EP1740684A1 - Verfahren zur herstellung von festen granulaten mit verbesserter lagerstabilität und abriebfestigkeit - Google Patents
Verfahren zur herstellung von festen granulaten mit verbesserter lagerstabilität und abriebfestigkeitInfo
- Publication number
- EP1740684A1 EP1740684A1 EP05740613A EP05740613A EP1740684A1 EP 1740684 A1 EP1740684 A1 EP 1740684A1 EP 05740613 A EP05740613 A EP 05740613A EP 05740613 A EP05740613 A EP 05740613A EP 1740684 A1 EP1740684 A1 EP 1740684A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- granules
- enzyme
- cellulose
- enzymes
- coating
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D11/00—Special methods for preparing compositions containing mixtures of detergents
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/2041—Dihydric alcohols
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/20—Organic compounds containing oxygen
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- C11D3/2065—Polyhydric alcohols
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/37—Polymers
- C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
- C11D3/3707—Polyethers, e.g. polyalkyleneoxides
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/37—Polymers
- C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
- C11D3/3753—Polyvinylalcohol; Ethers or esters thereof
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/384—Animal products
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38672—Granulated or coated enzymes
Definitions
- the present invention relates to a process for the production of solid granules with improved storage stability and abrasion resistance, in particular of enzyme granules which are an admixture component for detergents and / or cleaning agents, and detergents and / or cleaning agents which contain such granules.
- Chemical compounds manufactured industrially as solids, which are offered either as finished products or for further processing, are usually in the form of powders, flakes or granules.
- the granules in particular are characterized by good flow and free-flowing properties and a high bulk density.
- a further step based on this can be the mechanical compacting of such mixtures to macroscopic pieces, as is the case, for example, in the application JP 2004059606 A (cited from its German-language summary) for detergents and cleaning agents, perfumes, deodorants, bleaches, fertilizers, water quality improvers and others Compositions is listed, after which the ingredients are additionally mixed with a liquid before pressing.
- the solids are preferably used in the form of granules in many industrial processes.
- An example of such processes is the production of detergents and cleaning agents in granulation plants, e.g. B. in fluidized beds, mixers, extruders, rollers or in a combination of these systems.
- the products produced which are either produced as intermediate detergent products or admixture components or as finished detergents and cleaning agents, are advantageously distinguished by relatively high bulk densities compared to sprayed products and by good rubble and free-flowing behavior. They also have the advantage that their particle size distribution is adjusted so that the dust content is only low.
- enzymes in solid or in liquid form for various technical purposes, in particular in detergents and cleaning agents, is well established in the prior art.
- the enzymes in question are required in solid and also low-water form, for example as granules or as a rounded extrudate.
- they can be coated with protective layers.
- the protective layer thus serves to prevent chemical reactions, which is of crucial importance for long-term stability, the exclusion of direct skin contact, the avoidance of abrasion by the lungs, the increase in mechanical stability and the establishment of a controlled release effect.
- the aesthetics of the particles in particular the color, but also the smell, can be improved via the protective layer.
- the same technique can also be applied to particles of other detergent ingredients, in particular those that are sensitive to the other ingredients and / or to moisture and can react undesirably or that tend to form dust during mechanical stress.
- allergic reactions to quaternary ammonium compounds are also known.
- Protective layers for particulate detergent ingredients, in particular for enzyme particles are described in detail in the prior art. These include, for example, those in which the active ingredient as a particle core is surrounded by a simple protective layer.
- Protective compounds which are applied, for example, as a solution or as a melt are, for example, oily or waxy substances, mostly water-soluble polymers, surfactants or plastics formed in situ by condensation polymerization, but also inorganic substances such as silicates (water glass) or kaolins.
- pigments into such protective layers which improve the encapsulation effect or serve the coloring; minerals such as clays or white pigments such as CaCO 3 , ZnO or TiO 2 are described for this purpose.
- the wax-like substances such as polyethylene glycols (PEG) or polyvinyl alcohols (PVA) then also have a binding function compared to the pigments.
- PEG polyethylene glycols
- PVA polyvinyl alcohols
- Numerous patent applications deal with the optimization of the compositions of such coating solutions for coating solids.
- Multi-coated particles of detergent ingredients, in particular enzymes have also been described in the prior art.
- the enzyme component does not itself have to represent the substantial core of the particle, but can be applied in the form of a protein-salt mixture as a separate layer to an inert core, the so-called seed particle.
- Starch, modified starch, carrageenan, gum arabic, guar gum, polyethylene oxide, polyvinylpyrrolidone or polyethylene glycol are used as optional binder substances within the enzyme layer.
- a second layer of compounds such as polyvinyl alcohols (PVA), polyvinyl pyrrolidone, cellulose derivatives, polyethylene glycols (PEG), polyethylene oxide, chitosan, gum arabic, xanthan and carrageenan can be applied to the enzyme layer in order to coat the seed particle or to coat the enzyme-coated particle protect outside.
- PVA polyvinyl alcohols
- PEG polyethylene glycols
- chitosan chitosan
- gum arabic xanthan and carrageenan
- Corresponding production processes in a fluid bed reactor are also disclosed in this application.
- WO 03/055967 A1 describes an improved method for coating core particles with a salt layer.
- WO 92/11347 A2 discloses enzyme granules for use in granular detergents and cleaning agents which contain 2% by weight to 20% by weight of enzyme, 10% by weight to 50% by weight of swellable starch, 5% by weight. % to 50% by weight of water-soluble organic polymer as granulation aid, 10% by weight to 35% by weight of cereal flour and 3% by weight to 12% by weight of water. Such additives enable enzyme processing without major loss of activity.
- Coated enzyme granules are disclosed in the patent EP 804532 B1, the enzyme granules themselves having been obtained by coating an inert core and a coating material is applied thereon, which consists of a non-aqueous liquid or an aqueous emulsion thereof or of an ointment-like mixture of such a liquid or Emulsion with a component melting between 30 and 90 ° C.
- the protective layer should contain an agent that prevents agglomeration, such as silica fume, calcium phosphate, titanium dioxide, talc or starch, and should result in a low dust number triggered by the particles.
- the production of such particles is in any type of mixer or by spraying on the coating materials.
- one or more pre-coatings of the enzyme-containing particles can be carried out before the actual coating, preferably in a fluidized bed reactor.
- Patent EP 716685 B1 discloses a process according to which an enzyme-containing core, optionally containing carrier materials and granulating aids, is obtained by extrusion, optionally treated in intermediate steps and then coated with a layer of a second, previously particulate enzyme, and optionally binder, and that granules obtained are optionally protected externally with a dye or pigment-containing coating.
- an enzyme-containing core optionally containing carrier materials and granulating aids
- An enzyme layer is then applied directly or optionally via an intermediate layer containing vinyl polymer or vinyl copolymer, which also contains vinyl polymer or vinyl copolymer; this is closed to the outside - optionally via a further intermediate layer, which in turn contains an enzyme-protecting compound (in particular a chlorine scavenger) - by a layer which also contains vinyl polymer or vinyl copolymer and optionally pigments and / or binders.
- an enzyme-protecting compound in particular a chlorine scavenger
- Polyvinyl alcohols of different molecular weights, different degrees of hydrolysis or viscosities or mixtures of different polyvinyl alcohols are particularly preferred as vinyl polymers.
- WO 00/01793 A1 discloses a coating with a high moisture content. It consists of at least 60% by weight of a water-soluble substance with a molecular weight of less than 500 g / mol, a certain pH value and with a constant moisture content of more than 81% at 20 ° C. This coating is applied as a solution and the solvent is then distilled off. These water-soluble substances include inorganic salts such as sodium sulfate and citrate. The particles obtained can optionally be coated with further layers, both under the coating with a high moisture content and above it.
- the application WO 03/000625 A2 chooses a physical approach for describing the desirable properties of granules of active ingredients, such as enzymes, which are to be protected against mechanical stress. It is recommended that such granules be coated with a flexible polymer film, this polymer should have a certain biophysical property, namely a given maximum elongation value ("elongation upon break"). Examples of this are polymers such as PVA, gelatin or modified starch indicated, optionally with plasticizers such as glycerol or propylene glycol, the possible mixtures to be checked with regard to the maximum elongation value mentioned.
- the application US 2004/0033927 A1 discloses granules of the core / shell type, the core matrix of which contains, in addition to the active substance, 0.1 to 10% by weight of a synthetic polymer and 0.2 to 5% by weight of an antioxidant or reducing agent.
- WO 2004/058933 A1 describes an alternative chemical approach, according to which a plasticizable substance (“plasticizer”) is applied to the granulate after it has been produced, above its specific glass transition temperature, and is absorbed into the porous granulate by at least 50% of the substance in question are coated (“impregnated”) and have high mechanical stability.
- plasticizer a plasticizable substance
- the disadvantage of this method is that a large number of substances to be granulated, such as fragrances or enzymes, are destroyed at high temperatures, so that this method can only be used to a limited extent for these substances.
- the object was therefore to provide an inexpensive process for the production of solid granules, as a result of which mechanically sufficiently stable and abrasion-resistant solid granules with a low water content are obtained.
- the granulate according to the invention is also mechanically more stable, which leads to a lower dust development. This is particularly important in the case of enzyme granules, which are incorporated in large quantities in detergents and cleaning agents, and increases product safety considerably, since enzyme dusts, in particular those from proteases, can cause allergic reactions of the skin and the respiratory tract.
- the present invention thus relates to a process for the production of solid granules with improved storage stability and abrasion resistance, which is characterized in that hygroscopic polyols are added.
- Solid granules produced in a comparable manner, but without the addition of hygroscopic polyols, are brittle, on the one hand, so that they release abrasion more easily under mechanical stress and, after storage for the same length of time, have lower enzyme activities.
- higher enzyme stability is thus achieved by adding hygroscopic polyols.
- the hygroscopic polyols to be added according to the invention can, for example, be added to the concentrate to be granulated, for example the enzyme obtained after the enzyme work-up, or to the premix (premix), provided that the concentrate to be assembled is further processed prior to granulation by adding additives.
- This premix is to be understood as the mixture introduced into the actual packaging step (for example granulation and / or extrusion). This is, for example, the blending of an enzyme concentrate with the additives starch, cellulose powder or zeolite described below.
- a method according to the invention preferably comprises the extrusion step.
- the extrusion can also be used for the preparation of enzyme preparations. According to the invention, this is particularly advantageous because the thermal load on the enzyme preparation can be kept low. According to the invention, all known technical facilities for extrusion can in principle be used.
- the hygroscopic polyols are selected from: ethylene glycol, propylene glycol, triethylene glycol, glycerol, monoglycerides, diglycerides, polyethylene glycols (PEG), polypropylene glycols (PPG), polyvinyl alcohols (PVA), polysaccharides, cellulose ethers, alginates, modified and their hydrolyzates, the polymers and copolymers of these compounds or their copolymers with other polymers which are selected from polyethylene oxides, polyvinylpyrrolidones (PVP) and gelatin, in particular selected from: glycerol, cellulose, sorbitol, sucrose and starch.
- PEG polyethylene glycols
- PPG polypropylene glycols
- PVA polyvinyl alcohols
- PVP polyvinylpyrrolidones
- gelatin in particular selected from: glycerol, cellulose, sorbitol, sucrose and starch.
- hygroscopic polyols and / or their polymers for example from PEG or PPG which are liquid at the processing temperature.
- the hygroscopic polyols can be used individually or in a mixture.
- the production of the granulate particles according to the invention is preferably based on fermentation broths which For example, microfiltration can be used to remove insoluble accompanying substances.
- the microfiltration is preferably carried out as cross-flow microfiltration using porous tubes with micropores larger than 0.1 ⁇ m, flow rates of the concentrate solution of more than 2 m / s and a pressure difference to the permeate side of less than 5 bar, as described for example in EP 200032 B1 ,
- the microfiltration permeate is then concentrated to a desired enzyme content, preferably by ultrafiltration, optionally with subsequent vacuum evaporation.
- the concentration can, as described in WO 92/11347 A2, be carried out in such a way that only relatively low dry matter contents (TS) of preferably 15% by weight to 50% by weight, in particular 20% by weight, are obtained. % to 35% by weight.
- TS dry matter contents
- Processes according to the invention are preferably those which are characterized in that the hygroscopic polyols, in particular those listed above, are used in an amount of 0.1 to 10% by weight, in particular 3 to 7% by weight ,
- This quantity refers to the premix (premix), which contains the active substance to be assembled, additives and in many cases water; the latter applies in particular to the packaging of enzymes which are usually obtained from working up an aqueous solution.
- a higher concentration must be set if the hygroscopic polyols are not added to the premix but already to the concentrate to be granulated.
- This process variant is advantageous if, for example for modulating the physical properties of the granules, an intimate mixture of the hygroscopic polyol with the active component is to be achieved before the additives are added.
- compositions according to the invention which (if appropriate additionally) are characterized in that stabilizers are additionally added in a concentration of preferably 0.1 to 5% by weight, in particular 1 to 4% by weight.
- weight percentages in turn relate to the premix (premix) and are to be adjusted accordingly when additives are added.
- Stabilizers are to be understood in principle as meaning all chemical compounds which contain a protein and / or enzyme contained in a granulate according to the invention, particularly during storage, against damage such as inactivation, denaturation or decomposition, for example due to physical influences, oxidation or protect proteolytic cleavage.
- those are selected which in themselves only result in a low odor load.
- a group of stabilizers are reversible protease inhibitors.
- Benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters are frequently used for this, including above all derivatives with aromatic groups, for example ortho-, meta- or para-substituted phenylboronic acids, in particular 4-formylphenylboronic acid, or the salts or Esters of the compounds mentioned.
- Peptide aldehydes that is to say oligopeptides with a reduced C-terminus, in particular those of 2 to 50 monomers, are also used for this purpose.
- the peptide reversible protease inhibitors include, among others, ovomucoid and leupeptin. Specific, reversible peptide inhibitors for the protease subtilisin as well as fusion proteins from proteases and specific peptide inhibitors are also suitable for this.
- Further enzyme stabilizers are amino alcohols such as mono-, di-, triethanol- and -propanolamine and their mixtures, aliphatic carboxylic acids up to C 12 , such as succinic acid, other dicarboxylic acids or salts of the acids mentioned. End-capped fatty acid amide alkoxylates are also suitable for this purpose. Certain organic acids used as builders, as disclosed in WO 97/18287, can additionally stabilize an enzyme contained.
- Lower aliphatic alcohols but above all polyols, such as glycerol, ethylene glycol, propylene glycol or sorbitol are further frequently used enzyme stabilizers, so that if they are already used according to the invention as a hygroscopic polyol to improve storage stability and abrasion resistance, they have a double function.
- Di-glycerol phosphate also protects against denaturation due to physical influences.
- Calcium and / or magnesium salts are also used, such as calcium acetate or calcium formate.
- Polyamide oligomers or polymeric compounds such as lignin, water-soluble vinyl copolymers or cellulose ethers, acrylic polymers and / or polyamides stabilize the enzyme preparation against physical influences or pH fluctuations, among other things.
- Polymers containing polyamine-N-oxide act simultaneously as enzyme stabilizers and as color transfer inhibitors.
- Other polymers Stabilizers are linear C 8 -C 18 polyoxyalkylenes.
- Alkyl polyglycosides can also stabilize the enzymatic components of the agent according to the invention and preferably are capable of additionally increasing their performance.
- Crosslinked N-containing compounds preferably fulfill a double function as soil release agents and as enzyme stabilizers. Hydrophobic, nonionic polymer in particular stabilizes any cellulase that may be present.
- Reducing agents and antioxidants increase the stability of the enzymes against oxidative decay;
- sulfur-containing reducing agents are common.
- Other examples are sodium sulfite and reducing sugars.
- Combinations of stabilizers are particularly preferably used, for example made of polyols, boric acid and / or borax, the combination of boric acid or borate, reducing salts and succinic acid or other dicarboxylic acids or the combination of boric acid or borate with polyols or polyamino compounds and with reducing salts.
- the action of peptide-aldehyde stabilizers is favorably increased by the combination with boric acid and / or boric acid derivatives and polyols and even further by the additional action of divalent cations, such as calcium ions.
- stabilizers are selected from: ascorbic acid, sodium citrate, sodium sulfite, sodium thiosulfate and mixtures thereof. Because especially with enzyme granules, their reduction or antioxidant effect is required in particular.
- the granules produced by the process according to the invention can contain different active substances.
- organic-chemical compounds such as proteins, in particular enzymes, polysaccharides or non-biological polymers, polyethylene glycols, natural or synthetic fats, long-chain fatty acids, long-chain fatty acids (as the ingredients actually to be assembled)
- Fatty alcohols, biopolymers (e.g. xanthan), paraffins or long-chain nonionic surfactants can be incorporated individually, in a mixture and / or in carrier substances.
- those methods are furthermore preferred which are characterized in that enzymes obtained from the microorganisms and freed from the cells, such as proteases, lipases, amylases, mannanases and / or cellulases, preferably proteases produced by Bacillus aes or derived therefrom , alone or in combination with other enzymes.
- enzymes obtained from the microorganisms and freed from the cells such as proteases, lipases, amylases, mannanases and / or cellulases, preferably proteases produced by Bacillus aes or derived therefrom , alone or in combination with other enzymes.
- an enzyme concentrate is added in an amount of about 15 to 40%, in particular 20 to 35%, based on the moist premix to be granulated.
- the amount of cellulose used is advantageously about 0 to 5%, in particular 1 to 3%; the amount of sugar optionally used is about 0 to 5%, in particular 1 to 3% and the amount of stabilizer optionally used is about 0 to 5%, especially 1 to 4%.
- Suitable stabilizers for the enzyme concentrate are, for example, ascorbic acid, sodium citrate and sodium sulfite.
- the hygroscopic polyol, in particular glycerol is preferably used in an amount of 0-10%, in particular 3-7%.
- the viscosity of the concentrate is preferably in the range from 1 to 200 mPas, in particular 1 to 25 mPas.
- the enzyme activity of the concentrate if it is a protease granulate, is preferably 500,000 to 1,500,000 HPE / g, in particular 1,000,000 to 1,300,000 HPE / g, or if it is an amylase granulate, at preferably 25,000 to 75,000 TAU / g, in particular 50,000 to 65,000 TAU / g.
- protease activity in HPE can be determined according to van Raay, Saran and Verbeek, according to the publication "For the determination of proteolytic activity in enzyme concentrates and detergents, detergents and cleaning agents containing enzymes" in Tenside (1970), Volume 7, pp. 125-132
- a modified p-nitrophenylmaltoheptaoside is used, the terminal glucose unit of which is blocked by a benzylidene group, which is cleaved by amylase to free p-nitrophenyl-oligosaccharide, which in turn uses the auxiliary enzymes glucoamylase and alpha-glucosidase and p-nitrophenol.
- the amount of p-nitrophenol released is proportional to the amylase activity.
- the measurement is carried out, for example, with the Quick-Start ® test kit from Abbott, Abott Park, Illinois, USA.
- the increase in absorption (405 nm) in the test batch is detected against a blank value using a photometer at 37 ° C. for 3 min alibration via an enzyme standard of known activity (eg Maxamyl ® / ® Purastar® 2900 Genencor, Palo Alto, CA, USA, with 2900 TAU / g).
- the evaluation is carried out by plotting the absorption difference dE (405 nm) per min against the enzyme concentration of the standard.
- the enriched concentrate which may have been formed in this way is stirred and then advantageously sprayed onto a carrier matrix for conversion into a premix.
- a carrier matrix for conversion into a premix.
- all organic or inorganic pulverulent substances which do not destroy or inactivate the enzymes to be granulated, or tolerably little, and which are stable under granulation conditions, can be used as carrier materials for the enzyme.
- Such substances include, for example, starch, cereal flour, cellulose powder, alkali alumosilicate, in particular zeolite, layered silicate, for example bentonite or smectite, and water-soluble inorganic or organic salts, for example alkali metal chloride, alkali metal sulfate, alkali metal carbonate, citrate or acetate, where sodium or potassium preferred alkali metals.
- a carrier material mixture is preferably used which contains starch which is swellable in water and optionally corn flour, cellulose powder and / or alkali carbonate.
- the water-swellable starch is preferably corn, wheat and rice and potato starch or mixtures of these, with the use of corn and wheat starch being preferred.
- Swellable starch is contained in the enzyme granules according to the invention preferably in amounts from 1% by weight to 50% by weight, in particular from 1 to 10% by weight, preferably from 3% by weight to 6% by weight.
- the cereal flour which may be present is in particular a product which can be produced from wheat, rye, barley or oats or a mixture of these flours, wholemeal flours being preferred.
- a wholemeal flour is understood to mean a flour that has not been fully ground, which has been produced from whole, unpeeled grains or at least predominantly consists of such a product, the rest consisting of fully ground flour or starch.
- Commercial wheat flour qualities such as Type 450 or Type 550 are preferably used. It is also possible to use flour products from the cereals leading to the above-mentioned swellable starches, provided that care is taken to ensure that the flours have been produced from the whole grains.
- the flour component of the additive mixture is known to achieve a substantial reduction in odor of the enzyme preparation, which far exceeds the reduction in odor by incorporating the same amounts of corresponding starch types.
- Such cereal flour is contained in the enzyme granules according to the invention preferably in amounts of up to 45% by weight, in particular from 10% by weight to 28% by weight.
- the enzyme granules according to the invention preferably receive the alkali as a further component of the carrier material as a further component of the carrier material, based on the entire granulate, of a granulating aid system, 1 wt.% To 50 wt.%, In particular 5 wt.% To 25 wt -Carboxymethylcellulose with degrees of substitution from 0.5 to 1 and polyethylene glycol and / or alkyl polyethoxylate contains.
- granulation aid system based in each case on the finished enzyme granulate, 0.5 wt.% To 5 wt.% Alkali carboxymethyl cellulose with degrees of substitution from 0.5 to 1 and up to 4 wt.%
- Polyethylene glycol with an average molecular weight of preferably contain 400 to 35,000, in particular 1,500 to 4,000, and / or alkyl polyethoxylate.
- Phosphated, optionally partially hydrolyzed starches are also suitable as granulation aids.
- Phosphated starch is understood to mean a starch derivative in which hydroxyl groups of the starch anhydroglucose units are replaced by the group -OP (O) (OH) 2 or its water-soluble salts, in particular alkali metal salts such as sodium and / or potassium salts.
- the average degree of phosphatization of the starch is to be understood as the number of esterified oxygen atoms bearing a phosphate group per saccharide monomer of the starch, averaged over all saccharide units.
- the average degree of phosphatization in the case of preferably used phosphated starches is in the range from 1.5 to 2.5, since especially when they are used, much smaller amounts are required in order to achieve a certain granule strength than when using carboxymethyl cellulose.
- partially hydrolyzed starches are to be understood as meaning oligomers or polymers of carbohydrates which are accessible by conventional, for example acid or enzyme-catalyzed, processes by partial hydrolysis of starch. They are preferably hydrolysis products with average molecular weights in the range from 440 to 500,000.
- DE dextrose equivalent
- DE a customary measure of the reducing action of a polysaccharide compared to dextrose, which has a DE of 100
- maltodextrins DE 3 to 20
- dry glucose syrups DE 20 to 37
- yellow dextrins white dextrins with higher average molecular weights in the range of approximately 2,000 to 30,000
- contents of 0.1% by weight to 20% by weight, in particular 0.5% by weight to 15% by weight, of phosphated starch are preferred.
- additional cellulose or starch ethers such as carboxymethyl starch, methyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose and corresponding cellulose mixed ethers, gelatin, casein, tragacanth, maltodextrose, sucrose, invert sugar, glucose syrup or other water-soluble or readily dispersible olefin can also be used as additional constituents of the granulation aid system or polymers of natural or synthetic origin can be used.
- Useful synthetic water-soluble polymers are polyacrylates, polymethacrylates, copolymers of acrylic acid with maleic acid or compounds containing vinyl groups, furthermore polyvinyl alcohol, partially saponified polyvinyl acetate and polyvinylpyrrolidone.
- the aforementioned compounds are those with free carboxyl groups, they are normally in the form of their alkali metal salts, in particular their sodium salts.
- Such additional granulation aids can be contained in the enzyme granules according to the invention in amounts of up to 10% by weight, in particular from 0.5% by weight to 8% by weight.
- an enzyme to be incorporated is coated before it is incorporated into the mixture of the additives described above.
- the aqueous, concentrated enzyme solution is preferably mixed with a substance with surface-active properties, for example a surfactant (nonionic or anionic surfactant), before it is introduced into the mixer with the matrix material.
- a surfactant nonionic or anionic surfactant
- the surfactant molecules then arrange themselves in the approx. 10 ⁇ m large liquid drops so that the hydrophobic parts of the molecule point outwards.
- particles are then obtained which are coated with a wafer-thin surfactant layer and embedded in the matrix.
- polymers which are hydrophobic for example cellulose ethers such as HEC (hydroxyethyl cellulose) or starch ether, or synthetic polymers with similar properties, for example PVA or end-capped PEG (for example C-is-EO ; see also the book "Water-soluble polymers” by Yale L. Meltzer, NOYES-Verl., 1981, the disclosure of which is hereby incorporated by reference in its entirety).
- cellulose ethers such as HEC (hydroxyethyl cellulose) or starch ether
- synthetic polymers with similar properties for example PVA or end-capped PEG (for example C-is-EO ; see also the book "Water-soluble polymers” by Yale L. Meltzer, NOYES-Verl., 1981, the disclosure of which is hereby incorporated by reference in its entirety).
- the concentrate is metered — optionally after coating the enzyme — to a suitably previously prepared dry, powdery to granular mixture of the additives described above.
- the water content of the mixture taking into account the reduced water content of the concentrate according to the invention - should be chosen such that it can be converted into granular particles which are not adhesive at room temperature when processed with stirring and striking tools and plastically deformed and extruded when using higher pressure.
- the free-flowing premix is then processed in a known manner in principle in a kneader and a connected extruder to give a plastic mass which is as homogeneous as possible, the result of the mechanical processing being that the mass is at temperatures between 15 and 80 ° C., in particular 40 ° C.
- an extrusion temperature of below 50 ° C. and an extrusion pressure in the range from 30 to 130 bar, in particular in the range from 50 to, are advantageous 90 bar.
- the material leaving the extruder is passed through a perforated disc with a subsequent knock-off knife and is thereby crushed into cylindrical particles of a defined size.
- the diameter of the bores in the perforated disk is expediently 0.7 mm to 1.2 mm, preferably 0.8 mm to 1.0 mm.
- the particles which are usually still moist, can then be dried and coated in a coating system (see below). It has proven advantageous to spheronize the cylindrical particles leaving the extruder and chopper before coating, that is to round them off and deburr them in suitable devices.
- a device which consists of a cylindrical container with stationary, fixed side walls and a friction plate rotatably mounted on the bottom. Devices of this type are widely used in technology under the Marumerizer® name and are described, for example, in DE 2137042 and DE 2137043.
- any dusty particles with a grain size of less than 0.1 mm, in particular less than 0.4 mm and any coarse particles with a grain size of more than 2 mm, in particular more than 1.6 mm can then be removed by sieving or air separation and, if necessary, returned to the manufacturing process.
- the beads are continuously or batchwise, preferably using a fluidized bed drying unit, at supply air temperatures of preferably 35 ° C. to 70 ° C. and in particular at a product temperature of not more than 42 ° C. to the desired residual moisture content of, for example, 2% by weight 10% by weight, in particular 3% by weight to 8% by weight, based on the total granules, dried if they had previously higher water contents.
- these mixtures in particular can result in advantageous physical properties, in particular as regards the achievement of a viscosity which is favorable for further processing.
- the surfactant being a nonionic, anionic or amphoteric surfactant or a mixture thereof, in particular alkoxylated, advantageously ethoxylated, in particular primary alcohols having preferably 8 to 18 carbon atoms and an average of 1 to 12 Moles of ethylene oxide (EO) per mole of alcohol, to alkyl polyglycosides (APG), amine oxides, polyhydroxy fatty acid amides, sulfonates, sulfates, fatty acid glycerol esters, alkali and especially the sodium salts of sulfuric acid semiesters of C 2 -C 18 fatty alcohols, to sulfuric acid monoesters with 1 to 6 moles Ethylene oxide ethoxylated straight-chain, branched C 7-2 alcohols, to saturated fatty acid soaps or to mixtures thereof.
- EO ethylene oxide
- APG alkyl polyglycosides
- amine oxides polyhydroxy fatty acid amides
- sulfonates
- Particularly preferred processes according to the invention are characterized in that the granulate particles obtained according to the previous description are coated in a subsequent process step.
- a final, single or multiple coating (coating) is therefore very particularly preferably carried out.
- the granulate particles preferably enzyme particles
- the coating material is sprayed on using a top sprayer. This is done under drying conditions, that is 40-45 ° C, so that the product has about 35-38 ° C and remains dry.
- Preferred processes of this type are characterized in that the granulate particles, in particular enzyme granulate particles, are coated with an aqueous emulsion based on silicone oil.
- the teaching of DE 10108459 A1 can also be applied to this embodiment, according to which the foam regulator active ingredient applied can also be based on paraffin wax. It can be advantageous here to use the polymer in the form of an aqueous solution, for example as an aqueous PEG solution.
- the coating can also use surfactant, for example nonionic surfactant with approximately 80 EO.
- a pigment-containing coating of: (a) 5 to 70 wt .-% (based on the
- a coating containing a polyvalent metal salt of an unbranched or branched, unsaturated or saturated, mono- or poly-hydroxylated fatty acid with at least 12 carbon atoms is applied; such a coating emerges from WO 03/020868 A1;
- the present invention further provides solid, optionally coated granules with improved storage stability and abrasion resistance, which are obtainable by the processes according to the invention described above.
- each is a solid granulate with improved storage stability and abrasion resistance, which is characterized in that the granulate particles contain hygroscopic polyols.
- these hygroscopic polyols can be found, in particular, in the matrix according to the invention, since they are obtained by mixing with the active ingredient concentrate to be packaged or by incorporation into the premix to be granulated (premix). According to this, the majority of the hygroscopic polyols added in the matrix should also be present in the granules according to the invention remain and if at all then only a small proportion diffuse into the (optional) protective layer. The same applies analogously to the other optional components that are added to the concentrate or the premix to be granulated (premix) (see below).
- ⁇ such a granulate which, at the same time, is an extrudate with respect to its matrix, that is to say was originally obtained by extrusion and has the material properties attributable to it (see above);
- a granulate which is optionally additionally characterized in that the hygroscopic polyols are selected from: ethylene glycol, propylene glycol, triethylene glycol, glycerol, monoglycerides, diglycerides, polyethylene glycols (PEG), polypropylene glycols (PPG), polyvinyl alcohols (PVA), polysaccharides, cellulose , Alginates, modified starches and their hydrolyzates, the polymers and copolymers of these compounds or their copolymers with other polymers which are selected from polyethylene oxides, polyvinylpyrrolidones (PVP) and gelatin, in particular selected from: glycerol, cellulose,
- PVP polyvinylpyrrolidones
- Such a granulate which is optionally additionally characterized in that it contains enzymes, such as proteases, lipases, amylases, which are obtained from the microorganisms in particular in the matrix, Contains mannanases and / or cellulases, preferably proteases produced by or derived from beta / s species, alone or in combination with other enzymes.
- enzymes such as proteases, lipases, amylases, which are obtained from the microorganisms in particular in the matrix, Contains mannanases and / or cellulases, preferably proteases produced by or derived from beta / s species, alone or in combination with other enzymes.
- Such a granulate which is optionally additionally characterized in that it contains, in particular in the matrix, enzymes mixed with a substance with surface-active properties (surfactant);
- the surfactant being a nonionic, anionic or amphoteric surfactant or a mixture thereof, in particular alkoxylated, advantageously ethoxylated, in particular primary alcohols with preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, to alkyl polyglycosides (APG), amine oxides, polyhydroxy fatty acid amides, sulfonates, sulfates, fatty acid glycerol esters, alkali and especially the sodium salts of the sulfuric acid half-esters of C 12 -C 18 fatty alcohols, to sulfuric acid monoesters with 1 to 6 Moles of ethylene oxide ethoxylated straight-chain, branched C 7-21 alcohols, to saturated fatty acid soaps or to mixtures thereof;
- the surfactant being a nonionic, anionic or amphoteric surfactant or a mixture thereof, in particular alkoxylated, advantageously eth
- a granulate according to the invention which is optionally characterized in addition to the features listed so far in that the granulate particles are coated;
- granules are preferred, which are characterized in that the granulated particles, especially enzyme granulate particles are coated with an aqueous emulsion based on silicone oil;
- granules which are characterized in that the granulate particles, in particular enzyme granulate particles, are coated with an inorganic pigment and polymer-containing layer are also less preferred.
- pigment / polymer coated granules are those preferably having PEG, PVA, PVP, starch, starch derivative, cellulose, cellulose derivative or mixtures thereof or copolymers as polymer and kaolin, TiO 2 and / or antioxidants as an inorganic pigment;
- granules are the following granules according to the invention: (1.) those with a pigment-containing coating composed of: (a) 5 to 70% by weight (based on the coating) of fine, inorganic, water-insoluble pigment, (b) 45 to 90 % By weight of an organic substance with a Melting point of 40 to 70 ° C and (c) to 20 wt .-% of a pourability-improving agent, (2.) those with a coating containing a polyvalent metal salt of an unbranched or branched, unsaturated or saturated, mono- or poly-hydroxylated fatty acid at least 12 carbon atoms, (3.) those with a coating comprising a mixture of TiO2, urea and polyethylene glucol with a water content of less than 50% by weight, or (4.) those with a coating comprising an emulsion, the selected is under: Water-in-oil emulsions (W / O), oil-in-water emulsions (O / W), multiple
- the granules contain organic chemical compounds such as proteins, in particular enzymes, polysaccharides or non-biological polymers, polyethylene glycols, natural or synthetic fats, long-chain fatty acids, long-chain fatty alcohols, biopolymers (e.g. xanthan), paraffins or long-chain nonionic surfactants individually, incorporated in the mixture and / or in carrier substances.
- Long-chain in the sense of this invention are those compounds which, because of the alkyl radical, have a softening point above 20 ° C., preferably even above 25 ° C.
- proteases include in particular proteases, amylases, lipases, hemicellulases, cellulases or oxidoreductases, and preferably their mixtures.
- these enzymes are of natural origin; Based on the natural molecules, improved variants are available for use in detergents and cleaning agents, which are accordingly preferred.
- proteases those of the subtilisin type are preferred.
- subtilisins BPN 'and Carlsberg examples of these are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the enzymes theritase, proteinase K and no longer assigned to the subtilisins in the narrower sense the proteases TW3 and TW7.
- Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase ® from Novozymes A / S, Bagsvasrd, Denmark.
- the subtilisins 147 and 309 are sold under the trade names Esperase ®, or Savinase ® from Novozymes.
- protease from Bacillus lentus DSM 5483 (WO 91/02792 A1) is derived from the variants listed under the name BLAP ® , which are described in particular in WO 92/21760 A1, WO 95/23221 A1, WO 02/088340 A2 and WO 03 / 038082 A2.
- Other usable proteases from various Bacillus sp. and B. gibsonii emerge from the patent applications WO 03/054185 A1, WO 03/056017 A2, WO 03/055974 A2 and WO 03/054184 A1.
- proteases are, for example, under the trade names Durazym ®, relase ®, Everlase® ®, Nafizym, Natalase ®, Kannase® ® and Ovozymes ® from Novozymes, under the trade names Purafect ®, Purafect ® OxP and Properase.RTM ® by the company Genencor, which is sold under the trade name Protosol ® by Advanced Biochemicals Ltd., Thane, India, which is sold under the trade name Wuxi ® by Wuxi Snyder Bioproducts Ltd., China, and in the trade name Proleather ® and Protease P ® by the company Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
- amylases which can be used according to the invention are the ⁇ -amylases from Bacillus licheniformis, from B. amyloliquefaciens or from ⁇ . stearothermophilus and its further developments for use in detergents and cleaning agents.
- the enzyme from ß. licheniformis is available from Novozymes under the name Termamyl ® and from Genencor under the name Purastar ® ST.
- Development products of this ⁇ -amylase are available from Novozymes under the trade names Duramyl ® and Termamyl ® ultra, from Genencor under the name Purastar® ® OxAm and from Daiwa Seiko Inc., Tokyo, Japan, as Keistase ®.
- amyloliquefaciens ⁇ -amylase is supplied by the company Novozymes sold under the name BAN ® , and derived variants of the ⁇ -amylase from ß. stearothermophilus under the names BSG ® and Novamyl ® , also from Novozymes.
- ⁇ -amylase from Bacillus sp. Disclosed in the application WO 02/10356 A2.
- CCTase cyclodextrin glucanotransferase
- amylolytic enzymes which belong to the sequence space of ⁇ -amylases, which is defined in the application WO 03/002711 A2, and those which are described in the application WO 03/054177 A2. Fusion products of the molecules mentioned can also be used, for example those from the application DE 10138753 A1.
- Granules according to the invention can contain lipases or cutinases, in particular because of their triglyceride-cleaving activities, but also in order to generate peracids in situ from suitable precursors.
- lipases or cutinases include, for example, the lipases originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, in particular those with the amino acid exchange D96L. They are sold, for example, by Novozymes under the trade names Lipolase ® , Lipolase ® Ultra, LipoPrime ® , Lipozy e ® and Lipex ® .
- the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens.
- useable lipases are available from Amano under the designations Lipase CE ®, Lipase P ®, Lipase B ®, or lipase CES ®, Lipase AKG ®, Bacillis sp.
- Lipase ® , Lipase AP ® , Lipase M-AP ® and Lipase AML ® available.
- the Genencor company can use the lipases or cutinases whose starting enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii.
- Granules according to the invention can contain cellulases, depending on the purpose, as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously complement one another with regard to their various performance aspects.
- These performance aspects include, in particular, contributions to the primary washing performance, to the secondary washing performance of the agent (anti-deposition effect or graying inhibition) and finish (tissue effect), up to the exertion of a “stone washed” effect.
- EG endoglucanase
- Novozymes A useful fungal, endoglucanase (EG) -rich cellulase preparation or its further developments are offered by the Novozymes company under the trade name Celluzyme ® .
- the products Endolase ® and Carezyme ® also available from Novozymes, are based on the 50 kD-EG and the 43 kD-EG from H. insolens DSM 1800.
- Other usable commercial products from this company are Cellusoft ® and Renozyme ® . The latter is based on the application WO 96/29397 A1.
- Performance-improved cellulase variants can be found, for example, in the application WO 98/12307 A1.
- the cellulases disclosed in application WO 97/14804 A1 can also be used; For example, it revealed 20 kD EG Melanocarpus, available from AB Enzymes, Finland, under the trade names Ecostone® ® and Biotouch ®. Other commercial products from AB Enzymes are Econase ® and Ecopulp ® . Other suitable cellulases from Bacillus sp. CBS 670.93 and CBS 669.93 are disclosed in WO 96/34092 A2, the ones from Bacillus sp. CBS is available from Genencor under the trade name Puradax® ® 670.93. Other commercial products from Genencor are "Genencor detergent cellulase L" and IndiAge ® Neutra.
- Granules according to the invention for use in detergents and cleaning agents can contain further enzymes, in particular for removing certain problem soils, which are summarized under the term hemicellulases.
- Suitable mannanases for example, under the name Gamanase ® and Pektinex AR ® from Novozymes, under the name Rohapec ® B1 from AB Enzymes, under the name Pyrolase® ® from Diversa Corp., San Diego, CA, USA, and under the name Purabrite ® from Genencor Int., Inc., Palo Alto, CA, USA.
- a suitable ß-glucanase from a ß. alcalophilus can be found, for example, in application WO 99/06573 A1.
- the from ß. subtilis .beta.-glucanase obtained is available under the name Cereflo ® from Novozymes.
- granules according to the invention can be used, in particular for detergents and cleaning agents, to oxidoreductases, for example oxidases, oxygenases, catalases, peroxidases such as halo-, chloro-, bromo-, lignin, glucose or manganese peroxidases, dioxygenases or laccases (phenol oxidases , Polyphenol oxidases).
- oxidoreductases for example oxidases, oxygenases, catalases, peroxidases such as halo-, chloro-, bromo-, lignin, glucose or manganese peroxidases, dioxygenases or laccases (phenol oxidases , Polyphenol oxidases).
- Suitable commercial products are Denilite ® 1 and 2 from Novozymes.
- organic, particularly preferably aromatic, compounds interacting with the enzymes are additionally added in order to increase the activity of the oxidoreductases in question (enhancers) or to ensure the flow of electrons (mediators) in the case of greatly different redox potentials between the oxidizing enzymes and the soiling.
- the enzymes used in the granules according to the invention either originate from microorganisms, for example the genera Bacillus, Streptomyces, Humicola, or Pseudomonas, and / or are produced by biotechnological processes known per se by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or filamentous fungi.
- the enzymes in question are advantageously purified by methods which are in themselves established, for example by means of precipitation, sedimentation, concentration, filtration of the liquid phases, microfiltration, ultrafiltration, exposure to chemicals, deodorization or suitable combinations of these steps.
- Enzymes are preferably contained in the granules according to the invention in amounts of 4% by weight to 20% by weight. If the enzyme granulate according to the invention is a protease-containing formulation, the protease activity is preferably 150,000 to 550,000 HPE (see above), in particular 160,000 to 300,000 HPE per gram of enzyme granulate. In the case of an amylase formulation, the amylase activity is preferably 7,500 to 27,500 TAU (see above), in particular 8,000 to 15,000 TAU, per gram of enzyme granules.
- the granulate particles obtained preferably enzyme particles, have an average size of 0.85 mm.
- the outer layer is advantageously about 7 to 30 microns thick.
- the granules obtained by the process according to the invention consist of largely rounded, uniformly coated and dust-free particles which generally have a bulk density of approximately 500 to 800 grams per liter, in particular 600 to 720 grams per liter.
- the granules according to the invention are notable for very high storage stability, in particular at temperatures above room temperature and high atmospheric humidity, and for rapid and practically complete dissolution behavior in water.
- the granules according to the invention preferably release 100% of their enzyme activity in water at 25 ° C. within 3 minutes, in particular within 90 seconds to 2 minutes.
- the granules described here can be added in accordance with suitable agents.
- suitable agents According to the invention, the focus here is on detergents and cleaning agents.
- a further subject of the invention are detergents and / or cleaning agents which contain the granules according to the invention described above.
- This subject of the invention includes all conceivable types of cleaning agent, both concentrates and agents to be used undiluted, for use on a commercial scale, in the washing machine or for hand washing or cleaning.
- cleaning agent include, for example, detergents for textiles, carpets or natural fibers, for which the term detergent is used according to the present invention.
- Embodiments of the present invention include all administration forms established according to the prior art and / or all expedient administration forms of the washing or cleaning agents according to the invention. These include, in particular, solid, powdery agents, optionally also of several phases, compressed or uncompressed; it also includes, for example: extrudates, granules, tablets or pouches, both in large containers and packaged in portions.
- a washing or cleaning agent optionally contains further ingredients such as enzyme stabilizers (see above), surfactants, e.g. B. non-ionic, anionic and / or amphoteric surfactants, and / or bleaching agents, and / or builders, and optionally other conventional ingredients, among which the following may be mentioned in particular: (other) enzymes, in particular the sequestering agents, electrolytes already listed above, optical brighteners, graying inhibitors, silver corrosion inhibitors, color transfer inhibitors, foam inhibitors, abrasives, dyes and / or fragrances, and also microbial agents and / or UV absorbers.
- enzyme stabilizers see above
- surfactants e.g. B. non-ionic, anionic and / or amphoteric surfactants, and / or bleaching agents, and / or builders
- other conventional ingredients among which the following may be mentioned in particular: (other) enzymes, in particular the sequestering agents, electrolytes already listed above, optical brighteners, graying inhibitor
- the use of the granules according to the invention described as an admixture component in detergents or cleaning agents is a further subject of the present invention.
- the enzyme granulate according to the invention or produced by the method according to the invention is preferably used for the production of solid, in particular particulate washing or cleaning agents which can be obtained by simply mixing the enzyme granules with other powder components customary in such agents.
- the enzyme granules preferably have average grain sizes in the range from 0.7 to 1.2 mm.
- the granules according to the invention preferably contain less than 2% by weight, in particular at most 1.4% by weight, of particles with particle sizes outside the range from 0.4 to 1.6 mm.
- the process is not restricted to these particle sizes, but rather covers a wide range of grain sizes corresponding to the field of application, usually the average particle diameter (d 50 ) is between 0.1 and more than 2 mm.
- Enzyme concentrate 23%, stabilizer 1%, glycerin 5%, cellulose 1%, sugar 1%, wheat starch 4%, wheat flour 25%, PEG 4000 3%, maize starch 37% are mixed in the Lödige mixer for 90 s.
- Granule activity 260,000 HPE / g (discontinued)
- Bulk weight 620 g / l
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Abstract
Description
Claims
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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DE102004021384A DE102004021384A1 (de) | 2004-04-30 | 2004-04-30 | Verfahren zur Herstellung von Granulaten mit verbesserter Lagerstabilität und Abriebfestigkeit |
PCT/EP2005/004202 WO2005108539A1 (de) | 2004-04-30 | 2005-04-20 | Verfahren zur herstellung von festen granulaten mit verbesserter lagerstabilität und abriebfestigkeit |
Publications (1)
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EP1740684A1 true EP1740684A1 (de) | 2007-01-10 |
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Application Number | Title | Priority Date | Filing Date |
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EP05740613A Withdrawn EP1740684A1 (de) | 2004-04-30 | 2005-04-20 | Verfahren zur herstellung von festen granulaten mit verbesserter lagerstabilität und abriebfestigkeit |
Country Status (6)
Country | Link |
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US (1) | US20070111920A1 (de) |
EP (1) | EP1740684A1 (de) |
JP (1) | JP2007535597A (de) |
CN (1) | CN1984985A (de) |
DE (1) | DE102004021384A1 (de) |
WO (1) | WO2005108539A1 (de) |
Families Citing this family (43)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE102004047777B4 (de) | 2004-10-01 | 2018-05-09 | Basf Se | Alpha-Amylase-Varianten mit erhöhter Lösungsmittelstabilität, Verfahren zu deren Herstellung sowie deren Verwendung |
DE102004047776B4 (de) | 2004-10-01 | 2018-05-09 | Basf Se | Gegen Di- und/oder Multimerisierung stabilisierte Alpha-Amylase-Varianten, Verfahren zu deren Herstellung sowie deren Verwendung |
DE102004063801A1 (de) * | 2004-12-30 | 2006-07-13 | Henkel Kgaa | Verfahren zur Herstellung von Farbschutzwirkstoff-Granulaten |
NO20073834L (no) | 2006-07-21 | 2008-01-22 | Akzo Nobel Chemicals Int Bv | Sulfonerte podede kopolymerer |
DE102007029643A1 (de) | 2006-09-08 | 2009-01-15 | Henkel Ag & Co. Kgaa | Reinigungsmittel |
US20100323945A1 (en) * | 2007-01-11 | 2010-12-23 | Novozymes A/S | Particles Comprising Active Compounds |
DE102007039655A1 (de) * | 2007-08-22 | 2009-02-26 | Henkel Ag & Co. Kgaa | Reinigungsmittel |
WO2009030728A2 (en) * | 2007-09-05 | 2009-03-12 | Novozymes A/S | Enzyme compositions with stabilizing constituent |
US20110302722A1 (en) * | 2008-12-24 | 2011-12-15 | Danisco Us Inc. | Laccases and methods of use thereof at low temperature |
EP2421949B1 (de) | 2009-04-24 | 2014-03-19 | Unilever PLC | Herstellung von hochwaschaktiven detergenspartikeln |
AU2010278786B2 (en) | 2009-07-31 | 2014-04-10 | Akzo Nobel Chemicals International B.V. | Hybrid copolymer compositions |
WO2011131585A1 (en) | 2010-04-20 | 2011-10-27 | Henkel Ag & Co. Kgaa | Laundry article having cleaning properties |
KR101380836B1 (ko) * | 2011-01-18 | 2014-04-09 | 한국기계연구원 | 상온진공과립분사 공정을 위한 취성재료 과립 및 이를 이용한 코팅층의 형성방법 |
DE102011007627A1 (de) | 2011-04-18 | 2012-10-18 | Henkel Ag & Co. Kgaa | Wasch- oder Reinigungsmittel mit fester Enzymkonfektionierung |
US8841246B2 (en) | 2011-08-05 | 2014-09-23 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide hybrid polymer composition and methods of improving drainage |
US8853144B2 (en) | 2011-08-05 | 2014-10-07 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide graft polymer composition and methods of improving drainage |
US8679366B2 (en) | 2011-08-05 | 2014-03-25 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide graft polymer composition and methods of controlling hard water scale |
US8636918B2 (en) | 2011-08-05 | 2014-01-28 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide hybrid polymer composition and methods of controlling hard water scale |
EP2773321B1 (de) | 2011-11-04 | 2015-09-09 | Akzo Nobel Chemicals International B.V. | Dendrit-pfropfcopolymere und verfahren zu ihrer herstellung |
EP2773320B1 (de) | 2011-11-04 | 2016-02-03 | Akzo Nobel Chemicals International B.V. | Hybriddendrit-copolymere, zusammensetzungen daraus und verfahren zu ihrer herstellung |
US9856606B2 (en) | 2011-12-12 | 2018-01-02 | Enzymatic Deinking Technologies, L.L.C. | Enzymatic pre-treatment of market pulp to improve fiber drainage and physical properties |
CN103525797B (zh) * | 2012-07-03 | 2016-04-13 | 深圳市绿微康生物工程有限公司 | 液体脂肪酶保护剂及其制备方法和应用 |
US8945314B2 (en) | 2012-07-30 | 2015-02-03 | Ecolab Usa Inc. | Biodegradable stability binding agent for a solid detergent |
FI127111B (en) | 2012-08-20 | 2017-11-15 | Stora Enso Oyj | Process and intermediate for the production of highly refined or microfibrillated cellulose |
CN104561124A (zh) * | 2013-10-15 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 磷酸二甘油酯用于提高酒精产量 |
CN104561107A (zh) * | 2013-10-16 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 甘露糖基甘油酸用于提高沼气产量 |
CN104562822A (zh) * | 2013-10-16 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 一种木聚糖酶稳定剂在造纸工艺中的应用 |
CN104560932A (zh) * | 2013-10-16 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 一种常温下酶蛋白保护剂 |
CN104562842A (zh) * | 2013-10-16 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 一种造纸工艺中木聚糖酶的稳定剂 |
CN104543378A (zh) * | 2013-10-16 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 一种植酸酶稳定剂在饲料加工中的应用 |
CN104561108A (zh) * | 2013-10-16 | 2015-04-29 | 镇江拜因诺生物科技有限公司 | 一种提高沼气产量的增效剂 |
US10619298B2 (en) | 2013-11-18 | 2020-04-14 | Enzymatic Deinking Technologies, L.L.C. | Enzymatic treatment of virgin fiber and recycled paper to reduce residual mineral oil levels for paper production |
US10367827B2 (en) * | 2013-12-19 | 2019-07-30 | Splunk Inc. | Using network locations obtained from multiple threat lists to evaluate network data or machine data |
US9365805B2 (en) | 2014-05-15 | 2016-06-14 | Ecolab Usa Inc. | Bio-based pot and pan pre-soak |
KR101617379B1 (ko) | 2015-05-13 | 2016-05-02 | 주식회사 삼양사 | 혼합당 과립 분말 및 이의 제조방법 |
DE102015217816A1 (de) | 2015-09-17 | 2017-03-23 | Henkel Ag & Co. Kgaa | Verwendung hochkonzentrierter Enzymgranulate zur Erhöhung der Lagerstabilität von Enzymen |
EP3697881A1 (de) * | 2017-10-16 | 2020-08-26 | Novozymes A/S | Staubarme granulate |
MX2020007846A (es) | 2018-01-26 | 2020-09-25 | Ecolab Usa Inc | Solidificacion de tensioactivos de oxido de amina, betaina y/o sultaina liquidos con un portador. |
EP3743493B1 (de) | 2018-01-26 | 2024-07-17 | Ecolab Usa Inc. | Verfestigende flüssige anionische tenside |
US11655436B2 (en) | 2018-01-26 | 2023-05-23 | Ecolab Usa Inc. | Solidifying liquid amine oxide, betaine, and/or sultaine surfactants with a binder and optional carrier |
TWI662961B (zh) * | 2018-03-16 | 2019-06-21 | 共生地球生物科技有限公司 | 多重pH緩衝配方與胃蛋白酶和胰蛋白酶的共同蛋白質水解效率增益劑之緩衝組合物及其用途 |
AU2020225930A1 (en) * | 2019-02-20 | 2021-08-12 | Suntory Holdings Limited | Milk protein-containing granular composition, method for producing same, and method for improving dispersion properties of milk protein-containing granular composition |
CN111893008B (zh) * | 2020-08-10 | 2022-09-20 | 纳爱斯集团有限公司 | 一种洗涤制剂及其制备方法 |
Family Cites Families (44)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3853780A (en) * | 1969-10-06 | 1974-12-10 | Colgate Palmolive Co | Granular non-dusting enzyme product for detergent use |
DE2030531A1 (de) * | 1970-06-20 | 1971-12-30 | Kali-Chemie Ag, 3000 Hannover | Abriebfestes Enzymgranulat mit niedrigem Schüttgewicht |
FR2168988A1 (en) * | 1972-01-28 | 1973-09-07 | Mayer & Co Inc O | Stable particulate pepsin mixts - for bulk prodn |
GB1603640A (en) * | 1977-07-20 | 1981-11-25 | Gist Brocades Nv | Enzyme particles |
DE3120744A1 (de) * | 1981-05-25 | 1982-12-09 | Joh. A. Benckiser Gmbh, 6700 Ludwigshafen | Abriebfestes granulat auf basis alkalialuminiumsilikat mit guter dispergierbarkeit in waessriger flotte |
DE3515650A1 (de) * | 1985-05-02 | 1986-11-06 | Biochemie GmbH, Kundl, Tirol | Verfahren zur abtrennung von biotechnologisch hergestellten wertstoffen durch querstrom-mikrofiltration |
US4846001A (en) * | 1987-09-11 | 1989-07-11 | Sps Technologies, Inc. | Ultrasonic load indicating member |
US5131276A (en) * | 1990-08-27 | 1992-07-21 | Ultrafast, Inc. | Ultrasonic load indicating member with transducer |
US5879920A (en) * | 1991-10-07 | 1999-03-09 | Genencor International, Inc. | Coated enzyme-containing granule |
US5807048A (en) * | 1992-09-03 | 1998-09-15 | European Atomic Energy Community (Euratom) | Sealing fastener with ultrasonic identifier and removal attempt indicator, and ultrasonic reading device for same |
FR2696215B1 (fr) * | 1992-09-25 | 1994-12-02 | Serge Bras | Elément d'assemblage et procédé et machine d'assemblage. |
US5242253A (en) * | 1992-10-08 | 1993-09-07 | Semblex Corporation | Thread-forming screw |
DE4322229A1 (de) * | 1993-07-05 | 1995-01-12 | Cognis Bio Umwelt | Umhüllte Enzymzubereitung für Wasch- und Reinigungsmittel |
DE4329463A1 (de) * | 1993-09-01 | 1995-03-02 | Cognis Bio Umwelt | Mehrenzymgranulate |
DE4422433A1 (de) * | 1994-06-28 | 1996-01-04 | Cognis Bio Umwelt | Mehrenzymgranulat |
CA2164187C (en) * | 1994-12-27 | 2000-02-01 | Mohan L. Sanduja | Protective coating on steel parts |
US5858952A (en) * | 1995-12-22 | 1999-01-12 | Kao Corporation | Enzyme-containing granulated product method of preparation and compositions containing the granulated product |
US6204236B1 (en) * | 1996-06-01 | 2001-03-20 | Genencor International, Inc. | Enzyme granulates comprising an enzyme and an organic disulfide core |
DE19651446A1 (de) * | 1996-12-11 | 1998-06-18 | Henkel Kgaa | Umhüllte Enzymzubereitung mit verbesserter Löslichkeit |
US5827813A (en) * | 1997-02-28 | 1998-10-27 | Procter & Gamble Company | Detergent compositions having color care agents |
DE19732751A1 (de) * | 1997-07-30 | 1999-02-04 | Henkel Kgaa | Neue Beta-Glucanase aus Bacillus |
GB9717723D0 (en) * | 1997-08-21 | 1997-10-29 | Ici Plc | Synthetic detergent formulations |
BR9914674A (pt) * | 1998-10-27 | 2001-07-17 | Genencor Int | Grânulo matriz |
ES2355123T3 (es) * | 1998-11-13 | 2011-03-23 | Danisco Us Inc. | Gránulo de baja densidad en lecho fluidizado. |
ES2220437T3 (es) * | 1999-02-10 | 2004-12-16 | Basf Aktiengesellschaft | Granulados que contienen enzimas para piensos. |
DE19917222A1 (de) * | 1999-04-16 | 2000-11-02 | Schrauben Betzer Gmbh & Co Kg | Schraube sowie Vorrichtung zur Handhabung einer derartigen Schraube |
US6706773B1 (en) * | 1999-10-05 | 2004-03-16 | The Procter & Gamble Company | Process for preparing a foam component |
ATE307882T1 (de) * | 2000-07-28 | 2005-11-15 | Henkel Kgaa | Neues amylolytisches enzym aus bacillus sp. a 7-7 (dsm 12368) sowie wasch- und reinigungsmittel mit diesem neuen amylolytischen enzym |
ATE373716T1 (de) * | 2000-11-28 | 2007-10-15 | Henkel Kgaa | Cyclodextrin -glucanotransferase(cg tase) aus bacillus agaradherens(dsm 9948)sowie wasch-und reinigungsmittel mit dieser neuen cyclodextrin- glucanotransferase |
DE10108459A1 (de) * | 2001-02-22 | 2002-09-12 | Henkel Kgaa | Schaumregulatorgranulat |
GB2374082A (en) * | 2001-04-04 | 2002-10-09 | Procter & Gamble | Particles for a detergent product |
DE10121463A1 (de) * | 2001-05-02 | 2003-02-27 | Henkel Kgaa | Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten |
DE10131441A1 (de) * | 2001-06-29 | 2003-01-30 | Henkel Kgaa | Eine neue Gruppe von alpha-Amylasen sowie ein Verfahren zur Identifizierung und Gewinnung neuer alpha-Amylasen |
DE10138753B4 (de) * | 2001-08-07 | 2017-07-20 | Henkel Ag & Co. Kgaa | Wasch- und Reinigungsmittel mit Hybrid-Alpha-Amylasen |
DE10142124A1 (de) * | 2001-08-30 | 2003-03-27 | Henkel Kgaa | Umhüllte Wirkstoffzubereitung für den Einsatz in teilchenförmigen Wasch- und Reinigungsmitteln |
DE10153792A1 (de) * | 2001-10-31 | 2003-05-22 | Henkel Kgaa | Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten |
US6671185B2 (en) * | 2001-11-28 | 2003-12-30 | Landon Duval | Intelligent fasteners |
DE10162728A1 (de) * | 2001-12-20 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus gibsonii (DSM 14393) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease |
DE10162727A1 (de) * | 2001-12-20 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus gibsonii (DSM 14391) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease |
DE10163748A1 (de) * | 2001-12-21 | 2003-07-17 | Henkel Kgaa | Neue Glykosylhydrolasen |
DE10163883A1 (de) * | 2001-12-22 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus sp. (DSM 14390) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease |
DE10163884A1 (de) * | 2001-12-22 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease |
US7425528B2 (en) * | 2002-07-01 | 2008-09-16 | Novozymes A/S | Stabilization of granules |
EP1413202A1 (de) * | 2002-10-22 | 2004-04-28 | CSM Nederland B.V. | Fett-verkapselte funktionnelle Backzusätze |
-
2004
- 2004-04-30 DE DE102004021384A patent/DE102004021384A1/de not_active Withdrawn
-
2005
- 2005-04-20 JP JP2007509927A patent/JP2007535597A/ja active Pending
- 2005-04-20 CN CNA200580013497XA patent/CN1984985A/zh active Pending
- 2005-04-20 WO PCT/EP2005/004202 patent/WO2005108539A1/de not_active Application Discontinuation
- 2005-04-20 EP EP05740613A patent/EP1740684A1/de not_active Withdrawn
-
2006
- 2006-10-30 US US11/589,561 patent/US20070111920A1/en not_active Abandoned
Non-Patent Citations (1)
Title |
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See references of WO2005108539A1 * |
Also Published As
Publication number | Publication date |
---|---|
WO2005108539A1 (de) | 2005-11-17 |
US20070111920A1 (en) | 2007-05-17 |
CN1984985A (zh) | 2007-06-20 |
JP2007535597A (ja) | 2007-12-06 |
DE102004021384A1 (de) | 2005-11-24 |
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