JP2016528881A - Granules with small smooth core - Google Patents

Abstract

The present teachings provide an improved granule population that includes small smooth core particles. Methods of manufacture and use are also provided.

Description

(Cross-reference of related applications)
This application claims the benefit of priority of US Provisional Application No. 61 / 837,122, filed Jun. 19, 2013, which is hereby incorporated by reference in its entirety.

(Field of Invention)
The present disclosure is directed to granule masses containing improved active substances, as well as methods of manufacture and use.

  The use of active substances such as enzymes in dry product formulations in industrial and consumer applications such as detergents, textile compositions, oven cooking, food and animal feed has become a common practice . Enzymes break down stains, change the color and texture of fabrics, change the viscosity of doughs and foods, and improve the utilization of nutrients such as soluble phosphates, food and animal feed It is known to improve the productivity of animals by improving the digestibility of food and animal feed by lowering antinutritive factors such as phytic acid therein.

  Enzyme inactivation can occur in dry product formulations such as powdered laundry and dishwashing detergents, fiber treatment formulations, baking flours, grains (such as corn or soy), vitamins, During storage of animal feeds composed of ingredients such as mineral nutrients such as choline chloride, and additionally, high temperatures, steam or humidity, compression or shear stress, and chemicals (acids, bases, surfactants, bleaches) May occur during industrial processing (such as steam pelleting of animal feed) by exposure to agents, or organic solvents. Inactivation is at least partly reversible after processing, for example if the enzyme reactivates upon cooling after steaming and pelletization, but inactivation is mostly irreversible and processing Subsequent cooling, for example after steaming and pelleting, does not completely restore the catalytic activity of the enzyme. In processes such as steam pelletization, irreversible inactivation and reduced activity of the enzyme are generally undesirable.

  Compared to dry feed mix, feed pellets have industry-favored properties such as improved feed quality, reduced pathogens, reduced dust during production, ease of handling, and more uniform dosing of ingredients . A preferred industrial pelletization process uses steam injection in a process known as conditioning to add moisture and temperature prior to the pelletization step, which feeds steam-heated feed ingredients, or conditioned meal, through a die. Raise. The temperature of the pelletization process may be about 70 ° C to 95 ° C or higher.

  Depending on the steam, temperature, compressive force and chemicals used in the pelletization process, the activity of the enzyme, i.e. the titer, is often significantly reduced during processing and subsequent storage. Indeed, feed enzymes are often offered for commercial use as stabilized liquid products that are sprayed onto the feed pellets after the pelletization process to avoid enzyme inactivation. However, for example, when the enzyme is applied after pelletization by spraying the enzyme onto the pellet, it is difficult to apply the enzyme uniformly, and the cost of the apparatus for adding the enzyme after pelletization is high. Alternatively, a liquid enzyme formulation or a dry mixed enzyme formulation may be added to the mixer prior to pelletization. In some cases, more enzyme may be added than is required in other cases to compensate for losses during pelleting.

  Supplied as in-product components and premix formulations that can be stored for up to months or years without loss of significant enzyme activity or subjected to industrial processing operations such as mixing or steaming pelletization processes There is a need in the detergent, fiber, oven cooking, food, and feed industries for stable and durable enzyme granules.

  Identify new enzyme sources (eg, identification of known enzymes in hyperthermophilic microorganisms), or work in an effort to avoid problems such as irreversible inactivation of enzymes or reduced enzyme activity during industrial processes Specific means for stabilizing the enzyme can be mentioned. In Klibanov, 1983 (Stabilization of Enzymes Against Thermal Inactivation, Advances in Applied Microbiology, volume 29, pages 1-28), (1) and (1) It is disclosed that there are three basic means, including the inclusion of agents. However, Klibanov (1983) further discloses that any of these methods can lead to stabilization or destabilization, or no effect at all. In this field, efforts to date by compounding have made some progress (for example, WO 97/23606, U.S. Pat. No. 9854980, U.S. Pat. No. 9739116, U.S. Pat. No. 2,070,4968, European Patent No. 12224273B1, Publication 2009/102770, US Pat. No. 6,602,841, European Patent Nos. 1804592B1, 0098631B1, and 1996028), the present teachings utilize an improved granule structure Provides further progress in overcoming some of these problems.

  In many cases, it is desirable to provide a solid formulation containing a high concentration of active enzyme in granular or particulate form. Granular granules are formulated with coatings, barrier coatings, and additives or excipients designed to provide enzyme protection against inactivation. To minimize the cost of these protective coatings, additives, and excipients, and to minimize the impact of product transportation costs, granule enzymes with the highest ratio of active enzyme to inactive ingredients as much as possible It is desirable to blend. However, if the granule particle size is kept constant as the enzyme concentration or loading is increased, the number of particles for a certain amount of enzyme added to the final product or application is reduced. However, if the number of particles per dose decreases too much, the variability between product administrations may increase. For example, if the average number of enzyme granules in a glass of detergent, fiber treatment blend, oven-cooked dough, or a single animal feed is small, the distribution of enzyme concentration between individual doses or feeds will be poor. Become uniform, which can lead to the effect of the enzyme treatment varying from one to another.

  In order to avoid the problem of variability due to lack of particles per time, and to realize the economic benefits due to the increase in enzyme load, in order to maintain a sufficient number of particles per time, enzyme granules It is possible to try to reduce the average particle size of. However, it is difficult to apply enzyme coatings and protective barrier coatings to smaller core particles during coating processes such as fluid bed spray coating, pan coating, drum coating, and the like. When the diameter of the core particles is small, especially less than about 250 micrometers, less than 200 micrometers, less than 175 micrometers, and less than 150 micrometers, the tendency of the particles to aggregate increases. Furthermore, applying a weight percentage of coating material to a smaller core results in a coating that is thin, thus resulting in a less protective coating. The challenge of applying a uniform coating to a small core is difficult, especially when the particle shape is irregular. Coating a core with pointed or angled corners and edges on the surface may result in thin or non-continuous areas of coating. Also, coatings applied to irregular coatings may result in agglomerates that do not adhere in the same way, or surface irregularities on nearby core particles, or surface ridges that are in contact with each other. . Complementing this by applying a thicker coating (when done without agglomeration) will tend to increase costs.

US Provisional Patent Application No. 61 / 837,122 International Publication No. 97/23606 International Publication No. 9854980 International Publication No. 9739116 International Publication No. 200704968 European Patent No. 12224273B1 International Publication No. 2009/102770 US Pat. No. 6,602,841 European Patent No. 1804592B1 European Patent No. 0098631B1 European Patent No. 1996028

Klibanov, 1983, (Stabilization of Enzymes Against Thermal Inactivation, Advances in Applied Microbiology, volume 29, page 1-28.

  Accordingly, there is a need for an improved method of applying an enzyme coating to a core while ensuring an effective continuous protective coating without causing significant agglomeration. When such a high quality coating on smaller particles is achieved, during processing and storage while providing a higher loading and maintaining sufficient homogeneity of the mixture so as not to increase variability between doses The stability of the enzyme will be improved.

  The object of the present invention is to ensure or improve the stability of the enzyme during storage alone, during industrial processing, or in a mixture with other ingredients, while at the same time providing a constant and minimal for the particles. In terms of the weight percentage of coating material applied to a continuous coating of thickness, i.e., the core, i.e. the enzyme-containing core, to improve the ability to apply a coating with a reduced number of thin defects.

  Surprisingly, it has been found that providing a smoother, more regular surface and a core with a narrow particle size distribution allows an improved coating with a constant and minimal thickness to be applied to smaller particles. It was. In some embodiments, the improved coated enzyme granules have a smoothness index of less than 2.5, a weight average average particle size of less than 300 micrometers, and a particle size dispersion index (PSDI) of less than 2.0. Starting from a core population, this is achieved by coating the enzyme-containing core with a further coating comprising a polymer consisting of at least 7% w / w of the final granule.

Fig. 4 illustrates an exemplary small smooth core particle according to the teachings of the present invention compared to another core particle that is small but irregular. 2 shows a portion of exemplary data in accordance with the teachings of the present invention. 2 shows a portion of exemplary data in accordance with the teachings of the present invention. Figure 3 is a graph showing the pelletization results of three representative granule batches. The black bar shows the activity of the meal, while the dark gray and light gray bars show the recovery rate at 90 ° C. and 95 ° C., respectively. Figure 2 is a graph showing the pelleting results of three representative phytase standard TPT batches. The black bar shows the activity of the meal, while the dark gray and light gray bars show the recovery rate at 90 ° C. and 95 ° C., respectively.

  In the practice of the present teachings, unless otherwise indicated, conventional techniques of molecular biology (including recombinant technology), microbiology, cell biology, biochemistry, granulation, and animal feed pelleting are included in the art. This method is used. Such techniques are described, for example, in Molecular Cloning: A Laboratory Manual, second edition (Sambrook et al., 1989), Oligonucleotide Synthesis (M. J. Gait, ed., 1984), Current Protocol. et al., eds., 1994), PCR: The Polymerase Chain Reaction (Mullis et al., eds., 1994), Gene Transfer and Expression: A Laboratory Manual (Kriegler, 1990), ogy for Bioproducts (Kadam, 1990), and, Fairfield, D. 1994. Chapter 10, Pelleting Cost Center. In Feed Manufacturing Technology IV. (McEllhiney, editor), American Feed Industry Association, Arlington, Va. , Pp. Fully described in documents such as 110-139.

  Unless defined otherwise herein, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this teaching belongs. Singleton, et al. , Dictionary of Microbiology and Molecular Biology, second ed. , John Wiley and Sons, New York (1994), and Hale & Markham, The Harper Collins Dictionary of Biology, Harper Perennial, NY (1991), including many terms used in the present invention. To provide. Any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present teachings.

  For ease of reference, elements of the present teachings are described under one or more headings. Note that the teachings under each heading also apply to the teachings under another heading. For example, each embodiment and aspect mentioned for use of the present teachings is equally an embodiment or aspect for the methods of the present teachings or compositions of the present teachings. Similarly, each embodiment and aspect mentioned for a method or use of the present teachings is equally an embodiment or aspect for a composition of the present teachings. In this application, the use of the singular includes the plural unless specifically stated otherwise.

  All patents, patent applications, publications, materials, and literature cited herein are hereby incorporated by reference in their entirety.

  Numerical ranges described herein include numerical values that define the range.

Definitions As used herein, the term “granule” contains a core (typically small smooth core particles), an active substance (typically an enzyme), and optionally at least one additional coating. Refers to particles.

  As used herein, the term “core” refers to the inner core of the granule and typically includes “small smooth core particles”. The core of the present teachings is rotary atomization, wet granulation, dry granulation, spray drying, disk granulation, extrusion molding, pan coating, spheronization, drum granulation, fluidized bed agglomeration, high shear granulation, fluidized bed spraying It can be made by a variety of manufacturing techniques such as coating, crystallization, precipitation, emulsion gelation, rotating disk atomization, and other cast molding methods, and prill processes. Such processes are known in the art and are described in U.S. Pat. Nos. 4,689,297 and 5,324,649 (fluidized bed process), EP 6,56058B1 and U.S. Pat. No. 4,543,332 (extrusion process), U.S. Pat. No. 6,248,706. (Granulation, high shear) and European Patent No. 804532 B1 and US Pat. No. 6,534,466 (a combination of processes utilizing a fluidized bed core and mixer coating).

  The active substance is typically coated around the core. A core suitable for use in the present teachings may be any material that meets the definitions of smoothness index, mass median diameter, and particle size differences provided herein. In one embodiment of the present teachings, the core comprises sodium chloride or sodium sulfate crystals. In another embodiment of the present teachings, the core includes sucrose seeds. Particles consisting of inorganic salts and / or sugars and / or small organic molecules may be used as the core of the present teachings. Suitable water-soluble ingredients for incorporation into the core include inorganic salts such as sodium chloride, ammonium sulfate, sodium sulfate, magnesium sulfate, zinc sulfate, sugars such as urea, citric acid, sucrose, lactose, and the like. It is done. In some embodiments, the core particle is a crystalline inorganic salt. In some embodiments, the core particle is crystalline sodium sulfate.

  As used herein, the term “small smooth core particle” refers to the interior of a granule, granule that exhibits measurements of the specific smoothness index, mass median diameter, and particle size dispersion index provided herein. Refers to particles.

  As used herein, the term “smoothness index” refers to the ratio of the experimental specific surface area to the skin specific surface area calculated for a representative core sample.

  As used herein, a “representative core sample” refers to a random sample of at least 15 core particles.

  The term “experimental specific surface area” as used herein refers to the BET (Brunauer-Emmett-Teller) gas adsorption method (S. Brunauer, PH Emmett and E. Teller, J. Am. Chem. Soc., 1938, 60, 309. doi: 10.1021 / ja01269a023) refers to the experimentally measured surface area (measured in square meters / gram) per gram of a representative core sample. . Details of the BET method are described in the method section below.

  The term “skin specific surface area” as used herein refers to the measured particle size distribution and average true value of a representative core sample, with the ideal assumption that all core particles are perfectly spherical. Refers to the specific surface area (in square meters per gram) calculated based on density. The algorithm for calculating the skin specific surface area is described in the method section below.

  The term “particle size distribution” (abbreviated as PSD), as used herein, refers to the relative amount by weight percent of small smooth core particles present in each of several diameter dimension intervals. The PSD of the core sample is measured by laser light scattering (see, eg, T. Allen, Particle Size Measurement, Vol. 1 (Chapman and Hall, 1997)). In the present application, PSD is characterized by three mass percentile diameters that can be measured from the log-normal plot of the PSD.

D ₅₀ or MMD (mass median diameter), a mass median diameter of the lognormal distribution. MMD is considered to be the mass average particle size, with less than 50% w / w particles in a representative sample having a smaller diameter.

D ₁₀ : 10th percentile diameter (TPD), the diameter at which 10% w / w particles in a representative sample have a smaller diameter.

D ₉₀ : 90th percentile diameter (NPD), the diameter at which 90% w / w particles in a representative sample have a smaller diameter.

Typically, D ₁₀ , D ₅₀ , and D ₉₀ are expressed in micrometers.

The “particle size dispersion index” (abbreviated as PSDI) of the core sample is the D ₉₀ / D ₁₀ ratio of a representative sample.

  As used herein, the term “coating” refers to a layer of material surrounding an underlying material. The first coating layer typically encapsulates the core to form a substantially continuous layer so that there is little or no unmeeting area on the core surface, typically an active agent. It is a coating. Subsequent additional coating layers can encapsulate the growing granules and form one or more additional substantially continuous layers (“additional coatings”). The materials used in the granules (eg, active substances and components detailed herein) may be suitable for use in food and / or animal feed, but need to be And therefore may be food grade or feed grade.

  Coatings of the present teachings can be inorganic salts, salts of organic acids, sugars, sugar alcohols, starches (natural, pregelatinized, hydrolyzed, or chemically modified), and other polysaccharides, gums, additional active substances, feed or One or two of food grade polymers, pigments, clays, plasticizers, surfactants, fiber materials, anti-adhesives, fillers, spreaders, and other compounds known for use in coatings It may further include one or more. Suitable polymers include polyvinyl alcohol (PVA), including partially and fully hydrolyzed PVA, polyethylene glycol, polyethylene oxide, polyvinyl pyrrolidine, and carbohydrate polymers (eg starch, amylose, amylopectin, α and β- Glucan, pectin, glycogen, mixtures and derivatives thereof). Suitable fillers useful in coatings include inert materials that are used to increase bulk, reduce costs, or to adjust the enzyme activity aimed at in the final granule. Examples of such fillers include water-soluble agents such as salts, sugars, and water-dispersible agents such as clay, talc, silicate, cellulose, and starch, and derivatives of cellulose and starch. It is not limited to. Suitable plasticizers for use in the coatings of the present teachings are low molecular weight organic compounds that are very specific to the polymer being plasticized. Examples include sugars (eg, glucose, fructose, and sucrose), sugar alcohols (eg, sorbitol, xylitol, and maltitol, and other glycols), polar low molecular weight organic compounds such as urea, or other known such as water Or a feed grade plasticizer, but is not limited thereto. Suitable fiber materials for use in the coatings of the present teachings include cellulose and cellulose derivatives, such as HPMC (hydroxy-propyl-methylcellulose), CMC (carboxy-methylcellulose), HEC (hydroxy-ethylcellulose). It is not limited. In one embodiment of the present teachings, particularly feed applications, the coating comprises a water soluble or water dispersible corn cob material, or sugar, or salt crystals. In another embodiment particularly suitable for household cleaning applications, the coating comprises water-soluble or water-dispersible sugars, or salt crystals, or non-pareils. Those skilled in the art will recognize that for feed and food applications, coatings (and any polymers, fillers, plasticizers, fiber materials, and spreaders) are acceptable in food and / or feed applications. Let's go. For household cleaning applications, such restrictions need not apply.

  The term “active agent coating” as used herein refers to a coating that contains an active agent (typically an enzyme). In general, an active agent coating can be applied to small smooth core particles, followed by optional additional coatings.

  The term “additional coating” as used herein refers to one or more coatings optionally applied to small smooth core particles. Typically, additional coatings can be applied to unfinished granules containing small smooth core particles and an active agent coating. Non-limiting examples of additional coatings include moisture barrier coatings and hydration coatings.

  The term “moisture barrier coating” as used herein refers to a coating comprising a moisture barrier material.

  The term “hydrating coating” as used herein refers to a coating comprising a hydrating material.

  The term “moisture barrier material” refers to a material that eliminates, prevents or substantially delays the uptake of water. These materials are typically hydrophobic or amphiphilic, provide water shielding, and essentially do not absorb and / or bind water, including film-forming materials, It is not limited. Examples of moisture barrier materials include barrier polymers, proteins, lipids, fats and oils, fatty acids, and rubbers. Examples of film-forming moisture barrier materials include natural and modified barrier polymers such as gum arabic, whey, whey protein concentrate, PVA including modified and fully hydrolyzed PVA, and latex, HPMC, and acid treated hydroxypropyl Synthetic polymers such as starches such as PureCote ™, oxidized starch, and modified starch. Non-film-forming moisture barrier materials include, for example, waxes, fats, oils and lipids, and lecithin. Selected moisture barrier materials that are not readily participated are, for example, latex polymers and barrier polymers such as gum arabic.

  The term “hydrating material” refers to a material that absorbs an aqueous liquid, such as water, by some mechanism. In the first non-limiting mechanism, the material absorbs free water. In the second non-limiting mechanism, the material absorbs bound water that normally exists as hydrated crystal water. Thus, the material is provided as a partially or fully hydrated material or as a non-hydrated material that absorbs or binds aqueous liquids and slows or reduces the rate or degree of migration of such liquids into the active substance. May be. In a third non-limiting mechanism, the hydrated material thermally shields the active substance by delaying heat transfer to the active substance in the granule and keeping the active substance at a temperature below that of the outer surface of the granule. To do. Hydrated materials include inorganic salts including carbohydrates and hydrated salts such as magnesium sulfate, sodium sulfate, and ammonium sulfate; maltodextrins; sugars such as sucrose; starches such as corn starch.

  As used herein, the terms “pellet” and “pelletizing” refer to solid, round, spherical, and cylindrical tablets, ie pellets, and such solid shapes, especially feed pellets, and solid extrusions. It relates to the process of forming animal feed. Known food and animal feed pelleting processes typically involve mixing food or feed ingredients at room temperature for about 1 to about 5 minutes, transferring the resulting mixture to a surge bin, and mixing the mixture into a steam conditioner. Conveying, optionally transferring the mixture after steam conditioning to an expansion device, transferring the mixture to a pellet mill, ie an extruder, and finally transferring the pellets to a pellet cooler. Fairfield, D.C. 1994. Chapter 10, Pelleting Cost Center. In Feed Manufacturing Technology IV. (McEllhiney, editor), American Feed Industry Association, Arlington, Va. , Pp. 110-139.

  As used herein, the term “non-pelletized mixture” refers to premixes or precursors, base mixes, meals, and diluents. The premix typically contains vitamins and trace minerals. Base mixes typically include food and feed ingredients such as dicalcium phosphate, limestone, salt and vitamin and mineral premixes, but no grain and protein ingredients. As diluents, grains (eg wheat bran and rice bran), and clays such as phyllosilicates (magnesium silicate leptite, bentonite, kaolin, montmorillonite, hectorite, saponite, beidellite, attapulgite, and stevensite ), But is not limited thereto. Clay also functions as a feed premix carrier and fluidizing agent, or diluent. The meal is typically a complete animal diet.

  As used herein, the term “activity recovery” includes (i) heating, pressurization, increasing pH, decreasing pH, storage, drying, exposure to surfactants, solvents (including water / moisture) ), And the ratio of the activity of the active substance after treatment with one or more of the stress factors including mechanical stress to (ii) the activity of phytase before treatment. The activity recovery rate can be expressed as a percentage.

  The percent recovery of activity is calculated as follows.

  In the context of pelleting experiments, “pre-treatment activity” is estimated by measuring the activity of the active substance contained in untreated meals in a manner comparable to the active substance otherwise treated. it can.

  For example, the active substance in an untreated meal may be handled and stored under similar conditions for the same amount of time as the active substance in a treated (eg, pelleted) meal, other than the specific treatment itself. Control possible interactions or other effects.

  As used herein, the term “active substance” may be any substance that provides the desired functionality for the application being added to the granule. Active substances include biologically viable substances, food or feed ingredients, antibacterial agents, antibiotic substitutes, prebiotics, probiotics, pesticides, fertilizers, herbicides and other agricultural chemical ingredients, pharmaceutical ingredients, Or it may be an active ingredient for home care, or a combination thereof. In preferred embodiments, the active ingredient is a protein, enzyme, peptide, polypeptide, amino acid, carbohydrate, lipid or oil, vitamin, co-vitamin, hormone, or combinations thereof. In another embodiment, the active ingredient is an enzyme, bleach, bleach activator, perfume, or other biologically active ingredient. Inherently thermostable active substances are encompassed by the present teachings and can exhibit enhanced thermal stability within the granules. The most preferred active ingredients for food and feed applications are enzymes, peptides and polypeptides, amino acids, antibacterial agents, gastrointestinal health promoters, vitamins, and combinations thereof. Any enzyme can be used, and non-limiting examples of enzymes include phytase, xylanase, β-glucanase, phosphatase, protease, amylase (α or β or glucoamylase), cellulase, lipase, cutinase, oxidase, transferase, reductase , Hemicellulase, mannanase, esterase, isomerase, pectinase, lactase, peroxidase, laccase, other oxidoreductases, and mixtures thereof. Particularly preferred enzymes include a xylanase from Trichoderma reesei and a mutant xylanase from Trichoderma reesei (both available from DuPont Industrial Biosciences) or the essentially thermostable xylanase described in European Patent No. 1222256B1, and ssp. niger, Aspergillus kawachii, Aspergillus tubeigenis, Aspergillus clavatus, Bacillus circulus, Bacillus pumilus, Bacillus subtilis, Fusarius callimastix patriciarum, Penicillium species, Streptomyces lividans, Streptomyces thermoviolaceus, Thermomonospora fusca, Trichoderma harzianum, Trichoderma reesei, include other xylanases from Trichoderma viride. Additional particularly preferred enzymes include, for example, phytases such as Finase L®, which is a phytase from the Aspergillus species available from AB Enzymes (Darmstadt, Germany); both of which are available from Danisco Animal Nutrition, DuPont Trademarks) XP (E. coli derived phytase), and Axtra Phy (Buttiauxella derived phytase) and, for example, Trichoderma, Penicillium, Fusarium, Buttiauxella, Citrobacter, Enterobacter, Henacillium, Hum And other phytases described in US Patent Application Nos. 61 / 595,923 and 61 / 595,941 both filed on Feb. 12, 2012. Examples of cellulases include Multifect® BGL, which is a cellulase (β-glucanase) available from Danisco Animal Nutrition, DuPont, and Aspergillus, Trichoderma, Penicillium, Humanicola, Cellularh, Cellularh, Cellularh, Cellularp Other cellulases derived from species such as Cellulases and endoglucanases described in US Patent Application Publication No. 2006013897A1 can also be used. Amylases are, for example, species such as Aspergillus, Trichoderma, Penicillium, Bacillus, subtilis, B.M. stearothermophilus, B.I. lentus, B. et al. licheniformis, B.I. coagulans, and B.I. It may be derived from amyloliquefaciens. Suitable fungal amylases are Aspergillus, such as A. oryzae and A.I. It is derived from niger. The protease may be from Bacillus amyloliquefaciens, Bacillus lentus, Bacillus subtilis, Bacillus licheniformis, and Aspergillus and Trichoderma species. Phytase, xylanase, phosphatase, protease, amylase, esterase, oxidoreductase, lipase, transferase, cellulase, and β-glucanase are commonly used enzymes for inclusion in animal feed. Suitable enzymes for inclusion in tablets for home care use are similar, in particular proteases, amylases, lipases, pectate lyases, mannanases, hemicellulases, oxidoreductases, peroxidases, transferases and cellulases. In particularly preferred embodiments of the present teachings, the enzyme is selected from phytase, xylanase, β-glucanase, amylase, protease, lipase, esterase, and mixtures thereof. In one embodiment of the invention, two enzymes, xylanase and β-glucanase, are provided in the granules. In another embodiment of the invention, the two types of enzymes provided in the granules are proteases and amylases. The enzymes may be mixed together or applied separately to the granules. In another embodiment, three types of enzymes are provided in the granules, namely β-glucanase, xylanase, and phytase. The enzymes listed above are only examples and are not exclusive. Any enzyme, such as wild-type, recombinant, and mutant enzymes of bacterial, fungal, yeast, plant, insect, and animal sources, as well as acidic, neutral, or alkaline enzymes are used in the granules of the present teachings. Good. One skilled in the art will recognize that the amount of enzyme used will be determined, at least in part, by the enzyme selected and the type and characteristics of its intended use.

Methods BET Specific Surface Area Measurement To measure the specific surface area of the core particles, the BET method was used to evaluate the pore distribution of the core by krypton gas adsorption / desorption using the Micromeritics model ASAP 2420 Accelerated Porosity and Surface Area System. . Using the BJH method (Elliott P. Barrett, Leslie G. Joyner, Paul P. Halenda, J. Am. Chem. Soc., 1951, 73 (1), pp 373-380, DOI: 10.1021 / ja01145a126) The pore volume distribution was measured in the range of 20 to 1000 mm. A sample with a mass of about 4-6 grams was degassed overnight at 150 ° C. under reduced pressure to remove adsorbed water and / or volatile contaminants. These weights were remeasured, placed in a vacuum, and transferred to a porosity meter, cooled to -196 ° C (77K), the point at which the gas (Kr) adsorption isotherm was recorded by pressure measurement. The surface area range is automatically calculated by the ASAP 2420 V2.07J software package provided by Micromeritics.

Skin Specific Surface Area Calculation The skin specific surface area represents the specific surface area of a perfectly smooth, spherical, equivalent ideal particle sample whose PSD matches that of the actual core sample. The core particle size distribution (PSD) is measured by laser diffraction (ref. ISO 13320-1: 1999) using hexane as background fluid in the recirculation loop and using a Malvern Mastersizer 2000. An amount of core sample that is of sufficient mass is added to reach a laser opacity of about 10%. The PSD is automatically calculated from the diffraction pattern using Mie theory. In the case of sodium sulfate, the complex refractive index of the particles is considered 1.468 + 0.01i, and the refractive index of the fluid is considered 1.375. The resulting PSD is a differential mass fraction showing the percentage of particles in each of 81 logarithmically divided size bottles ranging from 0.01 micrometers to 10,000 micrometers. If necessary, the PSD must be corrected and renormalized to exclude artifacts such as fine dust or agglomerates, particularly any particles less than 60 micrometers or greater than 500 micrometers.

The geometric mean diameter of the upper and lower size fractions of each size bin is calculated by taking the square root of the product of the upper and lower size fractions. The skin specific surface area in square meters per gram in a given bottle is given by 6 / (d ^* ρ), where d is the particle size (cm) and ρ is the true density of the particulate solid (void) Is the density excluding) (g / cm ³ ). In the case of sodium sulfate, ρ = 2.664 g / cm ³ . Since PSD is a mass-weighted distribution, the total hull surface area is calculated by multiplying the differential mass fraction of each size bin by the specific surface area of that size bin and summing all size bins.

Exemplary Embodiments In some embodiments, the present teachings surprisingly have comparable stability compared to granules containing a small, non-smooth core, thereby allowing for material cost savings. A granule composition is provided. For example, the granule compositions of the present teachings can surprisingly have comparable storage stability. Desirable storage stability may be present in any of a variety of situations, such as dish detergents, laundry detergents, animal feed, fiber, and human food. Granules of the present teachings can exhibit improved stability under these various conditions as compared to granules lacking similarly preserved small smooth core particles of the present teachings. In some embodiments, the present teachings are believed to provide improved stability as compared to granules comprising larger and / or non-smooth cores.

  In some embodiments, the present teachings provide granule compositions that have an equivalent resistance to dust generation as compared to granules containing a small, non-smooth core as measured by a Heubach dust test.

  In some embodiments, the present teachings are believed to provide granule compositions with improved resistance to dust generation for granules containing a small, non-smooth core.

  In some embodiments, the present teachings provide granule compositions that are equivalent in resistance to steam pelletization as compared to granules containing a core that is not a small smooth core. For example, the degree of “activity recovery” as defined above can be measured for the granules of the present teachings and compared to similarly processed granules containing a different core than the small smooth core particles of the present teachings. In some embodiments, the present teachings are believed to provide granule compositions with improved resistance to steam pelletization as compared to granules containing small smooth cores.

  Additional uses and methods that utilize the granules of the present teachings are described in the non-limiting section below.

Compositions and Methods for Oven Cooking and Food Cooking The present teachings include, but are not limited to, “food compositions” including, but not limited to, food products, animal feeds, and / or food / feed additives, including the present granule compositions. As well as methods for preparing such food compositions, or uses thereof, comprising mixing the granule composition with one or more food ingredients.

  The granule composition can be used in the preparation of a food composition, wherein the food composition is oven cooked after the addition of the granule composition. As used herein, the term “oven cooking composition” includes an oven cooking powder, dough, oven cooking additive, and / or oven cooked product. By any composition and / or additive prepared by the process of providing a cooked food product. The food composition or additive may be liquid or solid.

  As used herein, the term “flour” means milled or ground grain. The term “flour” also means a sago or tuber product that has been ground or crushed. In some embodiments, the flour may also include ingredients that are added to the milled or milled grain or plant material. While not intending to be limiting, an example of an additional component is a swelling agent. Grains include wheat, oats, rye, and barley. Tuber products include tapioca flour, cassava flour, and powdered custard. The term “flour” also includes ground corn flour, corn meal, rice flour, whole grain flour, baking powdered flour, tapioca flour, cassava flour, ground rice, fortified flour, and powdered custard.

  In commercial and household oven cooking and food production flours, it is important to maintain the enzyme activity in the flour at an appropriate level. An activity level that is too high can result in a sticky and / or rod-like product, which is not a commercial product. Insufficient enzyme activity flour does not contain enough sugar for the original yeast function and may result in a dry crumb bread, ie an oven cooked product. Thus, the present granule composition combined with α-amylase can be added to the flour to increase the level of endogenous enzyme activity in the flour.

  Any amylase, alone or in combination with another amylase, can be added to the granule composition to prevent or delay aging of the oven-cooked product, i.e., crumb hardening. The amount of anti-aging amylase is typically in the range of 0.01 to 10 mg enzyme protein per kg flour, for example 0.5 mg / kg ds. Additional anti-aging amylases that can be used include endoamylases, for example bacterial endoamylases from Bacillus. The additional amylase may be, for example, another maltogenic α-amylase derived from Bacillus (EC 3.2.1.133). Novamyl (registered trademark) A representative maltogenic α-amylase derived from stearothermophilus NCIB 11837, see, eg, Christophersen et al. (1997) Starch 50: 39-45. Another example of an anti-aging endoamylase is Bacillus, such as B. licheniformis or B.I. Examples include bacterial α-amylase derived from amyloliquefaciens. The anti-aging amylase may be, for example, an exoamylase derived from a plant source such as soybeans or a microbial source such as Bacillus, such as β-amylase.

The oven cooking composition comprising the present granule composition may further comprise phospholipase or an enzyme having phospholipase activity. An enzyme having phospholipase activity has an activity that can be measured in lipase units (LU). Phospholipase form lysophospholipids except fatty acid from phospholipid, may have A ₁ or A ₂ activity. It may or may not have lipase activity, ie activity on triglyceride substrates. The phospholipase typically has an optimum temperature in the range of 30-90 ° C, such as 30-70 ° C. The added phospholipase may be of animal origin, eg, from the pancreas, eg, bovine or porcine pancreas, snake venom, or bee venom. Alternatively, the phospholipase may be derived from a microbial source, such as a filamentous fungus, such as a yeast or a bacterium.

  Add phospholipase in an amount that improves the softness of the bread early after cooking in the oven, especially during the first 24 hours. The amount of phospholipase is typically in the range of 0.01 to 10 mg enzyme protein per kg flour, for example 0.1 to 5 mg / kg. That is, the phospholipase activity is usually in the range of 20 to 1000 LU / kg of powder, where the lipase unit is 1 μmol per minute when gum arabic is used as an emulsifier and tributyrin as a substrate at 30 ° C. and pH 7.0. Defined as the amount of enzyme required to release the amount of butyric acid.

  The composition of the dough generally consists of whole wheat flour or wheat flour and / or other types of whole wheat flour, flour or starch such as corn flour, corn starch, rye whole wheat flour, rye flour, oat flour, oat whole wheat flour, Contains soy flour, sorghum whole grain flour, sorghum flour, potato flour, potato flour, or potato starch. The dough may be raw, frozen, or semi-baked. The fabric may be an expanded fabric or a expanded fabric. The dough may be swelled in various ways, such as by chemical swelling agents such as sodium bicarbonate or by the addition of bread seeds, ie fermentation dough. The dough is prepared from a suitable yeast culture, such as Saccharomyces cerevisiae (eg, baker's yeast), such as commercially available S. It may be expanded by adding a cerevisiae culture medium.

  The dough is made of other conventional dough ingredients such as proteins such as milk powder, gluten, and soybean; eggs (eg, whole egg, yolk, or white); ascorbic acid, potassium bromate, potassium iodate, azodicarbonamide (ADA) or oxidizing agents such as ammonium persulfate; amino acids such as L-cysteine; sugars; or salts such as sodium chloride, calcium acetate, sodium sulfate, or calcium sulfate. The dough may further comprise a fat, for example a triglyceride such as granular fat or shortening. The dough should contain an emulsifier such as mono- or diglyceride, mono- or diglyceride diacetyltartaric acid ester, fatty acid sugar ester, fatty acid polyglycerol ester, monoglyceride lactate ester, monoglyceride acetate ester, polyoxyethylene stearate, or lysolecithin Further may be included. For example, the dough may be manufactured without adding an emulsifier.

  The dough product may be any processed dough product, such as boiled, fried, roasted, baked, steamed, and boiled, such as steamed bread and rice cakes. In one embodiment, the food product is a bakery product. Typical bakery products include bread, such as loaf, rolls, buns, bagels, pizza dough, pastries, pretzels, tortillas, cakes, cookies, biscuits, crackers and the like.

  If desired, additional enzymes may be used with the anti-aging amylase and phospholipase. The additional enzyme may be a second amylase such as amyloglucosidase, β-amylase, cyclodextrin glucanotransferase, or the additional enzyme may be a peptidase, in particular an exopeptidase, transglutaminase, lipase, cellulase, xylanase, protease Protein disulfide isomerases, for example, protein disulfide isomerases disclosed in WO 95/00636, such as glycosyltransferases, branching enzymes (1,4-α-glucan branching enzymes), 4-α-glucanotransferases (Dextrin glycosyltransferase) or oxidoreductase such as peroxidase, laccase, glucose oxidase, pyranose oxidase, lipoxy Kinase (lipooxygenase), it may be a L- amino acid oxidase, or a carbohydrate oxidase. The additional enzyme may be of any origin, such as from mammals and plants, especially microorganisms (bacteria, yeast, or fungi) and may be obtained by techniques conventionally used in the art.

  The xylanase is typically a microbial source, for example from bacteria or fungi such as Aspergillus strains. Xylanases include, for example, Pentopan® and Novozym 384®, which are commercial xylanase preparations produced from Trichoderma reesei. Amiloglucosidase is A. Niger's amyloglucosidase (eg, AMG®). Other useful amylase products include Grindamyl® A 1000 or A 5000 (Grindstead Products (Denmark)), and Amylase® H or Amylase® P (DSM). The glucose oxidase may be a fungal glucose oxidase, especially an Aspergillus niger glucose oxidase (eg Gluzyme®). A typical protease is Neutrase®.

  This process can be used for any type of oven-cooked product made from dough (either soft or crisp, either white, light or dark type). Examples of this are typically loaf or roll breads, especially white whole grain or rye breads, French bread, pita bread, tortillas, cakes, pancakes, biscuits, cookies, pie crusts, crispbread, steamed bread, Although it is pizza etc., it is not limited to these.

  The granule composition can be used in a premix where the powder is included with anti-aging amylase, phospholipase, and / or phospholipid. The premix may contain other dough improving and / or bread improving additives, such as any additive containing the enzymes. The granule composition may be a component of an enzyme preparation comprising anti-aging amylase and phospholipase for use as an oven cooking additive.

  Storage, handling, and incorporation of the contained delivery vehicle can be accomplished by means of a packaged mix. The packaged mix may include the present granule composition. However, the packaged mix may further include additional ingredients required by the manufacturer or bakery. After the granule composition is mixed into the dough, the bakers continue the normal whole manufacturing process for the product.

  A food composition is contemplated wherein the food is an oil, meat, lard composition comprising the granule composition. The term “[oil / meat / lard] composition” in this sense means any composition based on, made from and / or comprising oil, meat or lard, respectively. An oil or meat or lard composition comprising the granule composition and / or a method for producing an additive comprising mixing the granule composition with an oil / meat / lard composition and / or an additive component. Intended.

  The food composition may be an animal feed composition, an animal feed additive, and / or a pet food comprising the present granule composition. Such an animal feed composition, animal feed, comprising mixing the granule composition itself with one or more animal feed ingredients and / or animal feed additive ingredients and / or pet food ingredients Additive compositions and / or methods for producing pet food are contemplated. This granule composition can be used for the production of animal feed compositions and / or animal feed additive compositions and / or pet foods.

  The term “animal” includes all non-ruminants and ruminants. In certain embodiments, the animals are non-ruminant animals such as horses and monogastric animals. Examples of monogastric animals include pigs (pig and sine) such as small pigs, breeding pigs, sows; poultry such as turkeys, ducks, chickens, broilers, layers; fishes such as salmon, trout, tilapia , Catfish and carp; and crustaceans such as, but not limited to, shrimp and shrimp. In a further embodiment, the animals include cattle, calves, goats, sheep, giraffes, bison, mousse, elk, yak, buffalo, deer, camel, alpaca, llama, antelope, horned antelope, and nilgai. A ruminant, but not limited to.

  In this context, the term “pet food” includes dogs, cats, gerbils, hamsters, chinchillas, pet rats, guinea pigs; avian pets such as canaries, parakeets, and parrots; reptile pets such as turtles, lizards, And snakes; are intended to be understood as meaning domestic animal foods, including but not limited to aquatic pets, such as tropical fish and frogs.

  The terms “animal feed composition”, “feed”, and “feed” are used interchangeably, and a) small grains (eg, wheat, barley, rye, oats, and combinations thereof) and / or Grains such as large grains (e.g. corn or sorghum); b) by-products derived from grains, e.g. corn gluten feed, grain distillers (DDGS) (especially maize distillers (cDDGS), wheat bran, bran in wheat, Wheat bran, rice bran, rice husk, oat husk, palm kernel, and citrus pulp; c) soy, sunflower, peanut, lupine, pea, broad bean, cotton, canola, fish, dried plasma protein, meat and bone meal, potato Protein obtained from sources such as protein, whey, copra, sesame; d) fats and oils obtained from plant and animal sources; e) minerals Fine vitamins are selected from the group comprising, it may include one or more feed materials.

Fiber desizing compositions and uses Further contemplated are compositions and methods for treating fabrics (eg, fiber desizing) using the present granule compositions. Fabric treatment methods are well known in the art (see, eg, US Pat. No. 6,077,316). For example, the feel and appearance of the fabric can be improved by a method that involves contacting the fabric with the granule composition in solution. The fabric may be treated with the solution under pressure.

  The granule composition can be applied during or after weaving the fibers, or during the desizing stage, or during one or more additional fabric processing steps. While weaving the fiber, the yarn is exposed to considerable mechanical strain. Before weaving on a loom, warp yarns are often coated with a starching starch or starch derivative to increase tensile strength and prevent cutting. The granule composition can be applied during or after weaving to remove this sizing starch or starch derivative. After weaving, to ensure a homogeneous and wash-resistant result, the granule composition can be used to remove the glued coating before further processing of the fabric.

  This granule composition can be used, for example, as a detergent additive in aqueous compositions, alone or in combination with other desizing chemicals and / or desizing enzymes, to desizing fabrics such as cotton blended fabrics. can do. This granule composition can also be used in a composition and method for subjecting an indigo-dyed denim fabric and garment to a stone wash process. In the manufacture of garments, the fabric can be cut and sewn into the garment, or garment, and then finished. In particular, various enzymatic finishing methods have been developed in the manufacture of denim jeans. Denim garment finishing usually begins with an enzymatic desizing process while the garment is subjected to the action of starch-degrading enzymes, giving the fabric flexibility and making more use of cotton cloth for the subsequent enzymatic finishing process Make it easy to do. The granule composition can be used in denim garment finishing (eg, a “biostone process”), enzymatic desizing, and methods that provide fabric flexibility and / or in the finishing process.

Cleaning Composition An aspect of the present composition and method is a cleaning composition comprising the present granule composition as a constituent. Protease polypeptides, or other suitable enzymes, can be used as a component in detergent compositions for hand washing, washing machine washing, dish washing, and other hard surface washing.

  Preferably, the granule composition is mixed into the detergent at a concentration at or near that at which amylase is conventionally used in the detergent. For example, the protease polypeptide may be added in an amount corresponding to 0.00001-1 mg (calculated as pure enzyme protein) of amylase per liter of laundry / dishwashing fluid. As exemplified below, representative formulations are provided herein.

  A protease polypeptide may be a component of a detergent composition as the sole enzyme or in conjunction with other enzymes, including other amylolytic enzymes. Therefore, it may be included in the detergent composition in the form of the present granule composition. When used in this context, a non-limiting example of a waxy coating material is a poly (ethylene oxide) product (polyethylene glycol, PEG) having an average molar weight of 1,000 to 20,000; 16 to 50 ethylene oxide units Ethoxylated nonylphenols having alcohols; ethoxylated fatty alcohols having 12 to 20 carbon atoms and having 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids It is. An example of a film-forming coating material suitable for application by the fluidized bed process is found, for example, in British Patent No. 1483591.

  The detergent composition may include one or more surfactants, each of which may be anionic, nonionic, cationic, or zwitterionic. Detergents are typically 0% to about 50% anionic surfactant, such as linear alkyl benzene sulfonate (LAS); α-olefin sulfonate (AOS); alkyl sulfate (aliphatic alcohol sulfate) (AS); alcohol ethoxy sulfate (AEOS or AES); secondary alkane sulfonate (SAS); α-sulfo fatty acid methyl ester; alkyl- or alkenyl succinic acid; or soap. This composition comprises 0% to about 40% nonionic surfactants such as alcohol ethoxylates (AEO or AE), carboxylated alcohol ethoxylates, nonylphenol ethoxylates, alkylpolyglycosides, alkyldimethylamine oxides, ethoxy Fatty acid monoethanolamide, fatty acid monoethanolamide, or polyhydroxyalkyl fatty acid amide (for example, described in WO 92/06154) may be contained.

  The detergent composition additionally comprises one or more other enzymes, such as another protease, another amylolytic enzyme, cutinase, lipase, cellulase, pectate lyase, perhydrase, mannanase, xylanase, peroxidase, and The laccase may be included in any combination.

  Detergents include from about 1% to about 65% detergent builders or complexing agents such as zeolites, diphosphates, triphosphates, phosphonates, citrates, nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid ( DTMPA), alkyl- or alkenyl succinic acids, soluble silicates or layered silicates (eg Hoechst SKS-6). The detergent may also be free of builders, i.e. essentially free of detergent builders. Enzymes, and in particular amylases with or without starch binding domains, in various compositions such as laundry and dishwashing applications, surface cleaners, and in compositions for producing ethanol from starch, ie biomass Can be used in

  The detergent may contain one or more polymers. Examples include carboxymethyl cellulose (CMC), poly (vinyl pyrrolidone) (PVP), polyethylene glycol (PEG), poly (vinyl alcohol) (PVA), polycarboxylates such as polyacrylates, maleic / acrylic acid copolymers, and lauryl Mention may be made of methacrylate / acrylic acid copolymers.

The detergent may contain a source of H ₂ O ₂ such as perborate or percarbonate and in combination with a peracid generating bleach activator such as tetraacetylethylenediamine (TAED) or nonanoyloxybenzenesulfonate (NOBS). Can contain a good bleaching system. Alternatively, the bleaching system may include a peroxy acid (eg, an amide, imide, or sulfone type peroxy acid). The bleaching system may be an enzymatic bleaching system, for example a perhydrase such as that described in WO 2005/056783.

  Enzymes in detergent compositions are stabilized using conventional stabilizers, for example, polyols such as propylene glycol or glycerol; sugars or sugar alcohols; lactic acid; boric acid or boric acid derivatives such as aromatic borate esters. The composition may be formulated as described, for example, in WO 92/19709 and 92/19708.

  Detergents include, for example, clay, foam enhancers, foam inhibitors, anticorrosives, soil suspending agents, soil reattachment inhibitors, dyes, bactericides, cloudy inhibitors, fluorescent whitening agents, or fragrances. Other conventional detergent ingredients such as fabric conditioners may be included.

  The pH (measured at the use concentration in an aqueous solution) is usually neutral or alkaline, eg, about pH 7.0 to about 11.0.

  Specific forms of detergent compositions included in the present teachings are described below.

Heavy Dry / Solid (HDD) Laundry Detergent Composition A typical HDD laundry detergent composition comprises an anionic detersive surfactant (eg, a linear or branched or random chain, substituted or unsubstituted alkyl sulfate, Alkyl sulfonates, alkyl alkoxylated sulfates, alkyl phosphates, alkyl phosphonates, alkyl carboxylates, and / or mixtures thereof), nonionic detersive surfactants (eg, linear, or branched or random chain, Substituted or unsubstituted C ₈ -C ₁₈ alkyl ethoxylates and / or C ₆ -C ₁₂ alkyl phenol alkoxylates), cationic detersive surfactants (eg, alkyl pyridinium compounds, alkyl quaternary ammonium compounds, alkyl quaternary phosphoniums) Compound, a Rutile tertiary sulfonium compounds, and mixtures thereof), zwitterionic and / or amphoteric detersive surfactants (eg, alkanolamine sulfo-betaines), amphoteric surfactants, semipolar nonionic surfactants, and Detersive surfactants containing these mixtures; phosphate-free builders (e.g. zeolite builders, in these examples, zeolite A, zeolite X, zeolite P and zeolite in the range of less than 0 wt% to less than 10 wt% MAP), phosphate builders (eg, sodium tripolyphosphate in the range of 0 wt% to less than 10 wt%), citric acid, citrate, and nitrilotriacetic acid, silicates (eg, 0 wt% to 10 wt%). Sodium or potassium silicate in a range of less than% by weight, or sodium metasilicate, or layered Builder (e.g. IKS (SKS-6)); carbonate salts (e.g. sodium carbonate and / or sodium bicarbonate ranging from 0% to less than 80% by weight); and photobleaching agents (e.g. sulfonation) Zinc phthalocyanine, sulfonated phthalocyanine aluminum, xanthene dyes, and mixtures thereof), hydrophobic or hydrophilic bleach activators (eg, dodecanoyloxybenzenesulfonate, decanoyloxybenzenesulfonate, decanoyloxybenzoic acid, or these) Salts, 3,5,5-trimethylhexanoyloxybenzenesulfonate, tetraacetylethylenediamine-TAED, nonanoyloxybenzenesulfonate-NOBS, nitrile quat, and mixtures thereof), hydrogen peroxide source (eg, inorganic overhydration) Salt, this Examples of perborate, percarbonate, persulfate, perphosphate, or persilicate mono- or tetrahydrate sodium salts), pre-formed hydrophilic and / or Or hydrophobic peracids (eg, percarboxylic acids and salts, percarbonates and salts, perimidic acids and salts, peroxymonosulfuric acid and salts, and mixtures thereof) and / or bleach catalysts (eg, imine bleach enhancers) (These examples include iminium cations and polyions), iminium zwitterions, modified amines, modified amine oxides, N-sulfonylimines, N-phosphonylimines, N-acylimines, thiadiazole dioxides, perfluoroimines, cyclic Sugar ketones, and mixtures thereof), and metal-containing bleach catalysts (eg, auxiliary metal cations such as zinc or aluminum, and ethylenediamine tetra Bleaching agents, including copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations, and water-soluble salts thereof, in combination with a sequestering agent such as acetic acid, ethylenediaminetetra (methylenephosphonic acid).

  The composition is preferably an enzyme such as protease, amylase, lipase, cellulase, choline oxidase, peroxidase / oxidase, pectate lyase, mannanase, cutinase, laccase, phospholipase, lysophospholipase, acyltransferase, perhydrase, arylesterase, and Including any mixtures of these.

  The composition comprises perfume microcapsules, perfume accord encapsulated with starch, toning agents, additional polymers such as fabric-integrated cationic polymers, dye fixing ingredients, fabric softeners, whitening agents (eg CI fluorescent) Whitening agents), flocculants, chelating agents, alkoxylated polyamines, fabric deposition aids, and / or additional detergent ingredients may be included.

Automatic Dishwashing (ADW) Detergent Composition A typical ADW detergent composition is an ethoxylated nonionic surfactant, an alcohol alkoxylated surfactant, an epoxy end-capped poly (poly () present in an amount of 0-10% by weight. Nonionic surfactants, including oxyalkylated) alcohols or amine oxide surfactants; phosphate builders (eg mono-phosphates, di-phosphates, tripolyphosphates, other oligomeric polyphosphates in the range of 5-60% , Sodium tripolyphosphate-STPP) and phosphate-free builders (eg, in the range of 0.5 wt% to 50 wt%, amino acid compounds such as methyl-glycine-diacetic acid (MGDA) and their salts and derivatives , Glutamine-N, N-diacetic acid (GLDA) and the same Salts and derivatives thereof, iminodisuccinic acid (IDS) and salts and derivatives thereof, carboxymethylinulin and salts and derivatives thereof, nitrilotriacetic acid (NTA), diethylenetriaminepentaacetic acid (DTPA), B-alanine diacetate ( B-ADA) and salts thereof, homopolymers and copolymers of poly-carboxylic acids and partially or fully neutralized salts thereof, monomeric polycarboxylic acids and hydroxycarboxylic acids, and salts thereof) Sulphonated / carboxylated polymers in the range of about 0.1% to about 50% by weight, providing dimensional stability; drying aids in the range of about 0.1% to about 10% by weight (eg polyesters, in particular An anionic polyester, optionally having from 3 to 6 functional groups (typically acids leading to polycondensation, Having together further monomers having (alcohol or ester functional groups), polycarbonate-, polyurethane- and / or polyurea-polyorganosiloxane compounds, or precursors thereof, in particular reactive cyclic carbonate and urea type Silicates (including sodium or potassium silicates such as sodium disilicate, sodium metasilicate, and crystalline phyllosilicates); inorganic bleaches (eg Perhydrate salts such as perborate, percarbonate, perphosphate, persulfate, and persilicate) and organic bleaches (eg, diperoxide decanedioic acid, diperoxytetradecanedioic acid) , And organic peroxyacids, including diacyl peroxide and tetraacyl peroxide, such as diperoxyhexadecanedioic acid)); bleach activation (Ie, organic peracid precursors ranging from about 0.1% to about 10% by weight); bleaching catalysts (eg, manganese triazacyclononane and related complexes, Co, Cu, Mn, and Fe bispyridylamine and related Complexes, and pentamineacetate cobalt (III) and related complexes); metal care agents in the range of about 0.1% to 5% by weight (eg, benzatriazoles, metal salts and complexes, and / or silicic acid) Salt); enzymes having an active enzyme range of about 0.01 to 5.0 mg per gram of automatic dishwashing detergent composition (eg, protease, amylase, lipase, cellulase, choline oxidase, peroxidase / oxidase, pectate lyase, mannanase, Cutinase, laccase, phospholipase, lysophospholipase, acyl transfer Over Ze, Peruhidoraze, aryl esterase, and mixtures thereof); and includes an enzyme stabilizer component (e.g., oligosaccharides, polysaccharides, and inorganic divalent metal salts), the.

Additional Detergent Compositions Additional exemplary detergent formulations to which any of a variety of suitable enzymes can be added in the granule composition are described below in the numbered section.
1) from about 7% to about 12% linear alkyl benzene sulfonate (calculated as acid) having a bulk density of at least 600 g / L; alcohol ethoxy sulfate (eg C _12-18 alcohol, 1-2 ethylene oxide ( EO)) or alkyl sulfates (eg C _16-18 ) from about 1% to about 4%; alcohol ethoxylates (eg C _14-15 alcohols, 7 EO) from about 5% to about 9%; About 14% to about 20% sodium (eg, Na ₂ CO ₃ ); about 2 to about 6% soluble silicate (eg, Na ₂ O, 2SiO ₂ ); about 15% zeolite (eg, NaAlSiO ₄ ) % to about 22%; sodium sulfate (e.g., _Na 2 SO ₄₎ 0% to about 6%; sodium citrate / citric acid _(e.g., C ₆ H 5 Na _{O 7 / C 6 H 8 O} 7) from about 0% to about 15%; sodium perborate (e.g., NaBO ₃ H ₂ O) of about 11% to about 18%; TAED about 2% to about 6% Carboxymethylcellulose (CMC) from 0% to about 2%; polymer (eg male / acrylic acid, copolymer, PVP, PEG) from 0 to 3%; enzyme (calculated as pure enzyme) from 0.0001 to 0.1 % Detergent; and 0-5% of a minor component (e.g., foam suppressant, fragrance, optical brightener, photobleach), formulated as a granule.
2) from about 6% to about 11% linear alkylbenzene sulfonate (calculated as acid) having a bulk density of at least 600 g / L; alcohol ethoxy sulfate (eg C _12-18 alcohol, 1-2 EO) Or from about 1% to about 3% alkyl sulfate (eg C _16-18 ); from about 5% to about 9% alcohol ethoxylate (eg C _14-15 alcohol, 7 EO); sodium carbonate (eg Na ₂ CO ₃ ) from about 15% to about 21%; soluble silicate (eg, Na ₂ O, 2SiO ₂ ) from about 1% to about 4%; zeolite (eg, NaAlSiO ₄ ) from about 24% to About 34%; sodium sulfate (eg Na ₂ SO ₄ ) about 4% to about 10%; sodium citrate / citric acid (eg C ₆ H ₅ Na ₃ O ₇ / C ₆ H ₈ O ₇ ) from 0% to about 15%; carboxymethylcellulose (CMC) from 0% to about 2%; polymer (eg male / acrylic acid copolymer, PVP, PEG) from 1 to 6%; enzyme (pure enzyme A detergent composition formulated as a granule comprising 0.0001 to 0.1% calculated as protein); 0 to 5% minor components (e.g., foam suppressants, perfumes).
3) having a bulk density of at least 600 g / L and about 5% to about 9% linear alkylbenzene sulfonate (calculated as acid); about alcohol ethoxylate (eg C _12-15 alcohol, 7 EO) 7% to about 14%; soap as fatty acid _{(e.g., C 16 to 22} fatty acid) about 1 to about 3%; about 10% to about 17% sodium carbonate (as _Na 2 CO _3); soluble silicate ( For example, Na ₂ O, 2SiO ₂ ) from about 3% to about 9%; zeolite (as NaAlSiO ₄ ) from about 23% to about 33%; sodium sulfate (eg, Na ₂ SO ₄ ) from 0% to about 4% ; sodium perborate (e.g., NaBO ₃ H ₂ O) from about 8% to about 16%; TAED about 2% to about 8%; phosphonate (e.g., EDTMPA) 0% to about 1%; carboxymethyl Rulose (CMC) from 0% to about 2%; polymer (eg male / acrylic acid copolymer, PVP, PEG) from 0 to 3%; enzyme (calculated as pure enzyme protein) from 0.0001 to 0.1%; A detergent composition formulated as a granule containing 0 to 5% of a minor component (for example, a foam inhibitor, a fragrance, or a fluorescent brightener).
4) having a bulk density of at least 600 g / L, about 8% to about 12% linear alkyl benzene sulfonate (calculated as acid); about alcohol ethoxylate (eg C _12-15 alcohol, 7 EO) 10% to about 25%; from about 14% to about 22% sodium carbonate (as _Na 2 CO _3); soluble silicate _(e.g., Na _{2 O,} 2SiO 2) from about 1% to about 5%; zeolite ( For example, NaAlSiO ₄ ) from about 25% to about 35%; sodium sulfate (eg, Na ₂ SO ₄ ) from 0% to about 10%; carboxymethylcellulose (CMC) from 0% to about 2%; polymer (eg, malein / Acrylic acid copolymer, PVP, PEG) 1-3%; enzyme (calculated as pure enzyme protein) 0.0001-0.1%; and minor components (eg foam Control agents, perfumes) and containing 0 to 5%, the detergent composition formulated as a granulate.
5) about 15% to about 21% linear alkyl benzene sulfonate (calculated as acid); about alcohol ethoxylate (eg C _12-15 alcohol, 7 EO or C _12-15 alcohol, 5 EO) 12% to about 18%; about 3% to about 13% soap (eg, oleic acid) as a fatty acid; 0% to about 13% alkenyl succinic acid (C _12-14 ); about 8% to about 13% aminoethanol 18%; citric acid about 2% to about 8%; phosphonate 0% to about 3%; polymer (eg, PVP, PEG) 0% to about 3%; borate (eg B ₄ O ₇ ) 0 % To about 2%; ethanol from 0% to about 3%; propylene glycol from about 8% to about 14%; enzyme (calculated as pure enzyme protein) from 0.0001 to 0.1%; and minor components (eg, , Dispersant, foam suppression Agents, perfumes, fluorescent whitening agents) 0-5% containing, aqueous liquid detergent compositions.
6) about 15% to about 21% linear alkyl benzene sulfonate (calculated as acid); alcohol ethoxylate (eg C _12-15 alcohol, 7 EO, or C _12-15 alcohol, 5 EO) About 3% to about 10% soap (eg oleic acid) as fatty acid; about 14% to about 22% zeolite (as NaAlSiO ₄ ); about 9% to about 18% potassium citrate; Borate (eg, B ₄ O ₇ ) from 0% to about 2%; Carboxymethylcellulose (CMC) from 0% to about 2%; Polymer (eg, PEG, PVP) from 0% to about 3%; Anchor polymer (eg, Lauryl methacrylate / acrylic acid copolymer; molar ratio 25: 1, MW 3800) from 0% to about 3%; glycerol from 0% to about 5%; enzyme (pure enzyme tamper) Aqueous structured liquid detergent composition comprising 0.0001-0.1%; calculated as quality); and 0-5% of minor components (eg, dispersants, foam inhibitors, fragrances, fluorescent brighteners) object.
7) having a bulk density of at least 600 g / L, about 5% to about 10% fatty alcohol sulfate; about 3% to about 9% ethoxylated fatty acid monoethanolamide; 0-3% soap as a fatty acid; About 5% to about 10% sodium carbonate (eg Na ₂ CO ₃ ); about 1% to about 4% soluble silicate (eg Na ₂ O, 2SiO ₂ ); zeolite (eg NaAlSiO ₄ ) About 20% to about 40%; sodium sulfate (eg, Na ₂ SO ₄ ) about 2% to about 8%; sodium perborate (eg, NaBO ₃ H ₂ O) about 12% to about 18%; TAED From about 2% to about 7%; from about 1% to about 5% of a polymer (eg, malein / acrylic acid copolymer, PEG); from 0.0001 to 0.1% of an enzyme (calculated as pure enzyme protein); and Trace components For example, optical brighteners, suds suppressors, perfume) and containing 0 to 5%, the detergent composition formulated as a granulate.
8) about 8% to about 14% linear alkyl benzene sulfonate (calculated as acid); about 5% to about 11% ethoxylated fatty acid monoethanolamide; 0% to about 3% soap as fatty acid; sodium carbonate (eg, , _Na 2 CO ₃₎ from about 4% to about 10%; soluble silicate _(Na 2 O, from about 1% to about 4% 2SiO _2); zeolites (e.g., NaAlSiO ₄₎ from about 30% to about 50 About 3% to about 11% sodium sulfate (eg Na ₂ SO ₄ ); about 5% to about 12% sodium citrate (eg C ₆ H ₅ Na ₃ O ₇ ); polymer (eg PVP) , Maleic / acrylic acid copolymer, PEG) from about 1% to about 5%; enzyme (calculated as pure enzyme protein) from 0.0001 to 0.1%; and minor components (eg, foam inhibitors, perfumes) 0-5 %, A detergent composition formulated as granules.
9) about 6% to about 12% linear alkyl benzene sulfonate (calculated as acid); about 1% to about 4% nonionic surfactant; about 2% to about 6% soap as fatty acid; sodium carbonate ( For example, Na ₂ CO ₃ ) from about 14% to about 22%; zeolite (eg, NaAlSiO ₄ ) from about 18% to about 32%; sodium sulfate (eg, Na ₂ SO ₄ ) from about 5% to about 20%. Sodium citrate (eg, C ₆ H ₅ Na ₃ O ₇ ) from about 3% to about 8%; sodium perborate (eg, NaBO ₃ H ₂ O) from about 4% to about 9%; bleach activation About 1% to about 5% of an agent (eg, NOBS or TAED); 0% to about 2% of carboxymethylcellulose (CMC); about 1% to about 5% of a polymer (eg, polycarboxylate or PEG); enzyme (Pure enzyme tamper A detergent composition formulated as a granule comprising 0.0001 to 0.1% calculated as the quality of the product; and 0 to 5% of minor components (e.g., optical brightener, fragrance).
10) about 15% to about 23% linear alkyl benzene sulfonate (calculated as acid); about 8% to about 15% alcohol ethoxy sulfate (e.g. _C12-15 alcohol, 2-3 EO); alcohol ethoxy About 3% to about 9% of a rate (eg, C _12-15 alcohol, 7 EO, or C _12-15 alcohol, 5 EO); 0% to about 9% soap (eg, lauric acid) as a fatty acid About 1% to about 5% aminoethanol; about 5% to about 10% sodium citrate; about 2% to about 6% hydrotrope (eg, sodium toluenesulfonate); borate (eg, B ₄ the O ₇₎ 0% to about 2%; carboxymethylcellulose 0% to about 1%; ethanol about 1% to about 3%; propylene glycol about 2% to about 5%; enzymes ( Aqueous liquid detergent composition comprising 0.0001-0.1%; calculated as pure enzyme protein); and 0-5% of minor components (eg, polymer, dispersant, fragrance, fluorescent brightener).
11) about 20% to about 32% linear alkyl benzene sulfonate (calculated as acid); alcohol ethoxylate (eg C _12-15 alcohol, 7 EO, or C _12-15 alcohol, 5 EO) 6-12%; aminoethanol from about 2% to about 6%; citric acid from about 8% to about 14%; borate (eg B ₄ O ₇ ) from about 1% to about 3%; polymer (eg malee / Acrylic acid copolymer, anchor polymer such as lauryl methacrylate / acrylic acid copolymer, etc.) 0% to about 3%; glycerol about 3% to about 8%; enzyme (calculated as pure enzyme protein) 0.0001-0 0.1%; and 0-5% of minor components (e.g., hydrotropes, dispersants, fragrances, optical brighteners).
12) Anionic surfactant (linear alkylbenzene sulfonate, alkyl sulfate, α-olefin sulfonate, α-sulfo fatty acid methyl ester, alkane sulfonate, soap) having a bulk density of at least 600 g / L and from about 25% to about 40%; about 1% to about 10% nonionic surfactant (eg, alcohol ethoxylate); about 8% to about 25% sodium carbonate (eg, Na ₂ CO ₃ ); soluble silicate (eg, Na ₂ O, 2SiO ₂ ) from about 5% to about 15%; sodium sulfate (eg, Na ₂ SO ₄ ) from 0% to about 5%; zeolite (NaAlSiO ₄ ) from about 15% to about 28%; sodium borate (e.g., NaBO ₃ ^· 4H ₂ O) 0% to about 20%; bleach activator (TAED or NOBS) about 0% to about 5 ; Enzyme (calculated as pure enzyme protein) from .0001 to 0.1%; minor components (e.g., perfumes, fluorescent whitening agents) 0-3% of, including, detergent compositions formulated as granules.
13) The detergent composition according to the above compositions 1) to 12), wherein all or part of the linear alkyl benzene sulfonate is replaced with (C ₁₂ -C ₁₈ ) alkyl sulfate.
14) having a bulk density of at least 600 g / L and having from about 9% to about 15% (C ₁₂ -C ₁₈ ) alkyl sulfate; from about 3% to about 6% alcohol ethoxylate; from about 3% to about 6% polyhydroxyalkyl fatty acid amide 1% to about 5%; zeolite (eg NaAlSiO ₄ ) about 10% to about 20%; layered disilicate (eg Hoechst SK56) about 10% to about 20%; sodium carbonate (eg Na ₂ CO ₃ ) from about 3% to about 12%; soluble silicates (eg, Na ₂ O, 2SiO ₂ ) from 0% to about 6%; sodium citrate from about 4% to about 8%; sodium percarbonate About 13% to about 22%; TAED about 3% to about 8%; polymer (eg, polycarboxylate and PVP) 0% to about 5%; enzyme (calculated as pure enzyme protein) 0.0 01 to 0.1%; and minor components (e.g., optical brightener, photobleach, perfume, suds suppressors) 0-5% containing, detergent compositions formulated as granules.
15) having a bulk density of at least 600 g / L, about 4% to about 8% (C ₁₂ -C ₁₈ ) alkyl sulfate; about 11% to about 15% alcohol ethoxylate; about 1% to about 15% soap 4%; about 35% to about 45% of zeolite MAP or zeolite A; about 2% to about 8% of sodium carbonate (as Na ₂ CO ₃ ); soluble silicate (eg, Na ₂ O, 2SiO ₂ ) 0% to about 4%; sodium percarbonate from about 13% to about 22%; TAED from 1 to 8%; carboxymethylcellulose (CMC) from 0% to about 3%; polymers (eg, polycarboxylates and PVP). From 0% to about 3%; from 0.0001 to 0.1% enzyme (calculated as pure enzyme protein); and from 0 to 3% minor components (eg, optical brightener, phosphonate, fragrance), As granules Formulated detergent composition.
16) Detergent formulations according to 1) to 15) above, containing a stabilized or encapsulated peracid as an additional component or as an alternative to the already defined bleach system.
17) The detergent composition according to 1), 3), 7), 9) and 12) above, wherein the perborate is replaced by percarbonate.
18) The detergent composition according to 1), 3), 7), 9), 12), 14), and 15) additionally containing a manganese catalyst. The manganese catalyst is, for example, one of the compounds described in “Efficient manganese catalysts for low-temperature bleaching”, Nature 369: 637-639 (1994).
19) As a non-aqueous detergent solution comprising a liquid nonionic surfactant such as, for example, a linear alkoxylated primary alcohol, a builder system (eg, phosphate), an enzyme (s), and an alkali. A detergent composition to be formulated. The detergent may also contain an anionic surfactant and / or a bleach system.

  As noted above, the enzyme may be included at a concentration commonly used in detergents. At present, in detergent compositions, it is contemplated that the enzyme may be added in an amount corresponding to 0.00001-1.0 mg (calculated as pure enzyme protein) of enzyme polypeptide per liter of wash solution.

  Detergent compositions include other conventional detergent ingredients such as peptizers, fillers, foam suppressors, anticorrosives, soil suspending agents, sequestering agents, soil re-adhesion agents, dehydrating agents, dyes, bactericides. Agents, fluorescent agents, thickeners, and fragrances may be included.

  The detergent composition comprises a laundry additive composition suitable for pre-treatment of a stained fabric and a fabric softener composition to be added to the rinsing liquid for hand washing (manual) or washing machine (automatic) laundry detergent It may be formulated as a composition, or it may be formulated as a detergent composition for use in a general household hard surface cleaning operation, or it may be formulated for dishwashing operations by hand or dishwasher.

  Any cleaning composition described herein may comprise any number of additional enzymes. In general, the enzyme must be compatible with the selected detergent (eg, for optimum pH, compatibility with other enzyme components and non-enzyme components, etc.), and the enzyme must not be present in an effective amount. must not. The following enzymes are described as examples.

  Proteases: Suitable proteases include those of animal, plant or microbial origin. Mutants that are chemically modified or subjected to protein manipulation, as well as naturally processed proteins are included. The protease may be a serine protease or metalloprotease, alkaline microbial protease, trypsin-like protease, or chymotrypsin-like protease. Examples of alkaline proteases are, for example, subtilisins from Bacillus, for example, subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147, and subtilisin 168 (see, for example, WO 89/06279). Examples of trypsin-like proteases are trypsin (eg from porcine or bovine) and Fusarium protease (see eg WO 89/06270 and 94/25583). Further useful proteases include, but are not limited to, the variants described in WO 92/19729, WO 98/2015, WO 98/2016, and WO 98/34946. . Commercially available protease enzymes include ALCALASE (R), SAVINASE (R), PRIMASE (TM), DURAASE (TM), ESPERASE (R), KANNASE (TM), and BLAZE (TM) (Novo Nordisk A / S) And MAXOVASE (R), MAXACAL (TM), MAXAPEM (TM), PROPERASE (R), PURAFECT (R), PURAFECT OXP (TM), FN2 (TM), and FN3 (TM) ) (Danisco US Inc.), but is not limited thereto. Other representative proteases include NprE derived from Bacillus amyloliquefaciens and ASP derived from the 69B4 system of Cellulomonas species.

  Lipases: Suitable lipases include those derived from bacteria or fungi. Variants that are chemically modified, proteolytically modified, or subjected to protein manipulation are included. Examples of useful lipases include lipases from Humicola (also known as Thermomyces), such as H. derived from T. lanuginosa (see, for example, European Patent Nos. 258068 and 305216). from insolens (see, eg, WO 96/13580); Pseudomonas lipase (eg, P. alcaligenes or P. pseudoalcaligenes; see, eg, European Patent No. 218272); cepacia (see, for example, EP 331 376), p. stutzeri (see, for example, British Patent No. 1,372,034), P.A. fluorescens, Pseudomonas sp. SD705 series (see, for example, International Publication Nos. 95/06720 and 96/27002); Wisconsinensis (see, eg, WO 96/12012); Bacillus lipase (eg, from B. subtilis; see, eg, Dartoise et al. Biochemica et Biophysica Acta, 1131: 253-360 (1993)), B. et al. stearothermophilus (see, for example, JP-A-64 / 744992) or B.I. pumilus (see, for example, WO 91/16422), but is not limited thereto. Additional lipase variants intended for use in the formulations include, for example, WO 92/05249, 94/01541, 95/35381, 96/00292, 95. No. / 30744, No. 94/25578, No. 95/14783, No. 95/22615, No. 97/04079, No. 97/07202, EP No. 407225, and No. 260105. The thing described in is mentioned. Some commercially available lipase enzymes include LIPOLASE® and LIPOLASE ULTRA ™ (Novo Nordisk A / S and Novozymes A / S).

  Polyesterases: Suitable polyesterases may be included in the composition, such as those described, for example, in WO 01/34899, 01/14629, and US Pat. No. 6,933,140.

  Amylase: The composition may be combined with an amylase, such as a non-production enhanced amylase. These include STAINZYME (R), NATALASE (R), DURAMYL (R), TERMAMYL (R), FUNGAMYL (R) and BAN (R) (Novo Nordisk A / S and Novozymes A / S). May include commercially available amylases such as, but not limited to, RAPIDASE®, POWERASE®, and PURASTAR® (Danisco US Inc.);

  Cellulase: Cellulase can be added to the composition. Suitable cellulases include those derived from bacteria or fungi. Variants that are chemically modified or subjected to protein manipulation are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, such as Humicola insolens, Mycellophthora thermophila, No. 7 from the United States No. 5,648,263, No. 5,691,178, No. 5,776,757, and WO 89/09259). Exemplary cellulases intended for use are those that have fiber color treatment benefits. Examples of such cellulases are, for example, the cellulases described in European Patent Nos. 0495257, 0531372, WO 96/11262, 96/29397, and 98/08940. Other examples are WO 94/07998, 98/12307, 95/24471, International Application PCT / DK98 / 00299, EP 531315, US Pat. No. 5,457,046. No. 5,686,593, and 5,763,254, cellulase variants. Commercial cellulases include CELLUZYME® and CAREZYME® (Novo Nordisk A / S and Novozymes A / S); and PURADAX HA® (Danisco US Inc.); and KAC-500 (B ) (Trademark) (Kao Corporation).

  Peroxidase / oxidase: Suitable peroxidases / oxidases intended for use in the composition include those derived from plants, bacteria, or fungi. Variants that are chemically modified or subjected to protein manipulation are included. Examples of useful peroxidases include those derived from Coprinus, such as C.I. cinereus-derived peroxidase and variants thereof such as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include, for example, GUARDZYME (trademark) (NOVO NORDISK A / S and NOVozymes A / S).

  The detergent composition may comprise 2,6-β-D-fructan hydrolase effective to remove / clean biofilm present in textile / laundry at home and / or factory.

  Detergent enzyme (s) can be prepared by adding separate additives containing one or more enzymes, or by adding a mixed additive containing all of these enzymes. It may be included in the composition. Detergent additives, i.e. separate or mixed additives, may be formulated, for example, as granules, liquids, slurries and the like. Exemplary detergent additive formulations include, but are not limited to, granules, especially non-dusty granules, liquids, particularly stabilizing liquids, or slurries.

  For example, as disclosed in U.S. Pat. Nos. 4,106,991 and 4,661,452, low dust granules can be made and added to the granule composition, as is known in the art. It can be arbitrarily coated by the method. Examples of waxy coating materials are poly (ethylene oxide) products (eg, polyethylene glycol, PEG) having an average molar weight of 1,000 to 20,000; ethoxylated nonylphenol having 16 to 50 ethylene oxide units; Ethoxylated fatty alcohols containing 12 to 20 carbon atoms and having 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. An example of a film-forming coating material suitable for application by the fluidized bed method is found, for example, in British Patent No. 14835991. Liquid enzyme preparations may be stabilized, for example, by adding polyols such as propylene glycol, sugars or sugar alcohols, lactic acid or boric acid by established methods.

  The detergent composition may be in any convenient form, for example, a bar, tablet, powder, granule, paste, or liquid. Liquid detergents may be aqueous, typically comprising up to about 70% water and 0% to about 30% organic solvent. Compact detergent gels containing up to about 30% water are also contemplated. The detergent composition optionally includes one or more surfactants that may be non-ionic, including semipolar, and / or anionic, and / or cationic, and / or zwitterionic. It's okay. Surfactants may be present in a wide range from about 0.1% to about 60% by weight.

  When included, detergents typically contain from about 1% to about 40% anionic surfactant, such as linear alkyl benzene sulfonate, alpha-olefin sulfonate, alkyl sulfate (aliphatic alcohol sulfate), alcohol ethoxy sulfate. Secondary alkane sulfonates, α-sulfo fatty acid methyl esters, alkyl- or alkenyl succinic acids, or soaps.

  When included, detergents typically contain from about 0.2% to about 40% nonionic surfactants such as alcohol ethoxylates, nonylphenol ethoxylates, alkyl polyglycosides, alkyl dimethylamine oxides, ethoxylated fatty acid mono Contains N-acyl-N-alkyl derivatives of ethanolamide, fatty acid monoethanolamide, polyhydroxyalkyl fatty acid amide, or glucosamine ("glucamide").

  Detergents are 0% to about 65% detergent builders or complexing agents such as zeolites, diphosphates, triphosphates, phosphonates, carbonates, citrates, nitrilotriacetic acid, ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid, alkyl- Or alkenyl succinic acid, soluble silicates or layered silicates (eg Hoechst SKS-6).

  The detergent may contain one or more polymers. Representative polymers include carboxymethyl cellulose (CMC), poly (vinyl pyrrolidone) (PVP), poly (ethylene glycol) (PEG), poly (vinyl alcohol) (PVA), poly (vinyl pyridine-N-oxide), poly (Vinyl imidazole), polycarboxylates such as polyacrylates, malee / acrylic acid copolymers, and lauryl methacrylate / acrylic acid copolymers.

  The enzyme of the detergent composition can be a conventional stabilizer, such as a polyol (eg, propylene glycol or glycerol), sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative (eg, an aromatic borate ester), or Phenylboronic acid derivatives (eg 4-formylphenylboronic acid) may be used for stabilization. The composition may be formulated as described in WO 92/19709 and 92/19708.

  In enzyme-containing detergent compositions, about 0.01 to about 100 mg of enzyme protein per liter of cleaning solution (e.g., about 0.05 to about 5.0 mg of enzyme protein per liter of cleaning solution, or 0.1 to 0.1 per liter of cleaning solution). It is contemplated that it can be added in an amount equivalent to about 1.0 mg enzyme protein).

  Although the present compositions and methods are described in detail below, it will be understood that various modifications may be made.

  Many enzyme wash assays are known in the art, such as test strips and test strip strip assays.

Brewing Composition The granule composition may be a component of a brewing composition used in a process for providing a fermented beverage, such as beer brewing. Non-fermentable carbohydrates are believed to form the majority of the solids dissolved in the final beer. This residue remains because malt amylase cannot hydrolyze the α-1,6-linkage of starch. Non-fermentable carbohydrates yield about 50 calories per about 340 grams (12 ounces) of beer. The granule composition is usually combined with glucoamylase, and optionally with pullulanase and / or isoamylase, to convert starch into dextrin and fermentable sugar, reducing non-fermentable carbohydrates remaining in the final beer. To help.

  The main raw materials used in the production of these beverages are water, hops and malt. In addition, only in the following, auxiliary ingredients such as common corn grits, refined corn grits, ground beer yeast, rice, sorghum, refined corn starch, barley, barley starch, threshed barley, wheat, Starches such as wheat starch, dried cereals, cereal flakes, rye, oats, potatoes, tapioca, and syrups such as corn syrup, sugarcane syrup, invert sugar syrup, barley and / or wheat syrup, and the like Can be used as a source.

  For many reasons, malt produced primarily from a variety of selected barley has a significant impact on the overall characteristics and quality of beer. First, malt is the main flavor of beer. Secondly, malt provides the bulk of the fermentable sugar. Third, the malt supplies protein that contributes to the body and foam characteristics of the beer. Fourth, malt provides the necessary enzyme activity during wheat grinding. Hops also contribute greatly to the quality of flavors and other beers. In particular, hops (or hop ingredients) add desirable bitter substances to beer. In addition, hops can act as protein precipitants, provide antiseptic properties, and help foam formation and stabilization.

  Cereal grains, such as barley, oats, wheat, and corn and rice are often used in beer brewing, both in industrial and home brewing, but other plant components such as hops Are often added. The constituents used for beer brewing may not be malted or may be malted, i.e. partially germinated, resulting in an increase in the amount of enzymes such as [alpha] -amylase. Successful beer brewing requires an appropriate amount of α-amylase enzyme activity to ensure an adequate sugar level for fermentation. This granule composition may also be added to the ingredients used for beer brewing.

  As used herein, the term “stock” means grains and plant components that are ground or crushed. For example, barley used in beer production is a grain that is coarsely ground, i.e. ground, and provides a suitable consistency for the production of ground wheat for fermentation. As used herein, the term “stock” includes any plant and kernel of the above types in a crushed or coarsely ground form. The methods described herein can be used to measure α-amylase activity levels in both flour and stock.

  The process for producing beer is well known in the art. See, for example, Wolfgang Kunze (2004) “Technology Brewing and Malting”, Research and Teaching Institute of Brewing, Berlin (VLB), 3rd edition. Briefly, this process consists of (a) preparing ground wheat, (b) filtering ground wheat to prepare wort, and (c) fermenting wort to beer, etc. Obtaining a fermented beverage. Typically, milled or pulverized malt, malt and secondary ingredients, or auxiliary ingredients are mixed with water and held at a controlled temperature for a period of time, depending on the enzymes present in the malt and / or auxiliary ingredients, Convert starch present in the malt to fermentable sugar. The ground wheat is then transferred to a ground wheat filter to separate the liquid from the grain residue. This sweet liquid is called “wort” and the remaining grain residue is called “beer lees”. The ground wheat is typically subjected to an extraction process that includes adding water to the ground wheat to recover the remaining soluble extract from the beer lees. The wort is then boiled vigorously to sterilize the wort and promote the formation of color, flavor and aroma. Add hops at some point during boiling. Cool the wort and transfer to the fermenter.

  Subsequently, the wort is contacted with the yeast in the fermenter. The fermentation tank may be cooled to stop the fermentation. Remove yeast that can agglutinate. Finally, the beer is cooled and clarified and stored for a period of time while flavoring occurs, precipitating all materials that may impair the appearance, flavor, and shelf life of the beer. Beer typically contains about 2% to about 10% v / v alcohol, although higher alcohol content, eg, 18% v / v beer can also be obtained. Prior to packaging, carbonated beer is added to the beer and, if desired, sterilized with bass.

  Brewing compositions comprising α-amylase (often but not necessarily combined with one or more exogenous enzymes such as glucoamylase, pullulanase and / or isoamylase, and any combination thereof) The product can be added to the ground wheat during the above step (a), ie the preparation of ground wheat. Alternatively or additionally, the brewing composition can be added to the ground wheat during the above step (b), for example during filtration of the ground wheat. Alternatively or additionally, the brewing composition can be added to the wort during step (c), eg, fermentation of the wort.

  Certain embodiments relate to any of the above uses, methods, or fermented beverages, wherein such fermented beverages are beer, eg, all-malt beer, beer brewed under “Reinheitsgebot”, ale , IPA, lager, bitter, sparkling liquor (second beer), third beer, dry beer, beer-taste beverage, calorie light beer, low alcohol beer, low calorie beer, porter, bock beer, stout, malt liquor, non Alcoholic beer, non-alcoholic malt liquor, etc., but also other cereals and malt beverages, eg fruity malt beverages, eg citrus tastes such as lemon, orange, lime, eg berry flavored malt beverages, liquor Flavored malt beverages, such as vodka, rum, or tequila-flavored malt liquor, or Hi flavored malt beverages, for example, is also the like Morutorika of caffeine taste.

Additional Animal Feed Embodiments Particularly in animal feed applications, in some embodiments, the granules of the present teachings can be used with any of a variety of at least one of the following enzymes.

  By way of example only, a chicken, for example a broiler chicken feed, may comprise one or more ingredients listed in the table below, for example in the proportions in the table below.

  By way of example only, feed standards for chickens such as broiler chickens may be set as shown in the table below.

  By way of example only, a laying hen's feed may include one or more ingredients listed in the table below, for example in the proportions in the table below.

  As an example only, feed standards for laying hens may be set as shown in the table below.

  By way of example only, turkey feed may include one or more ingredients listed in the table below, for example, in the proportions in the table below.

  As an example only, feed standards for turkeys may be set as shown in the table below.

  By way of example only, a small pig feed can include one or more ingredients listed in the table below, for example, in the proportions in the table below.

  As an example only, feed standards for small pigs may be set as shown in the table below.

  By way of example only, a growing / fattening pig feed can include one or more ingredients listed in the table below, for example, in the proportions shown in the table below.

  As an example only, feed standards for growing / fattening pigs may be set as shown in the table below.

Feed Administration The feed additive composition according to the present invention may be designed for a single dose or may be designed for a daily feed.

  The optimal amount of composition (and each component included) used in the combination of the present invention will depend on the product being treated and / or the method of contacting the product with the composition and / or its intended use. Determined.

  The amount of enzyme used in the composition must be sufficient to be effective and to maintain the effect of improving the performance of the feed product containing the composition that the animal ate. This time of effectiveness must extend at least to the time of use of the product (eg, feed additive composition or feed containing it).

Combinations with other components in feed applications The enzymes described herein may be used in combination with other components.

  The component may be a prebiotic. Prebiotics are typically non-digestible carbohydrates (oligo- or polysaccharides) or sugar alcohols that are not degraded or absorbed in the upper gastrointestinal tract. Known prebiotics used in commercial products and useful in accordance with the present invention include inulin (fructooligosaccharide, or FOS) and transgalactooligosaccharide (GOS or TOS). Suitable prebiotics include palatinose oligosaccharide, soy oligosaccharide, alginic acid, xanthan, pectin, locust bean gum (LBG), inulin, guar gum, galactooligosaccharide (GOS), fructooligosaccharide (FOS), non-degradable starch, lacto Saccharose, lactulose, lactitol, maltitol, maltodextrin, polydextrose (ie, Litesse®), lactitol, lactosucrose, soybean oligosaccharide, palatinose, isomaltoligosaccharide, glucooligosaccharide, and xylooligosaccharide.

  The prebiotic may be simultaneously (eg, mixed together or administered simultaneously from the same or different route) or sequentially (eg, the same) the feed additive composition (or component thereof) according to the present invention. (Or by different routes).

  Other components of the combination of the present invention include polydextrose, such as Litesese® and / or maltodextrin and / or lactitol. These other components may optionally be added to the feed additive composition to aid in the drying process.

  As further examples of other suitable components, one or more thickeners, gelling agents, emulsifiers, binders, crystal modifiers, sweeteners (including artificial sweeteners), rheology modifiers, stable Agents, antioxidants, dyes, enzymes, carriers, media, excipients, diluents, lubricants, flavoring agents, coloring substances, suspending agents, disintegrating agents, particle binders and the like. These other components may be natural. These other components may be prepared using chemical and / or enzymatic techniques.

  In one preferred embodiment, the enzyme used in the present invention can be used in combination with one or more lipids.

  For example, the enzyme used in the present invention can be used in combination with one or more lipid micelles. The lipid micelle may be a single lipid micelle or a complex lipid micelle.

  Lipid micelles may be aggregates of molecules oriented with amphiphiles such as lipids and / or oils.

  The present teachings further provide a method of increasing the subject's weight gain, comprising providing a feed comprising a feed additive composition according to the invention of a subject, eg, a poultry or pig.

  The present invention can be further understood by reference to the following examples, which are provided by way of illustration and are not intended to be limiting.

Example 1
Sodium Sulfate Core Size Distribution and Smoothness Index Seven samples of anhydrous crystalline sodium sulfate core particles were obtained from two suppliers, Minera de Santa Marta (Villarubio, Spain) and Saltex (Forth Worth, Texas).

The sample particle size distribution was obtained by laser light scattering using a Malvern Mastersizer 2000 laser diffraction particle size analyzer. The skin specific surface area of these particle size distributions was calculated using the true density of anhydrous sodium sulfate (2.664 g / cm ³ ) using the algorithm described in the method section. BET specific surface area was measured using the Micromeritics model ASAP 2420 Accelerated Porosity and Surface Area System as described in the Methods section. The smoothness index for each sample is calculated as the ratio of these two specific surface areas. A representative image of two lots of cores is shown in FIG.

(Example 2)
Preparation of detergent enzyme granule sample using sodium sulfate core 79.8 kg of Minera de Santa Marta sodium sulfate core (MSM lot # 3 in Table 1 of Example 1) into a pilot scale fluidized bed coater with a batch size of 150 kg. I put it in. According to the light scattering method, the core has a mass median diameter (D ₅₀ ) of 258 micrometers, D10 of 182 micrometers, and D90 of 358 micrometers, and sieving techniques have a D _{50 of} 210 micrometers. Had. Based on this, MSM lot # 3 had a PSDI of 362/182 = 1.99.

  According to Table 1 of Example 1, the smoothness index of the core of MSM lot # 3 was 1.1, which was very close to 1.0, which is the smoothness index of completely smooth particles. An optical micrograph of the core, a scanning electron micrograph, is shown in FIG. It can be seen from the same figure that these cores are considerably smoother than the Saltex comparative core sample. Table 1 shows that the smoothness index of Saltex lot # 1 was 3.9, indicating a significant deviation from the perfect smoothness index of 1.0.

  The core was fluidized at a bed temperature of 41 ° C. and 1% w / w partially hydrolyzed polyvinyl alcohol (enzyme / PVA final solids% w / w amount of 16%) and 0.5% w / W defoamer (polyglycol EP 436E (lot 1L05091501), solid content 20% w / w concentration (3450 PU / g) aqueous protease enzyme solution (Purafast) from 3.5 (initial) to The core was sprayed in a 3.9 (final) bar atomizing air pressure gradient.

  After the enzyme spraying is complete, a solution containing a mixture of sodium sulfate and magnesium sulfate (MgSO4 7H2O, 30.5%, Na2SO4, 15%) is sprayed onto the core to give a net 20% w / w based on the final granule weight. w was delivered onto the core. The salt solution was sprayed with an atomizing air pressure of 45 ° C. bed temperature and 0.35 MPa (3.5 bar).

  The final coating solution consisting of partially hydrolyzed polyvinyl alcohol (Celvol 5-88), titanium dioxide, and Lutensol nonionic surfactant is sprayed onto the salt-coated enzyme core to yield a net 11% w / Delivered a total coating weight of w. The coating solution was sprayed at an initial atomization air pressure of 0.53 MPa (5.3 bar), reducing the bed temperature to 55 ° C. to 0.48 MPa (4.8 bar).

  After cooling the batch of coated granules, 150 kg of product was recovered from the fluid bed coater. The final granule had a D50 of 308 μm (sieving method) and a bulk density of 1.18 g / cm 3. The granule had a Hunter whiteness L value of 73 and a Heubach enzyme total dust of 3.2 mg / pad.

(Example 3)
According to the formulation and process described in Example 2, the amount of Purafast enzyme concentrate solution coated on the core, only the core particle size, was changed, and the core dose was adjusted as needed to accommodate different amounts of enzyme solids. Conditioned to prepare four additional batches of Purafast granules. Additional coating and process parameters were not changed.

  The following enzyme samples were subjected to a storage test in various “under stress” storage conditions in a laundry powder detergent. Stability was assessed by performance and biochemical analysis.

Storage test: sample preparation An open plastic cup (in the corresponding room), stored in an acclimatization room at 37, 45 and 60 ° C. with 70% relative humidity at the corresponding amount of enzyme (see below) 150 mL).

A. 10g laundry detergent + sample A1
B. 10g laundry detergent + sample B1
C. 10g laundry detergent + sample B2
D. 10g laundry detergent + sample C1
E. 10g laundry detergent + sample C2

  Samples were analyzed in the new state and after storage for 1 hour, 2 hours, and 3 days (60 ° C.) and after storage for 1, 3, and 8 days (37 and 45 ° C.).

Performance evaluation A so-called Launder-O-meter was subjected to a cleaning test at 30 C, 25 FH, and 15 minutes.

  Ten grams of the stored sample was dissolved in 2.5 liters of 25 ° FH water (see below) in a stirred beaker for 2 minutes. 300 mL of this solution was placed in a LOM beaker and the following stains were added to make the liquid to fabric ratio L / C to 90 (excluding steel balls).

To prepare 25 L of 25 ° FH = 250 ppm Ca ⁺² / Mg ⁺² = 2/1, 416.75 mL of 15.000 ppm stock solution was diluted with 24583.25 mL of deionized water (to 25 liters) and stock The solution 15.000 ppm is 14.70 grams CaCl2.2H2O 10.1065 grams MgCl2.6H2O in 1 liter DI water.

Stain per beaker (initial reflectance [L ^* a ^* b, D65 light source] of test cloth measured in advance with a reflectometer):

  After washing, the stain was rinsed with running tap water (17FH, Ca / Mg = 4/1) for 3 minutes, dehydrated and allowed to air dry overnight (covered with a black cloth) at ambient conditions.

Using the reflectometer, the final reflectance [L ^* a ^* b, D65 light source] of the test cloth piece was measured three times. The% Δ stain removal (% dE) is calculated according to the following formula:

式中、Ｌ_ｒｅｆ＝９６．０
ａ_ｒｅｆ＝０．５５
ｂ_ｒｅｆ＝１．９５

In the formula, L _ref = 96.0
a _ref = 0.55
b _ref = 1.95

Biochemical Evaluation This method was used to determine the proteolytic activity of Properase in fermentation, recovery, and final product samples (liquid and granules). This assay is a colorimetric assay and monitors the degradation rate of the N-succinyl-ala-ala-pro-phe-p-nitroanalide substrate. Substrate p-nitroanilide release was measured at 405 nm in a Konelab analyzer. The assay is calibrated against designated standards.

Sample preparation:
Tris buffer -100 g (0.1 M _{Tris, 0.01M CaCL 2, 0.005% Triton} X-100, pH 8.6) was added to 10g of the detergent sample and stirred for 30 minutes. Thereafter, 2 mL of the lysate was taken in an Eppendorf tube and centrifuged at 14000 rpm for 10 minutes.
-A second lysate (10X) was prepared using a HAMILTON diluter and Tris buffer.
-After dilution, the sample was vortexed and poured into the corresponding cuvette for Konelab. A control solution was also included (in these cases PU / g). The cuvette was placed in the sample rack. The rack was inserted into the instrument.

Performing the Konelab assay:
-Working substrate solution [N-succinyl-ala-ala-pro-phe-p-nitroanilide (AAPF) (Sigma # S7388)] was prepared, poured into a reagent container, and placed in a reagent installation part (substrate = 20 mL container, code = AAPF).

Reagent preparation Stock substrate solution (100 mg / mL): 500 mg of AAPF is dissolved in 5 mL of DMSO. Store in the dark at room temperature. Discard when the solution turns yellow. Stable for 1 month.
2. Intermediate substrate solution (20 mg / mL): Add 800 μL stock substrate solution to 3.2 mL DMSO and mix. Store in the dark at room temperature. Discard when the solution turns yellow. Stable for 1 month.
3. Working substrate solution (1 mg / mL): Add 250 μL of intermediate substrate solution to 4.75 mL of assay buffer and mix. Prepare for business. Typically, it is stable for 1 hour when stored on ice. Discard when the solution turns yellow.

-Labeled the sample cup in the software and revealed that the test was done with Konelab (repeated 6 times). The instrument was operated and the calibration was confirmed. Calculation of the activity of the granule sample (this formula assumes 1 g = 1 mL is the specific gravity of the lysate mixture):
PU / g granule = [(PU / mL) ^* (working diluent)] ^* [weight of solution buffer + granule (mL) / weight of granule (g)]

  -The mean value was calculated for each sample iteration. % CV (coefficient of variation) was calculated.

  In this example, a “mini” granule is one that includes a small smooth core in accordance with the teachings of the present invention.

  The data is shown in FIG.

Example 4
Production of three representative batches of phytase 45 kg of Minera de Santa Marta sodium sulfate core (MSM lot 41418.B in Table 1 of Example 1) was charged into a pilot scale fluidized bed coater with a batch size of 150 kg. . According to the light scattering method, the core had a mass median diameter of 199 micrometers.

  The core is fluidized and 2% w / w partially hydrolyzed polyvinyl alcohol (Celvol 5-88) and 0.5% w / w sodium phytate solution (Dr. Straetmans; Dermofel PA-3; An aqueous phytase enzyme solution (batch 488115613) containing lot NA2062) at a concentration of 17.5% solids w / w was sprayed onto the core.

  After enzyme spraying, a solution containing sodium sulfate (MSM, lot 13130405) was sprayed onto the core to deliver a net 50% w / w based on the final granule weight.

  The final coating solution consisting of partially hydrolyzed polyvinyl alcohol (Celvol 5-88) and talc (Microtalc FC CG-AW, Lot 13/00328) was sprayed onto the salt-coated enzyme core to obtain a net 9% w / Delivered a total coating weight of w.

  After cooling each batch of coated granules, 136 kg, 140 kg, and 134 kg of product were recovered from the fluid bed coater. According to the light scattering method, the final granules had an average D50 of 362 μm and a bulk density of 1.27 g / cm 3.

  FIG. 4 shows the pelletization results of three representative granule batches (3115, 3116, and 3117). Pelletization experiments were performed at the Danish Technical Institute.

(Example 5)
Pilot scale production of three representative batches of phytase standard TPT granules from the same concentrate batch 65 kg of Minera de Santa Marta sodium sulfate core (MSM Na-G.III-EE, lot 41235, 12) And put into a pilot scale fluidized bed coater with a batch size of 150 kg. According to the light scattering method, the core typically had a mass median diameter of 290 micrometers.

  The core is fluidized and 2% w / w partially hydrolyzed polyvinyl alcohol (Celvol 5-88) and 0.5% w / w sodium phytate solution (Dr. Straetmans; Dermofel PA-3; An aqueous phytase enzyme solution (batch 488115613) containing lot NA2062) at a concentration of 17.5% solids w / w was sprayed onto the core.

  After enzyme spraying, a solution containing sodium sulfate (MSM, lot 13130405) was sprayed onto the core to deliver a net 40% w / w based on the final granule weight.

  The final coating solution consisting of partially hydrolyzed polyvinyl alcohol (Celvol 5-88) and talc (Microtalc FC CG-AW, Lot 13/00328) was sprayed onto the salt-coated enzyme core to obtain a net 9% w / Delivered a total coating weight of w.

  After cooling each batch of coated granules, 151 kg, 151 kg and 150 kg of product were recovered from the fluid bed coater. According to the light scattering method, the final granules had an average D50 of 388 μm and a bulk density of 1.39 g / cm 3.

  Pelletization of three representative phytase standard TPT batches is shown in FIG.

Claims (26)

A granule population, wherein the granules are
Small smooth core particles,
An active substance,
The small smooth core particles contained in the granule population are
A smoothness index of less than 3, and
A mass median diameter of less than 300 micrometers;
A granule population having a particle size dispersion index of less than 2.5.   The granule population of claim 1, wherein the active substance is an enzyme.   A granule mass according to claim 1 or 2, wherein the active substance is in an active agent coating surrounding the smooth core particles.   4. Granule population according to any one of claims 1 to 3, further comprising at least one additional coating.   5. Granule population according to any one of the preceding claims, further comprising at least one additional coating, each of said at least one additional coating being included at at least 5% w / w of the final granule.   The granule population according to any one of claims 1 to 5, wherein the small smooth core particles comprise salt crystals.   The granule population according to any one of claims 1 to 6, wherein the small smooth core particles comprise sodium sulfate crystals.   The granule population according to any one of claims 1 to 7, wherein the active substance comprises an enzyme, and the enzyme is at least one of phytase, protease, or amylase. The small smooth core particles are
A smoothness index of less than 2.8, less than 2.5, or less than 2, and
A mass median diameter of less than 250 micrometers, less than 225 micrometers, less than 200 micrometers, less than 175 micrometers, less than 150 micrometers, less than 125 micrometers, or less than 100 micrometers;
The granule population according to any one of claims 1 to 8, comprising a particle size dispersion index of less than 2.5, less than 2, or less than 1.5.   10. Further comprising at least one additional coating, each of said at least one additional coating comprising at least 6%, 7%, 8%, 9%, or 10% w / w of the final granule. The granule population according to any one of the above. Small smooth core particles,
A smoothness index less than 2.5 but greater than or equal to 1.25;
A mass median diameter that is less than 250 micrometers but greater than or equal to 100 micrometers;
A small smooth core particle having a particle size dispersion index of less than 2.5 but greater than or equal to 1.5;
An active agent coating comprising an enzyme, wherein the enzyme is at least one of phytase, protease, or amylase;
A granule population comprising: at least one additional coating, each of the at least one additional coating being at least 7% of the final granule, but not more than 10% w / w. A first moisture barrier coating comprising a moisture barrier material;
The granule population according to any one of claims 1 to 11, further comprising a hydration coating comprising a hydration material surrounding the first moisture barrier coating.   The granule population according to any one of claims 1 to 12, wherein the moisture barrier material is selected from barrier polymers, proteins, lipids, fats and oils, fatty acids, and rubbers.   14. Granule population according to any one of the preceding claims, wherein the hydrating material is selected from starch, inorganic salts and sugars.   Animal feed pellets comprising the granule population according to any one of claims 1-14.   Animal feed non-pelletized mixture comprising the granule population of any one of claims 1-14.   A laundry detergent composition comprising the granule population according to any one of claims 1-14.   A dishwashing detergent composition comprising the granule population according to any one of claims 1-14.   A fiber treatment composition comprising the granule population according to any one of claims 1-14.   A composition for oven cooking comprising the granule mass according to any one of claims 1-14. In a method for producing a granule mass comprising the step of coating small smooth core particles with an active agent coating comprising an enzyme, the small smooth core particles have a smoothness index of less than 2.5 but greater than or equal to 1.25,
A mass median diameter of less than 300 micrometers but greater than or equal to 150 micrometers;
A method for producing a granule population having a particle size dispersion index of less than 3.0 but not less than 1.5. A process for producing an animal feed composition comprising:
Preparing a granule population according to any one of claims 1-14;
Mixing the granules with feed to obtain a non-pelletized mixture;
Pelletizing said non-pelletized mixture at a temperature between 70 ° C and 95 ° C. Preparing the granule population according to any one of claims 1-14;
Mixing the granules with a feed acceptable carrier, diluent or excipient;
(Optionally) a method of preparing a feed additive granule population comprising packaging.   Use of the granule mass according to any one of claims 1 to 14 in a steaming or pelletizing process.   Storage stability comprising the steps of producing the granule population according to any one of claims 1 to 14 and comparing the storage stability with a representative sample of the granule population lacking small smooth core particles. How to improve.   15. A method of reducing dust comprising the steps of producing a granule population according to any one of claims 1-14 and comparing the dust with a representative sample of the granule population lacking small smooth core particles.

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