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    • 专利摘要:
    METHOD FOR PROCESSING PEROXYGEN SOLUTIONS. The present disclosure relates to a multi-step method for processing peroxygen solutions for reuse or disposal. The method uses an enzyme and a reducing agent.
    公开号:BR112012021933B1
    申请号:R112012021933-2
    申请日:2011-03-02
    公开日:2021-05-18
    发明作者:John D. Hilgren；Jelte Lanting；Roger J.A. Tippett
    申请人:Ecolab Usa Inc；
    IPC主号:
    专利说明:

    Field of Invention
    [001] This description refers to a multi-step method for processing peroxygen solutions for reuse or disposal. Background of the Invention
    [002] Peroxygen compounds are used as decontamination agents, bleaching agents or oxidizing agents in various applications including in food and beverage processing such as food surface decontamination treatments, food packaging decontamination treatments , on-site cleaning treatments, food processing water decontamination treatments, food contact surface decontamination treatment and the like. Used peroxygen solutions must be reused or discarded. If the peroxygen solution is discarded, the residual peroxygen concentration may need to be lowered for the peroxygen solution to be compatible with biological waste treatment processes. If the residual concentration of peroxygen is too high, the peroxygen compounds can inhibit or kill beneficial microorganisms used in the wastewater treatment process. It is against this scenario that this disclosure is made. Summary
    [003] It has been surprisingly found that the introduction of selected agents reduces the levels of peroxygen compounds in peroxygen solutions without causing a significant increase in the level of total dissolved solids, allowing the treated solution to be reused or safely discharged to a process of biological wastewater treatment.
    [004] A first aspect of the present disclosure is a method of treating a peroxygen solution that contains a peracid and hydrogen peroxide. In the method, the peroxygen solution is collected, an enzyme is added, and then a reducing agent is added. The enzyme and reducing agent degrade the peroxygen compounds in solution at a rate where at least 0.1 part of the peroxygen compounds is degraded by the enzyme for every 1 part of the peroxygen compounds that is degraded by the reducing agent. It is generally understood that “peroxygen compounds” refers to hydrogen peroxide and peracids.
    [005] A second aspect of the disclosure is a method of treating a peroxygen solution that contains a peracid, hydrogen peroxide and a carboxylic acid. In the method, the peroxygen solution is collected, an enzyme is added, and then a reducing agent is added. The enzyme and reducing agent degrade the peroxygen compounds in solution at a rate where at least 0.1 part of the peroxygen compounds is degraded by the enzyme for every 1 part of the peroxygen compounds that is degraded by the reducing agent.
    [006] A third aspect of the disclosure is a method of treating a peroxygen solution that contains hydrogen peroxide. In the method, the peroxygen solution is collected, an enzyme is added, and then a reducing agent is added. The enzyme and reducing agent degrade the peroxygen compounds in solution at a rate where at least 0.1 part of the peroxygen compounds is degraded by the enzyme for every 1 part of the peroxygen compounds that is degraded by the reducing agent.
    [007] A fourth aspect of the disclosure is a method of treating a peroxygen solution. In the method, an enzyme is added to a peroxygen solution, before or during a decontamination, bleaching or oxidation process. After the decontamination, bleaching or oxidation process is completed, a reducing agent is added to the peroxygen solution. The enzyme and reducing agent degrade the peroxygen compounds in solution at a rate where at least 0.1 part of the peroxygen compounds is degraded by the enzyme for every 1 part of the peroxygen compounds that is degraded by the reducing agent.
    [008]Other features and advantages of the disclosure will become evident upon reading the description and examples that follow. Brief Description of Drawings
    [009] Figure 1 is a graph showing the degradation of peroxygen by the enzyme after 10 minutes at 25 °C.
    [0010] Figure 2 is a graph showing the degradation of the peroxygen compound by the reducing agent after thirty minutes at 25 °C.
    [0011] Figure 3 is a graph showing the degradation of hydrogen peroxide by the enzyme as a function of time at 25 °C.
    [0012] Figure 4 is a graph showing the degradation of hydrogen peroxide by the enzyme as a function of temperature.
    [0013] Detailed Description
    [0014] The present disclosure relates to methods of treating peroxygen solutions for reuse or disposal.
    [0015] Peroxygen solutions are applied to various surfaces to decontaminate the surface, to whiten that surface or to function as an oxidizing agent on that surface. Decontamination can refer to a process that reduces physical, chemical or biological contamination. Examples of surfaces include environmental surfaces such as walls, floors and drains, processing equipment, food packaging, food contact surfaces, ready-to-cook and ready-to-eat food surfaces such as whole and cut meats, carcasses and fruit and vegetables, textile materials such as clothing, rugs, upholstery, surgical drapes and drapes, kitchen surfaces such as those found in warehouses, delicatessens and restaurants, and health surfaces such as medical instruments, devices and endoscopes, and patient contact surfaces.
    [0016] In some methods disclosed herein, a peroxygen solution is collected from a decontamination, bleaching or oxidation process such as those described above. This peroxygen solution may be referred to in this disclosure as the "initial peroxygen solution" because it is the peroxygen solution that goes into the disclosed method. It is understood, however, that this “initial peroxygen solution” may already have been used to treat a surface or substance and may be considered at least partially “spent” in terms of decontamination effectiveness or could be a new or fresh solution. to be used for the treatment of a surface or substance. The peroxygen solution can be collected as part of a batch process. The peroxygen solution can also be continuously collected and processed as part of a continuous flow process. In the method, selected agents are added to the initial peroxygen solution in a multi-step process, in an amount sufficient to degrade the peroxygen compounds to an acceptable level, where the solution can be reused or disposed of. In the first step, an enzyme is used to degrade the peroxygen compounds and, in a second step, a reducing agent is used to further degrade the peroxygen compounds. In cases where the peroxygen compounds include both hydrogen peroxide and a peracid, the hydrogen peroxide is degraded by the enzyme in the first step, and the peracid is degraded by a reducing agent in the second step.
    [0017] In some methods disclosed herein, the enzyme can be added to the peroxygen solution in the middle of a decontamination, bleaching or oxidation process. For example, the enzyme can be added to the peroxygen solution, since the peroxygen solution is being used as part of an on-site clean-up operation, or food packaging decontamination operation for aseptic or living food. extended shelf. Once the decontamination, bleaching or oxidation process is complete, the reducing agent can be added to the peroxygen solution.
    [0018] In some methods disclosed herein, the enzyme may be added to the peroxygen solution before the start of the decontamination, bleaching or oxidation process, or it may be part of the peroxygen solution before the start of the decontamination, bleaching or oxidation process.
    [0019] The peroxygen solution may include hydrogen peroxide. The peroxygen solution can include hydrogen peroxide and a peracid. And the peroxygen solution can include hydrogen peroxide, carboxylic acid and the corresponding peracid. When the peroxygen solution includes a peracid, the peracid can be a simple peracid or a solution of mixed peracids. The peroxygen solution coming out of a decontamination, bleaching or oxidation process may include residues or fragments from the process, or from other processes, including water, sugars, starches, fats, oils, proteins, dirt, salts, blood, minerals and detergents. The peroxygen solution can also be combined with other waste streams and then treated.
    [0020] If the peroxygen solution is eliminated using a biological wastewater treatment process, and the concentration of hydrogen peroxide or peracids is very high, the peroxygen solution may inhibit or potentially kill beneficial microorganisms in the water treatment process biological residuals. Therefore, in the present method, the level of residual peroxygen compounds is reduced so that the biological wastewater treatment process is not adversely affected. In this way, the peroxygen solution is collected after being used in a process as a decontamination agent, bleaching agent or oxidizing agent (initial peroxygen solution) or the peroxygen solution can still be used as part of a decontamination process , bleaching or oxidation. An enzyme is added to the peroxygen solution in an amount sufficient to eliminate 0.1 or more parts (by weight) of the total peroxygen compounds for every 1 part (by weight) eliminated with the reducing agent. After the enzyme is added, a reducing agent is added. Once the enzyme and reducing agent are added to the initial peroxygen solution, the resulting product can be referred to as the “treated peroxygen solution” to differentiate the treated solution from the initial solution that is collected from the decontamination process. , bleaching or oxidation.
    [0021] One factor to achieve the desired decrease in the concentration of peroxygen compounds is the contact time between the enzyme or reducing agent and the peroxygen solution. Increased contact time between the peroxygen solution and the enzyme, the reducing agent, or both can lead to a greater decrease in the peroxygen concentration. The use of constant-flow reactors or full-mix reactors in series are two methods of increasing contact time.
    [0022] In a specific embodiment, a peroxygen solution containing hydrogen peroxide, carboxylic acid and the corresponding peracid can be used as part of an aseptic or extended shelf-life food packaging decontamination operation. The enzyme can be added before or during the decontamination process, where food packages are being decontaminated. Once the packages are decontaminated, the peroxygen solution can be collected and then the reducing agent can be added to the peroxygen solution. Once the peroxygen solution has been treated with the enzyme and reducing agent, it can be discarded or further treated.
    [0023] In the wastewater treatment process, the peroxygen solution can go through several other processes. For example, the peroxygen solution may be subject to physical and/or chemical separation processes, such as sweeping, gravity decantation, sedimentation, equalization, flocculation, mechanical separation, dissolved air flotation (DAF), modification of the pH, filtration, clarification, disinfection and biological treatment processes to remove organic compounds, and oxidize inorganic compounds (eg sulfides and ammonia) and total nitrogen (through nitrification and denitrification). Biological treatments can use aerobic, facultative or anaerobic microorganisms. Biologically treated water can be further clarified using a separation process prior to disinfection and discharge of the remaining liquid into a receiving stream such as a lake or river. An example of a biological process includes an anaerobic waste treatment digester such as that described in U.S. Patent No. 5,733,454. The peroxygen solution can also be combined with other waste streams. And the peroxygen solution (initial or treated) can also be sent to a publicly owned treatment plant (POTW), municipal sewage treatment facility, industrial waste treatment facility, or a municipal or industrial energy recovery facility. Enzyme
    [0024] The enzyme used in the method reduces the concentration of hydrogen peroxide. Exemplary hydrogen peroxide reducing enzymes include catalase, peroxidase or a combination of catalase and peroxidase.
    [0025] Catalase Enzyme
    [0026] Catalase enzymes catalyze the decomposition of hydrogen peroxide into water and oxygen. Sources of catalase enzymes include animal sources such as bovine catalase isolated from beef livers, fungal catalases isolated from fungi including Penicillium chrysogenum, Penicillium notatum and Aspergillus niger, from plant sources, bacterial sources such as Staphylococcus aureus, and genetic variations and modifications of the same. Fungal catalases are especially suitable because of their ability to break down hydrogen peroxide into lower concentrations of catalase enzyme compared to non-fungal catalase enzymes. In addition, fungal catalase enzymes are more stable at pH and room temperature than found in peroxygen solutions.
    [0027] The catalase molecule is susceptible to denaturation by heat, oxidation, and extreme pH levels. In general, preferred starting peroxygen solutions contain between 1 and 50000 ppm (by weight) of total peroxygen compounds, with a pH between 1 and 10, and a temperature between 1 and 70 °C (34 and 158 °F), or between 1 and 10,000 ppm of total peroxygen compounds, with a pH between 2 and 9, and a temperature between 10 and 60 °C (50 and 140 °F), or between 1 and 5000 ppm of total peroxygen compounds, with a pH between 3 and 8, and a temperature between 20 and 50 °C (68 and 122 °F).
    [0028]Catalase can be introduced floating free in the peroxygen solution. Alternatively, the catalase can be immobilized on a surface that is in fluid communication with the peroxygen solution in a way that allows the catalase to interact with and break down the hydrogen peroxide. Immobilized catalase may be more stable than unbound soluble enzyme. An immobilized catalase also has the advantage of being able to be easily removed from the solution. An immobilized catalase can include a soluble catalase that is bound to a substrate. Examples of substrates may include polyurethane foams, polyacrylamide gels, polyethylene maleic anhydride gels, polystyrene maleic anhydride gels, cellulose, nitrocellulose, silastic resins, porous glass, macroporous glass membranes, glass beads, activated clay, zeolites, alumina, silica, silicate and other inorganic and organic substrates. The enzyme can be attached to the substrate in a number of ways, including carrier covalent bonding, cross-linking, physical adsorption, ionic bonding, and trapping.
    Commercially available catalases are available in lyophilized and atomized forms. Commercially available catalase includes both the active enzyme and additional ingredients to improve enzyme stability or performance. Some examples of commercially available catalase enzymes include Genencor CA-100 and CA-400, as well as ASC Super G and ASC Super 200, from Mitsubishi Gas Chemical (MGC). The method preferably includes at least one fungal catalase. peroxidase enzyme
    [0030] The peroxidase enzymes also catalyze the decomposition of hydrogen peroxide into water and oxygen. Peroxidase sources include animals, plants and microorganisms.
    [0031] The peroxidase molecule is susceptible to denaturation by heat, oxidation and extreme pH levels. In general, preferred starting peroxygen solutions contain between 1 and 50,000 ppm (by weight) of total peroxygen compounds, with a pH between 1 and 10, and a temperature between 1 and 70°C (34 and 158°F); or between 1 and 10,000 ppm of total peroxygen compounds, with a pH between 2 and 9, and a temperature between 10 and 60 °C (50 and 140 °F), or between 1 and 5,000 ppm of total peroxygen compounds, with a pH between 3 and 8, and a temperature between 20 and 50 °C (68 and 122 °F).
    [0032] The peroxidase can be introduced floating free in the peroxygen solution. Alternatively, the peroxidase can be immobilized on a surface, which is in fluid communication with the peroxygen solution in a form that allows the peroxidase to interact and decompose the hydrogen peroxide. An immobilized peroxidase has the advantage of being able to be easily removed from solution. An immobilized peroxidase can include a soluble peroxidase that is bound to a substrate. Examples of substrates may include polyurethane foams, polyacrylamide gels, polyethylene maleic anhydride gels, polystyrenemaleic anhydride gels, cellulose, nitrocellulose, silastic resins, porous glass, macroporous glass membranes, glass beads, activated clay, zeolites, alumina, silica, silicates and other inorganic and organic substrates. The enzyme can be attached to the substrate in a variety of ways, including carrier covalent bonding, cross-linking, physical adsorption, ionic bonding, and trapping.
    [0033] Commercially available peroxidases are available in liquid and powder forms. Commercially available peroxidase includes the active enzyme as well as additional ingredients to improve enzyme stability. Some exemplary commercially available peroxidase enzymes include horseradish peroxidases available from Sigma-Aldrich, Genencor International and Novozymes. The Reducing Agent
    [0034] The reducing agent eliminates part of the hydrogen peroxide not eliminated by the enzyme and also eliminates a certain amount of peracid, if present. Exemplary reducing agents include the following: bisulfite salts, (eg, sodium, potassium, and ammonium bisulfite salts, sodium metabisulfite), thiosulfate salts (eg, sodium, potassium, and ammonium thiosulfate), sulfite salts ( eg sodium, potassium and ammonium sulfite), sulfur dioxide, porous carbonaceous materials (eg carbon, charcoal, activated carbon), ascorbic acid, erythorbic acid, metal catalysts (eg manganese, silver) and its mixtures. The reducing agent can also be a physical process, such as ultraviolet (UV) light.
    [0035] The enzyme and reducing agent must be added in amounts that cause significant reductions in the concentration of the peroxygen compounds with each addition. The enzyme will always degrade hydrogen peroxide. The reducing agent will degrade hydrogen peroxide or peracid. The amount of relative peroxygen that is degraded by the enzyme versus the reducing agent will depend on the concentration of hydrogen peroxide versus peracid. For example, if the peroxygen composition contains high levels of peracid compared to hydrogen peroxide, the enzyme will degrade a smaller amount of hydrogen peroxide compared to the reducing agent that degrades the peracid. In contrast, if there is more hydrogen peroxide than peracid, the enzyme will degrade a greater amount of hydrogen peroxide than the reducing agent will degrade the peracid. Since the chemical reducing agent contributes to the TDS levels in the treated peroxygen solution to a much greater degree than the enzyme, the methods described are especially suitable for peroxygen solutions with significant levels of hydrogen peroxide relative to the level of peracid. Therefore, the enzyme and reducing agent are preferably added to the peroxygen solution in amounts where the enzyme degrades at least 0.1 part of peroxygen for every 1 part of peroxygen that is degraded by the reducing agent. Other ratios include at least 0.5, at least 1 and at least 5 parts of peroxygen that are degraded by the enzyme for every 1 part of peroxygen that is degraded by the reducing agent.
    [0036] The amount of enzyme added will vary according to which enzyme is selected and the concentration of hydrogen peroxide in the initial peroxygen solution. A person skilled in the art will be able to calculate the amount of enzyme needed to achieve the desired ratios described above, however representative and non-limiting enzyme concentrations include from about 0.01 to about 100 mg/L, from about 0. 01 to about 10 mg/L, and from about 0.05 to about 5 mg/L (active enzyme). Likewise, the amount of reducing agent added will vary depending on which reducing agent is selected and the concentration of peroxygen species in the initial peroxygen solution. A person skilled in the art will be able to calculate the amount of reducing agent needed to achieve the desired ratios described above, but representative and non-limiting concentrations of the reducing agent, expressed as sodium metabisulfite, include from about 5 to about 450 mg/L, from about 10 to about 90,000 mg/L, and from about 10 to about 9,000 mg/L.
    [0037] After addition of enzyme and reducing agent, the total dissolved solids of the peroxygen solution preferably do not increase by more than 100 mg/L, 1,000 mg/L or 10,000 mg/L. If used in large quantities, chemical reducing agents such as sodium bisulfite and sodium metabisulfite increase the cost and increase the level of total dissolved solids (TDS). The concentration of total dissolved solids in wastewater streams can be regulated or restricted. The TDS level in wastewater is primarily due to the presence of inorganic salt ions (eg calcium, magnesium, potassium, sodium, bicarbonates, sulfates and chlorides). Wastewater treatment facilities are not normally equipped to remove these salt ions. The concentration of TDS that can be discharged from an industrial facility or POTW can be restricted due to the adverse impact that TDS can have on surface waters and aquifers.
    [0038]Two advantages of the methods disclosed herein are the lower levels of reducing agents and the lower levels of TDS in the treated peroxygen solution. Consider the following hypothetical example:


    [0039] For example, for every 1 part (by weight) of hydrogen peroxide in a peroxygen solution, about 3 parts of sodium bisulfite are needed to degrade it. Thus, 1 liter of a solution containing 3000 mg of hydrogen peroxide would need approximately 9000 mg of sodium bisulfite for neutralization, resulting in an increase in the TDS level of approximately 9000 mg/L. In contrast, under the present disclosure, only 3 mg of catalase is added to a 3000 mg/L hydrogen peroxide solution for hydrogen peroxide neutralization - this has virtually no impact on the TDS level.
    [0040] In the disclosed methods, the levels of peroxygen compounds in the treated peroxygen solution are from about 0.1 to about 1000 ppm, from about 0.1 ppm to about 100 ppm, from about 0.1 ppm to about 10 ppm and from about 0.1 ppm to about 1 ppm. Alternatively, the treated peroxygen solution is substantially free of peroxygen compounds. Finally, the treated peroxygen solution can be free of peroxygen compounds. Peroxygen Solutions
    [0041] The methods described are used in peroxygen solutions that have been or are being used as part of a decontamination, bleaching or oxidation process. The method focuses primarily on the components of the peroxygen solution that are found in the spent peroxygen solution or waste stream. The peroxygen solution can include hydrogen peroxide. The peroxygen solution can include hydrogen peroxide and peracid. Finally, the peroxygen solution can include hydrogen peroxide, peracid and the corresponding carboxylic acid for the peracid. If the peroxygen solution includes hydrogen peroxide and peracid, then in the method, the enzyme is used to degrade hydrogen peroxide in the first step and then the reducing agent is used to degrade peracid, and peroxide of hydrogen, if present, in the second step.
    [0042] The method is preferably used with compositions with significant levels of hydrogen peroxide in relation to the level of peracid. For example, preferred ratios of hydrogen peroxide to peracid include 0.1 part or more (by weight) of hydrogen peroxide per 1 part (by weight) of peracid. Additional hydrogen peroxide:peracid ratios include: 0.5:1, 1:1, 2:1, 3:1, 4:1 and 5:1.
    [0043]Carboxylic acid. A carboxylic acid includes any compound of the general formula R-(COOH)n where R may be hydrogen, alkyl, alkenyl, an alicyclic group, aryl, heteroaryl or a heterocyclic group, and n is 1, 2, or 3. Preferably, R includes hydrogen, alkyl or alkenyl. Alkyl and alkenyl include 1 to 12 carbon atoms and can be substituted or unsubstituted.
    [0044]Examples of suitable carboxylic acids include a variety of monocarboxylic acids, dicarboxylic acids and tricarboxylic acids. Monocarboxylic acids include, for example, formic acid, acetic acid, propanoic acid, butanoic acid, pentanoic acid, hexanoic acid, heptanoic acid, octanoic acid, nonanoic acid, decanoic acid, undecanoic acid, dodecanoic acid, glycolic acid, lactic acid, salicylic acid, acetylsalicylic acid, mandelic acid, etc. Dicarboxylic acids include, for example, adipic acid, fumaric acid, glutaric acid, maleic acid, succinic acid, malic acid, tartaric acid, etc. Tricarboxylic acids include, for example, citric acid, trimellitic acid, isocitric acid, agaic acid, etc. A carboxylic acid suitable for use in a composition of the invention can be selected for its solubility, cost, approval as a food additive, odor, purity, etc. A particularly useful carboxylic acid for a composition of the invention includes a carboxylic acid that is soluble in water, such as formic acid, acetic acid, propionic acid, butanoic acid, lactic acid, glycolic acid, citric acid, mandelic acid, glutaric acid, acid maleic acid, malic acid, adipic acid, succinic acid, tartaric acid, etc. These carboxylic acids can also be useful because the water-soluble carboxylic acids can be food additives such as formic acid, acetic acid, lactic acid, citric acid, tartaric acid, etc.
    Preferred carboxylic acids include acetic acid, octanoic acid or propionic acid, lactic acid, heptanoic acid, nonanoic acid or a combination thereof.
    [0046] Peracid. A peracid is also known in the art as a peroxycarboxylic acid, a peroxyacid and a peroxycarboxylic acid. A peracid includes any compound of the formula R-(COOOH)n, where R may be hydrogen, alkyl, alkenyl, an alicyclic group, aryl, heteroaryl, or a heterocyclic group, and n is 1, 2, or 3. Preferably R includes hydrogen, alkyl or alkenyl.
    [0047] Preferred peracids include any peroxycarboxylic acid that can be prepared from the acid-catalyzed equilibrium reaction between a carboxylic acid and hydrogen peroxide. Preferably, a composition of the invention includes peroxyacetic acid, peroxyoctanoic acid or peroxypropionic acid, peroxylactic acid, peroxyeptanoic acid, peroxynonanoic acid or a combination thereof. Additional Optional Materials
    [0048] Peroxygen solutions can include a number of additional optional materials including stabilizing agents, hydrotropes, surfactants, defoamers, corrosion inhibitors, rheology modifiers, dyes and fragrances. These materials are typically part of peroxygen concentrates and therefore may be present in the initial or treated peroxygen solution. Stabilizing agents
    [0049] The solutions may optionally include stabilizing agents to stabilize and prevent premature oxidation of the concentrated peroxygen material used to prepare a peroxygen solution, or the peroxygen solution itself.
    Chelating or sequestering agents generally useful as stabilizing agents include phosphonic acid and phosphonates, phosphates, aminocarboxylates and their derivatives, pyrophosphates, ethylenediamine and ethylenetriamine derivatives, hydroxy acids and mono, di and tricarboxylates and their corresponding acids .
    [0051] Other chelating agents include nitroloacetates and their derivatives, and mixtures thereof. Examples of aminocarboxylates include aminoacetates and their salts. Suitable aminoacetates include: N-hydroxyethylaminodiacetic acid; hydroxyethylenediaminetetraacetic acid; nitrilotriacetic acid (NTA); ethylenediaminetetraacetic acid (EDTA); N-hydroxyethylethylenediaminetriacetic acid (HEDTA); tetrasodium ethylenediaminetetraacetic acid (EDTA); diethylenetriamine pentaacetic acid (DTPA); and alanine-N,N-diacetic acid; hydroxyethyliminodiacetic acid; and the like; their alkali metal salts; and its mixtures. Suitable aminophosphates include nitrilotrismethylenephosphate and other aminophosphates with alkyl or alkaline groups having less than 8 carbon atoms. Exemplary polycarboxylates include iminodisuccinic acids (IDS), sodium polyacrylates, citric acid, glycolic acid, oxalic acid, their salts, mixtures, and the like. Additional polycarboxylates include citric or citrate type chelating agents, polymeric polycarboxylate and acrylic or polyacrylic acid type chelating agents. Additional chelating agents include polyaspartic acid or cocondensates of aspartic acid with other amino acids, C4-C25 mono or dicarboxylic acids and C4-C25 mono or diamines. Examples of polymeric polycarboxylates include polyacrylic acid, maleic/olefin copolymer, acrylic/maleic copolymer, polymethacrylic acid, acrylic acid-methacrylic acid copolymers, hydrolyzed polyacrylamide, hydrolyzed polymethacrylamide, hydrolyzed polyamide-methacrylamide copolymers, hydrolyzed polyacrylonitrile hydrolyzed polymethacrylonitrile, hydrolyzed acrylonitrile-methacrylonitrile copolymers, and the like. Hydrotropes
    [0052] The solution may optionally include a solubilized or hydrotrope coupler.
    [0053] Such materials can be used to ensure that the concentrated peroxygen material used to prepare a peroxygen solution, or the peroxygen solution itself, remains stable in phase and in a unique highly active aqueous form. Such hydrotropic solubilizers or couplers can be used at concentrations that maintain phase stability but do not result in unwanted compositional interaction.
    Representative classes of hydrotrope solubilizers or coupling agents include an anionic surfactant, such as an alkyl sulfate, an alkyl sulfonate or alkane sulfonate, a linear alkylbenzene or naphthalene sulfonate, a secondary alkane sulfonate, alkyl ether sulfonate or sulfonate, an alkyl phosphate or phosphonate, dialkylsulfosuccinic acid ester, sugar esters (eg, sorbitan esters) and a C8-C10 alkylglycoside.
    [0055] Coupling agents may also include n-octane sulfonate, aromatic sulfonates, such as an alkyl aryl sulfonate (eg, xylene sulfonate or sodium naphthalene sulfonate), and alkylated diphenyl oxide disulfonic acids, such as those sold under the trade name DOWFAX™ , preferably the acid forms of these hydrotropes. Surfactants
    [0056] The composition may optionally include a surfactant or mixture of surfactants. The surfactant can include commercially available anionic, nonionic, cationic, amphoteric and zwitterionic surfactants, and mixtures thereof. In one embodiment, the surfactant includes a nonionic or anionic surfactant. For a discussion of surfactants, see Kirk-Othmer, Encyclopedia of Chemical Technology, Third Edition, volume 8, pages 900-912.
    [0057] Nonionic surfactants can include those that have a polyalkylene oxide polymer as a portion of the surfactant molecule. These surfactants can be protected or unprotected. Such nonionic surfactants include, for example, polyethylene glycol ethers of fatty alcohols protected with chlorine, benzyl, methyl, ethyl, propyl, butyl and other alkyls; polyalkylene oxide free nonionics such as alkylpolyglycosides; sorbitan and sucrose esters and their ethoxylates; alkoxylated ethylenediamine; alcohol alkoxylates such as alcohol ethoxylates alcohol propoxylates, alcohol propoxylate ethoxylate propoxylates, alcohol ethoxylates butoxylates, fatty alcohol ethoxylates (e.g., tridecyl alcohol alkoxylate, ethylene oxide adduct), and the like; nonylphenol ethoxylate, polyoxyethylene glycol ethers, and the like; carboxylic acid esters such as glycerol esters, polyoxyethylene esters, ethoxylated fatty acid glycol esters; and the like; carboxylic amides such as diethanolamine condensates, monoalkanolamine condensates, polyoxyethylene fatty acid amides and the like; and polyalkylene oxide block copolymers including an ethylene oxide/propylene oxide block copolymer, such as those commercially available under the trademark PLURONIC (BASF-Wyandotte), and the like; commercially available ethoxylated amines and ether amines from Tomah Corporation and other nonionic compounds. Silicone surfactants such as ABIL B8852 (Goldschmidt) can also be used.
    [0058] The nonionic surfactant can include linear and secondary alcohol ethoxylates (fatty alcohol ethoxylates, eg, tridecyl alcohol alkoxylate, ethylene oxide adduct), alkylphenol ethoxylates, ethoxy/propoxy block surfactants and similar. Examples of preferred linear or secondary ethoxylates (fatty alcohol ethoxylates, eg, tridecyl alcohol alkoxylate, ethylene oxide adduct) include the primary, linear 12-14 carbon alcohol with five moles of ethoxylate (C12-14H25- 29)-O-(CH2CH2O)5H, which is sold under the trade name LAE 24-5), the 12-14 carbon, linear, primary alcohol with seven moles of ethoxylate (C12-14H25-29)-O- (CH2CH2O)7H (one of which is sold under the trade name LAE 24-7), the 12-14 carbon, linear, primary alcohol with twelve moles of ethoxylate (C12-14H25-29)-O-(CH2CH2O) 12H (one of which is sold under the trade name LAE 24-12), and the like.
    Anionic surfactants can include, for example, carboxylates such as alkylcarboxylates (carboxylic acid salts) and polyalkoxycarboxylates, alcohol ethoxylate carboxylates, nonylphenol ethoxylate carboxylates and the like; sulfonates, such as alkyl sulfonates, alkylbenzene sulfonates, (for example, linear dodecylbenzene sulfonic acid or salts thereof), alkylaryl sulfonates, sulfonated fatty acid esters, and the like; sulfates such as sulfated alcohols, sulfated alcohol ethoxylates, sulfated alkylphenols, alkyl sulfates, sulfosuccinates, alkyl ether sulfates and the like; and phosphate esters such as alkyl phosphate esters, ethoxylated phosphate alcohol esters, and the like.
    [0060]Surface active substances are classified as cationic if the charge on the hydrophilic portion of the molecule is positive. Surfactants in which the hydrophile carries no charge unless the pH is reduced to neutrality or below, but which are then cationic (eg, alkylamines), are also included in this group.
    [0061] Cationic surfactants can be found in some peroxygen solutions. Cationic surfactants can include compounds that contain at least one long carbon chain hydrophobic group and at least one positively charged nitrogen atom. The long carbon chain group can be attached directly to the nitrogen atom by simple substitution; or indirectly, by a bridged functional group or groups on so-called alkyl amines and interrupted amido amines. Such functional groups can make the molecule more hydrophilic and/or more dispersible in water, more easily solubilized in water by cosurfactant mixtures, and/or soluble in water. For increased water solubility, additional primary, secondary or tertiary amino groups can be introduced or the amino nitrogen can be quaternized with low molecular weight alkyl groups. Furthermore, nitrogen can be a part of a straight or branched chain portion of different degrees of unsaturation or a saturated or unsaturated heterocyclic ring. In addition, cationic surfactants can contain complex bonds that have more than one cationic nitrogen atom.
    [0062] The cationic surfactant may include a quaternary ammonium surfactant, such as a tallow quaternary ammonium surfactant, such as a tallow amine ethoxylated quaternary ammonium compound. For example, a tallow amine ethoxylated quaternary ammonium compound may include a quaternary nitrogen bonded to a methyl group, a tallow portion and two ethoxylate portions. The ethoxylate moieties can include 6 to 10 ethoxylate groups.
    [0063] Surfactant compounds classified as amine oxides, amphoterics and zwitterions are themselves typically cationic in nearly neutral to acidic pH solutions and may overlap the surfactant classifications. Polyoxyethylated cationic surfactants generally behave as nonionic surfactants in alkaline solution and as cationic surfactants in acidic solution.
    [0064] Most large volume commercial cationic surfactants can be subdivided into four main classes and additional subgroups, for example as described in “Surfactant Encyclopedia”, Cosmetics & Toiletries, vol. 104 (2) 86-96 (1989). The first class includes alkylamines and their salts. The second class includes alkylimidazolines. The third class includes ethoxylated amines. The fourth class includes quaternaries, such as alkylbenzyldimethylammonium salts, alkylbenzene salts, heterocyclic ammonium salts, dialkylammonium salts, and the like. Defoamers
    [0065]The solution can optionally include defoamers. Generally, defoamers can include silica and silicones, esters or aliphatic acids; alcohols; sulfates or sulfonates; amines or amides; halogenated compounds, such as fluorochlorohydrocarbons, vegetable oils, waxes, mineral oils, as well as their sulfated derivatives; and phosphates and phosphate esters such as alkali and alkyl diphosphates, and tributyl phosphates, among others; and its mixtures. Food grade defoamers are preferred. Silicones, such as dimethylsilicone, glycolpolysiloxane, methylphenolpolysiloxane, trialkyl or tetraalkylsilanes, hydrophobic silica defoamers and mixtures thereof can be used in defoaming applications. Commonly available commercial defoamers include silicones such as Ardefoam™ from Armor Industrial Chemical Company, which is a silicone bonded to an organic emulsion; Foam Kill™ or Kresseo™, available from Kirusable Chemical Company, which are silicone and non-silicone type defoamers as well as silicone esters; and Anti-Foam A™ and DC-200 from Dow Corning Corporation, which are both food grade silicones, among others. Corrosion Inhibitors
    [0066] The solution can optionally include a corrosion inhibitor. Useful corrosion inhibitors include polycarboxylic acids such as short chain carboxylic diacids, triacids, as well as phosphate esters and combinations thereof. Useful phosphate esters include alkyl phosphate esters, monoalkylaryl phosphate esters, dialkylaryl phosphate esters, trialkylaryl phosphate esters, and mixtures thereof, such as Emphos PS 236 commercially available from the Witco Chemical Company. Other useful corrosion inhibitors include triazoles such as benzotriazole, tolyltriazole and mercaptobenzothiazole, and in combinations with phosphonates such as 1-hydroxyethylidene-1,1-diphosphonic acid, and surfactants such as oleic acid diethanolamide and oleic sulfonate cocoamphohydroxypropyl, and the like. Useful corrosion inhibitors include polycarboxylic acids, such as dicarboxylic acids. Acids that are preferred include adipic, glutaric, succinic and mixtures thereof. Most preferred is a blend of adipic, glutaric and succinic acid, which is a raw material sold by BASF under the name SOKALAN™ DCS. Rheology Modifiers
    [0067]The solution may optionally include one or more rheology modifiers.
    [0068] Water-soluble or water-dispersible rheology modifiers that are useful can be classified as inorganic or organic. Organic thickeners can be further divided into natural and synthetic polymers, with the latter being further subdivided into synthetic natural based and synthetic petroleum based.
    [0069] Inorganic thickeners are generally compounds such as colloidal magnesium aluminum silica (VEEGUM™), colloidal clays (Bentonites) or silicas (CAB-O-SILS™), which have been fumigated or precipitated to create large particles surface to size ratios. Suitable natural hydrogel thickeners are primarily plant-derived exudates. For example, gum tragacanth, karaya and acacia; and extractives such as carrageenan, locust bean gum, guar gum and pectin; or pure culture fermentation products such as xanthan gum. Chemically, all these materials are salts of complex anionic polysaccharides. Applicationable synthetic natural-based thickeners are cellulose derivatives, in which the free hydroxyl groups in linear anhydrous glucose polymers have been etherified or esterified to produce a family of substances, which dissolve in water and produce viscous solutions. This group of materials includes alkyl and hydroxyalkylcelluloses, specifically methylcellulose, hydroxyethylmethylcellulose, hydroxypropylmethylcellulose, hydroxybutylmethylcellulose, hydroxyethylcellulose, ethylhydroxyethylcellulose, hydroxypropylcellulose and carboxymethylcellulose. Synthetic petroleum-based water-soluble polymers are prepared by direct polymerization of suitable monomers of which polyvinylpyrrolidone, polyvinylmethyl ether, polyacrylic acid and polymethacrylic acid, polyacrylamide, polyethylene oxide and polyethyleneimine are representative. Dyes and Fragrances
    [0070] The solution can optionally include various dyes, odorants including perfumes and other aesthetic enhancing agents. Preferred dyes include FD&C dyes, D&C dyes and the like.
    [0071]For a more complete understanding of the disclosure, the following examples are presented to illustrate some modalities. These examples and experiments are to be understood as being illustrative and not limiting. All parts are by weight unless otherwise indicated. Examples Example 1
    [0072] The purpose of example 1 was to characterize the impact of the enzyme catalase on the levels of hydrogen peroxide and peroxyacetic acid in a peroxygen solution. Various levels of the catalase enzyme Optimase® CA 400L (Genencor International, Rochester, NY) were added to a peroxygen solution at 25°C and held for 10 minutes during mixing. It is observed that the enzyme concentration measures the concentration of the active enzyme. The peroxygen solution was prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained 2952 ppm of hydrogen peroxide and 650 ppm of peracetic acid at the beginning of the experiment. After the 10-minute exposure, the levels of hydrogen peroxide and peroxyacetic acid were measured.
    [0073] The results are shown in figure 1 and demonstrate that the addition of catalase to a peroxygen solution resulted in significant elimination of hydrogen peroxide, but did not provide significant elimination of peroxyacetic acid. Example 2
    [0074] The purpose of example 2 was to characterize the impact of reducing agent sodium bisulfite upon the levels of hydrogen peroxide and peroxyacetic acid in a peroxygen solution. Various levels of sodium bisulfite (Sigma-Aldrich, St. Louis, MO) were added to a peroxygen solution at 25°C and held for 30 minutes. The peroxygen solution was prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained 225 ppm hydrogen peroxide and 50 ppm peracetic acid at the beginning of the experiment. After the 30-minute exposure, the levels of hydrogen peroxide and peroxyacetic acid were measured.
    [0075] The results are shown in figure 2 and demonstrate that the addition of sodium bisulfite to a peroxygen solution results in significant elimination of hydrogen peroxide and peroxyacetic acid. The hydrogen peroxide scavenging rate was proportional to the peroxyacetic acid scavenging rate. Example 3
    [0076] The purpose of example 3 was to characterize the impact of exposure time on the elimination of hydrogen peroxide from a peroxygen solution using catalase. The catalase enzyme Optimase® CA 400L (Genencor International, Rochester, NY) was added to a peroxygen solution to give a final concentration of 0.116 mg/L. The peroxygen solution was prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained 2893 ppm hydrogen peroxide and 634 ppm peracetic acid at the beginning of the experiment. At 2-minute intervals, the hydrogen peroxide level was measured.
    [0077] The results are shown in figure 3 and demonstrate that the addition of catalase to a peroxygen solution eliminated about 50, 90 and 99% of the initial level of hydrogen peroxide in 1, 5 and 10 minutes, respectively. Example 4
    [0078] The purpose of example 4 was to characterize the impact of exposure temperature on the degradation of hydrogen peroxide from a peroxygen solution using catalase. Various levels of the catalase enzyme Optimase® CA 400L (Genencor International, Rochester, NY) were added to the peroxygen solutions at different temperatures. Peroxygen solutions were prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained approximately 2950 ppm of hydrogen peroxide and approximately 650 ppm of peracetic acid at the beginning of the experiment. After a 10-minute exposure, the hydrogen peroxide level was measured. Data were normalized to account for slight differences in starting concentrations, and log-transformed to fit a linear model.
    [0079] The results are shown in figure 4 and demonstrate that the effectiveness of catalase for the degradation of hydrogen peroxide in peroxygen solutions was more effective within a temperature range of about 25 to 50 °C. The effectiveness of catalase for scavenging hydrogen peroxide in peroxygen solutions was reduced at temperatures above 50 °C, and at 4 °C. Example 5
    [0080] The purpose of example 5 was to compare TDS levels in neutralized peroxygen solutions using two different processes: (1) a process using only the reducing agent sodium bisulfite, and (2) a process using the enzyme catalase followed by sodium bisulfite. In a first experiment, a minimal level of sodium bisulfite (Sigma-Aldrich, St. Louis, MO) was added to a peroxygen solution to degrade both hydrogen peroxide and peroxyacetic acid. In a second experiment, in a first step, the minimal level of catalase enzyme Optimase® CA 400L (Genencor International, Rochester, NY) was added to a peroxygen solution to degrade hydrogen peroxide in just 10 minutes at 25 °C. In a second step, a minimal level of sodium bisulfite was added to the peroxygen solution to degrade the remaining peroxygen compounds. Peroxygen solutions in both experiments were prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained 2952 ppm hydrogen peroxide and 650 ppm peracetic acid at the beginning of the experiment.
    [0081] The results are shown in table 1 and demonstrate that the level of TDS in a peroxygen solution treated using only the reducing agent sodium bisulphite (Process 1) was 13.6 times higher than a process using the enzyme catalase followed by sodium bisulfite (Process 2). Table 1
    Example 6
    [0082] The purpose of example 6 was to compare the levels of total peroxygen compounds in a treated peroxygen solution using a variation of Process 2 described in example 5, specifically, a process in which the order of addition was reversed (this is, sodium bisulfite was added first, then catalase). This new process was designated Process 3. In this experiment, in a first step, the same level of sodium bisulfite (Sigma-Aldrich, St. Louis, MO) used in Example 5, Process 2, was added to a peroxygen solution. not. In a second step, the same level of catalase enzyme Optimase® CA 400L (Genencor International, Rochester, NY) used in Example 5, Process 2 was added to the peroxygen solution. The peroxygen solution used in the experiment was prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained 2886 ppm of hydrogen peroxide and 636 ppm of peracetic acid at the beginning of the experiment.
    [0083] The results are shown in Table 2 and demonstrate that reversing the order of addition (ie, adding the reducing agent first, then the enzyme) was not effective in degrading the peroxygen compounds. Table 2
    Example 7
    [0084] The purpose of example 7 was to characterize how the efficiency of hydrogen peroxide degradation in a peroxygen solution is affected when the ratio of enzyme to peroxygen compounds is changed. Catalase enzyme Optimase® CA 400L (Genencor International, Rochester, NY) was added to two different peroxygen solutions to result in a final enzyme concentration of 0.039 mg/L. The peroxygen solution was prepared from Oxonia Active® (Ecolab Inc., St. Paul, MN) and contained 2943 ppm hydrogen peroxide and 650 ppm peracetic acid at the beginning of the experiment (Peroxygen Solution 1), or 577 ppm of hydrogen peroxide and 129 ppm of peracetic acid at the beginning of the experiment (Peroxygen Solution 2). After a 10 minute exposure to 55 °C, the hydrogen peroxide level was measured.
    [0085] The results are shown in table 3 and demonstrate that the degradation of hydrogen peroxide in a peroxygen solution is more effective when the ratio of enzyme to hydrogen peroxide is increased. Thus, it may be preferable to add a defined amount of enzyme to the peroxygen solution before that peroxygen solution is diluted. Table 3
    Example 8
    [0086] The purpose of example 8 was to determine the effectiveness of the disclosed method in a commercial-scale beverage plant's extended shelf-life food packaging line. The impact of reagent dose, contact time and temperature was also evaluated.
    [0087]Various concentrations of Oxonia Active were applied to containers on the packaging line. After the containers were treated, the spent peroxygen solutions were collected. Various concentrations of the enzyme catalase (Optimase CA-400L) were added to the solution and allowed to react. Then, various concentrations of BC1002 (30% sodium metabisulfite solution, commercially available from Ecolab Inc., St. Paul, MN) were added to the solution and allowed to react. Samples were collected after the addition of enzyme and sodium metabisulphite and analyzed. The results are shown below.
    [0088] Table 4 shows that a dose of 1 part catalase to 5,000 parts hydrogen peroxide at a contact time of 20 minutes, in general, reduced the hydrogen peroxide concentration to below the detection limit of the method of test used. The highest concentrations decreased in as little as 10 minutes. Table 4

    [0089] Table 5 shows that the degradation of hydrogen peroxide by catalase increases as the temperature increases, which may be desirable for compositions with low concentrations of peroxygen. Table 5

    [0090] Tables 6 and 7 show that a dose of 1.75 to 2.6 parts of sodium metabisulfite from BC1002 (30% sodium metabisulfite) per part of peracetic acid with a contact time of 10 minutes adequately reduced the concentration of peracetic acid. Table 6

    Table 7

    [0091] Table 8 determined the effect of temperature on the ability of sodium metabisulfite in BC1002 (30% sodium metabisulfite) to reduce the concentration of peracetic acid, at a ratio of 1.75 part sodium metabisulfite to 1 part of peracetic acid. Table 8 shows that temperature has very little effect on the reduction of peracetic acid. Table 8

    [0092] Table 9 determined the effect of the initial concentration of peracetic acid and the contact time in the reaction between sodium metabisulfite and peracetic acid. Table 9 shows that the reaction of BC1002 sodium metabisulfite with peracetic acid at a ratio of 1.75:1 generally appears to complete in less than 10 minutes, but also appears to produce a secondary residue at higher initial acid concentrations peracetic, which suggests that the reaction rate is concentration dependent. Table 9

    [0093] The above summary, detailed description and examples provide a solid foundation for understanding the disclosure and some specific examples. As the invention may comprise a variety of embodiments, the above information is not intended to be limiting. The invention consists of the claims.
    权利要求:
    Claims (11)
    [0001]
    1. Method for treating a peroxygen solution, CHARACTERIZED by the fact that it comprises: a) collecting an initial peroxygen solution comprising a peracid and hydrogen peroxide, wherein the initial peroxygen solution is collected from a decontamination process, process from a bleaching or oxidation process in a food and beverage plant, health care facility, kitchen, restaurant, laundry, or wastewater treatment plant; b) add 1 mg/L or less of an isolated enzyme for every 1000 mg/L of hydrogen peroxide to the initial peroxygen solution and then c) add a reducing agent to the initial peroxygen solution, where 0.1 part to 5 parts of hydrogen peroxide is degraded by the enzyme for every 1 part of the peracid and hydrogen peroxide that is degraded by the reducing agent; and d) forming a treated peroxygen solution as a result of the addition of the enzyme and reducing agent.
    [0002]
    2. Method according to claim 1, CHARACTERIZED by the fact that the peracid is selected from the group consisting of peracetic acid, peroctanoic acid and mixtures thereof.
    [0003]
    3. Method according to claim 1, CHARACTERIZED by the fact that the enzyme is selected from the group consisting of catalase, peroxidase and mixtures thereof.
    [0004]
    4. Method according to claim 1, CHARACTERIZED by the fact that the reducing agent is selected from the group consisting of bisulfite salts, metabisulfite salts, thiosulfate salts, sulfite salts, sulfur dioxide, coal vegetable, activated carbon, ascorbic acid, erythorbic acid, metal catalysts, UV light and mixtures thereof.
    [0005]
    5. Method according to claim 1, CHARACTERIZED by the fact that the pH of the initial peroxygen solution is from 1 to 10.
    [0006]
    6. Method according to claim 1, CHARACTERIZED by the fact that the concentration of peracid in the initial peroxygen solution is from 1 ppm to 50,000 ppm.
    [0007]
    7. Method according to claim 1, CHARACTERIZED by the fact that the treated peroxygen solution is further treated with a wastewater treatment process.
    [0008]
    8. Method, according to claim 1, CHARACTERIZED by the fact that the concentration of peracid in the treated peroxygen solution is from 0.1 ppm to 1,000 ppm.
    [0009]
    9. Method according to claim 1, CHARACTERIZED by the fact that the total dissolved solids in the treated peroxygen solution does not increase by more than 10,000 ppm.
    [0010]
    10. Method according to claim 1, CHARACTERIZED by the fact that the initial or treated peroxygen solution further comprises a material selected from the group consisting of a carboxylic acid, stabilizing agent, hydrotrope, surfactant, defoamer, inhibitor corrosion, rheology modifier, dye, fragrance, water, sugar, salt, fat, oil, protein, starch, detergent, mineral, dirt, blood and mixtures thereof.
    [0011]
    11. Method according to claim 1, CHARACTERIZED by the fact that the enzyme and the reducing agent are added to the peroxygen solution after it has been used in a decontamination, bleaching or oxidation process, but before being combined with other waste streams.
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    同族专利:
    公开号 | 公开日
    ES2669818T3|2018-05-29|
    EP2542103B1|2018-04-25|
    JP2016137491A|2016-08-04|
    CA2789964C|2020-07-21|
    WO2011107942A3|2012-01-12|
    RU2012141885A|2014-04-10|
    CN102781263A|2012-11-14|
    CN105836897A|2016-08-10|
    EP2542103A2|2013-01-09|
    MX2012009983A|2012-10-05|
    WO2011107942A2|2011-09-09|
    RU2565435C2|2015-10-20|
    US9254400B2|2016-02-09|
    MX340127B|2016-06-28|
    CA2789964A1|2011-09-09|
    US20110217761A1|2011-09-08|
    AU2011222493B2|2016-11-03|
    JP2013521116A|2013-06-10|
    AU2011222493A1|2012-08-30|
    BR112012021933A2|2015-09-08|
    EP2542103A4|2013-11-20|
    JP6001458B2|2016-10-05|
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    法律状态:
    2018-04-10| B06F| Objections, documents and/or translations needed after an examination request according [chapter 6.6 patent gazette]|
    2019-12-17| B15K| Others concerning applications: alteration of classification|Free format text: AS CLASSIFICACOES ANTERIORES ERAM: A23L 3/34 , A23L 2/70 Ipc: C02F 1/70 (1980.01), C02F 101/10 (2000.01), C02F 1 |
    2019-12-24| B06U| Preliminary requirement: requests with searches performed by other patent offices: procedure suspended [chapter 6.21 patent gazette]|
    2020-11-17| B06A| Notification to applicant to reply to the report for non-patentability or inadequacy of the application [chapter 6.1 patent gazette]|
    2021-03-16| B09A| Decision: intention to grant [chapter 9.1 patent gazette]|
    2021-04-06| B09X| Decision of grant: republication|
    2021-05-18| B16A| Patent or certificate of addition of invention granted|Free format text: PRAZO DE VALIDADE: 20 (VINTE) ANOS CONTADOS A PARTIR DE 02/03/2011, OBSERVADAS AS CONDICOES LEGAIS. PATENTE CONCEDIDA CONFORME ADI 5.529/DF |
    优先权:
    申请号 | 申请日 | 专利标题
    US30963910P| true| 2010-03-02|2010-03-02|
    US61/309,639|2010-03-02|
    PCT/IB2011/050873|WO2011107942A2|2010-03-02|2011-03-02|Method for processing peroxygen solutions|
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