cystine|
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    2021-08-12| PLFP| Fee payment|Year of fee payment: 7 |
    优先权:
    申请号 | 申请日 | 专利标题
    FR1559257A|FR3041635B1|2015-09-30|2015-09-30|PROCESS FOR THE PRODUCTION OF MERCAPTANS BY ENZYMATIC HYDROGENOLYSIS OF DISULFIDE|
    FR1559257|2015-09-30|FR1559257A| FR3041635B1|2015-09-30|2015-09-30|PROCESS FOR THE PRODUCTION OF MERCAPTANS BY ENZYMATIC HYDROGENOLYSIS OF DISULFIDE|
    JP2018516718A| JP7036714B2|2015-09-30|2016-09-29|Method for producing mercaptan by hydrolysis of disulfide enzyme|
    CN201680056787.0A| CN108137493B|2015-09-30|2016-09-29|Method for producing thiols by enzymatic hydrogenolysis of disulfides|
    RU2018115348A| RU2709486C1|2015-09-30|2016-09-29|Method of producing mercaptans by enzymatic hydrogenolysis of disulphides|
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    EP16785250.8A| EP3356325B1|2015-09-30|2016-09-29|Method for producing mercaptans by disulfide enzyme hydrogenolysis|
    PCT/FR2016/052479| WO2017055752A1|2015-09-30|2016-09-29|Method for producing mercaptans by disulfide enzyme hydrogenolysis|
    BR112018006044-5A| BR112018006044B1|2015-09-30|2016-09-29|METHOD OF PREPARATION OF A MERCAPTAN OF FORMULA R-SH|
    US15/764,480| US20190055586A1|2015-09-30|2016-09-29|Method for producing mercaptans by disulfide enzyme hydrogenolysis|
    SG11201802687VA| SG11201802687VA|2015-09-30|2016-09-29|Method for producing mercaptans by disulfide enzyme hydrogenolysis|
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