WO1993007260A1 - Procede de fabrication d'enzymes depourvues de poussiere - Google Patents
Procede de fabrication d'enzymes depourvues de poussiere Download PDFInfo
- Publication number
- WO1993007260A1 WO1993007260A1 PCT/US1991/007675 US9107675W WO9307260A1 WO 1993007260 A1 WO1993007260 A1 WO 1993007260A1 US 9107675 W US9107675 W US 9107675W WO 9307260 A1 WO9307260 A1 WO 9307260A1
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- WO
- WIPO (PCT)
- Prior art keywords
- enzyme
- broth
- solids
- cores
- total
- Prior art date
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Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J2/00—Processes or devices for granulating materials, e.g. fertilisers in general; Rendering particulate materials free flowing in general, e.g. making them hydrophobic
- B01J2/16—Processes or devices for granulating materials, e.g. fertilisers in general; Rendering particulate materials free flowing in general, e.g. making them hydrophobic by suspending the powder material in a gas, e.g. in fluidised beds or as a falling curtain
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J2/00—Processes or devices for granulating materials, e.g. fertilisers in general; Rendering particulate materials free flowing in general, e.g. making them hydrophobic
- B01J2/006—Coating of the granules without description of the process or the device by which the granules are obtained
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38672—Granulated or coated enzymes
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/04—Enzymes or microbial cells immobilised on or in an organic carrier entrapped within the carrier, e.g. gel or hollow fibres
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/10—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a carbohydrate
Definitions
- the present invention relates to a novel procedure for making dry and dust-free enzyme granules from a fermentation broth containing the enzyme.
- enzymes useful in detergent applications such as proteases, a ylases.
- Upases, and cellulases have been produced in a wide variety of microbial hosts. When enzymes are produced in a microbial host they are usually either secreted directly into the fermentation broth by the microorganism or released into the fermentation broth by lysing the cell. The enzyme can then be recovered from the broth in a soluble form by a number of techniques including filtration, centrifugation, membrane filtration, chromatography.
- the dissolved enzyme can be converted to a dry form from a liquid using techniques such as precipitation, crystallization, or spray-drying.
- a problem associated with dry enzyme preparations is that there is a high dust level associated with them, which can cause dermatologic distress to the manufacturer, consumer, or any other person handling the enzyme. It has been a desire in the art to treat these dry enzymes so as to reduce the hazard of dusting. To control dusting and increase particle size, dry enzymes are often granulated by various means known by those skilled in the art. Various enzyme formulations and processes for these preparations have been developed in an effort to alleviate the dusting problem. For example, German Patent No.
- 21 37 042 discloses a process in which an extrudable enzyme containing formulation is extruded through a die onto the revolving plate of a spheronizing device to form spherical particles of the enzyme-containing formulations which are optionally coated with a material designed to prevent dusting.
- U.S. Pat. No. 4,016,040 discloses a method for the preparation of free-flowing substantially dust-free, spherical enzyme-containing beads prepared by blending a powdered
- SUBSTITUTE SHEET concentrate of the enzyme with a binder in molten form and spraying droplets of the blend through a spray nozzle into cool air to solidify the droplets and form the beads.
- U.S. Pat. No 4,009,076 Another type of granular enzyme formulation is described in U.S. Pat. No 4,009,076.
- This formulation is prepared by mixing the dry enzyme with a solid nonviable substance and optionally a cohesive organic material as binder to form an enzymatically active core.
- An enzyme slurry containing the cohesive organic material can be sprayed onto, for example, sodium tripolyphosphate and the cohesive organic material sprayed onto it with subsequent extrusion through a die.
- the enzyme-containing granule is sprayed with an aqueous solution containing a plasticized organic resin, then dried.
- a process is described in GDR Pat. 0 151 598 in which sodium tripolyphosphate is sprayed with an aqueous fermentation broth and agglomerated in a cyclone apparatus. The agglomerates are removed from the cyclone apparatus while still wet and placed
- SUBSTITUTE SHEET It is desirable to be able to produce a dry dust-free product with a relatively low percentage of total weight as enzyme, especially with enzymes of high specific activity.
- proteases of high specific activity are often more subject to autolysis, and the addition of large percentages of solid stabilizer compounds may be needed to achieve high process yields; (2) in general, it is most economical to remove as much water as possible from the enzyme solution prior to spray-coating by methods such as ultrafiltration, thereby reducing the batch cycle time in the spray-coater; (3) it is sometimes desirable to add processing aids such as binders or powders into the enzyme concentrate to reduce product dustiness or help prevent excessive agglomeration of the granules. For any of these reasons, it may be desirable to provide a fermentation broth containing between about 31% and 55% solids on a dry weight basis, so long as it is not too viscous to be pumped through a spray nozzle.
- This invention achieves these and other desirable objectives in a cost-effective, efficient, and safe manner.
- a dry dust-free enzyme particle can be produced from fermentation broth by the followi method: a) introducing a particulate, hydratable core material into a fluidized-bed spray-coater and maintaining the core particles suspended in the reaction chamber: optionally, producing, building up, or otherwise modifying the core particles in a fluidized-bed spray-coater and maintaining the core particles suspended in the reaction chamber; b) providing a fermentation broth containing from about 5% to about 100% w/w of the total solids therein ⁇ f a water solubl or dispersible enzyme produced in the fermentation broth and a total solids content of 4 - 31% w/w of the fermentation broth such that the broth has a viscosity of 10 - 5,000 cps at room temperature and: c) spraying the broth onto the core and evaporating the liquid to leave the solids coated on the core, such that the fermentation broth solids added to the core provides a total dry weight gain of 1% - 19% w/w over the initial
- SUBSTITUTESHEET total dry weight gain of 1% - 24% w/w over the initial weight of the core.
- the fermentation broth has a total solids content of 31% to 55% w/w.
- the total dry weight gain of the core particles is from 1% to 100% w/w.
- the enzyme-containing particles prepared by these processes are included in this invention.
- a fluidize bed spray-coater comprising a fluidized-bed dryer consisting of a conical product chamber that has a porous grid on the bottom and is open on the top to be put up against a cylindrical or conical shaped expansion chamber of a larger diameter than the product chamber; a filter to collect dust and help air flow is placed at the far end of the expansion chamber and one or more spray nozzles are located within the chamber to apply the solution to the core.
- a fluidized-bed dryer consisting of a conical product chamber that has a porous grid on the bottom and is open on the top to be put up against a cylindrical or conical shaped expansion chamber of a larger diameter than the product chamber; a filter to collect dust and help air flow is placed at the far end of the expansion chamber and one or more spray nozzles are located within the chamber to apply the solution to the core.
- a fluidized-bed dryer consisting of a conical product chamber that has a porous grid on the bottom and is open on the top to be put up against a cylindrical or conical
- the initial step in the method involves introducing a particulate, hydratable core material into the reaction chamber of the fluidized-bed dryer and suspending the particles therein on a stream of air.
- the core particles preferably are composed of a highly hydratable material, i.e. a material which is readil dispersible or soluble in water.
- the core material should either disperse (fall apart by failure to maintain its integrity) or dissolve by going into a true solution.
- Clays bentonite, kaolin
- non pareils non pareils
- agglomerated potato starch are considered dispersible.
- Non pareils are spherical particles consisting of a solid nucleus that has been rounded into a spherical shape by binding layers of powder and crystallized solute, generally starch and sugar, to the nucleus in a rotating spherical container and are preferred.
- Non pareil particles are often called "seeds”.
- Salt particles are considered soluble. Also suitable are agglomerated trisodium citrate, pan crystallized NaCl flakes, bentonite granules and prills, bentonite/kaolin/diatomaceous earth disk-pelletized granules, and sodium citrate crystals.
- the core particle is of a material which is not dissolved during the subsequent spraying process and is preferably of a particle size from 150 to 2,000 microns (100 mesh to 10 mesh on the U.S. Standard Sieve Series) in its longest dimension.
- fermentation broth the liquid in which the enzyme is produced by fermentation of a microorganism.
- the broth may be modified by deleting or adding material, e.g. filtration of cell solids or addition of binders, salts, pigments, plasticizers, and fragrances, however, it still contains the enzyme. It also may be concentrated or purified by removal or substitution of a portion of the liquid material, by such processes as ultrafiltration, extraction, and chromatography.
- Enzymes suitable for use in this method are those which are soluble or dispersible in the fermentation broth they are produced in and from which the volatile components of the fermentation broth can be removed to leave a residual layer of enzyme on the surface of the core material.
- Suitable enzymes include, for example, proteases (bacterial, fungal, acid, neutral, or alkaline), amylases (alpha and beta), lipases, and cellulases.
- the enzyme is present in the broth at from about 5% to about 100% w/w of total solids, and fermentation broth solids range from about 0.5% to about 95.5% w/w of total solids in the fermentation broth, with any remaining solids comprising added metallic salts, sugars, pigments, binders, stabilizers, plasticizers, and fragrances such that total solids represent
- the broth including any optional metallic salts, sugars, pigments, binders, stabilizers, plasticizers, and fragrances, must have a viscosity low enough to be pumped and atomized for effective spray-coating (typically 10 to 5,000 cps at room temperature).
- the broth solids and enzymes are applied to the surface of the core material by fluidizing the core particles in a flow of air whereupon a broth containing the enzyme and other solids is then atomized and sprayed into the expansion chamber of the spray-coater.
- the atomized droplets contact the surface of the core particles leaving a film of the solids adhering to the surface of the particles when the water and other volatiles are evaporated.
- Airflow is maintained upwards and out the top of the expansion chamber through a filter.
- the filter may be located inside or outside of the unit, or may be substituted for by a scrubber or cyclone. This filter traps fine dried particles which contribute to dust. Fluidized-bed spray-coaters that have this filter typically have automatic shakers which shake the filter to prevent excessive restriction of the air flow.
- the shaker unit is turned off during the last 5 minutes of operations, thus reducing the dust content of the product due to release of fines trapped within the filter.
- the filter is located outside the unit or substituted by a scrubber or cyclone. When recovering fermentation broth enzymes, the broth may be treated in various ways to achieve desired results.
- the broth may be filtered to remove cells and cell debris or to remove microorganisms to yield a sterile product.
- the broth may be concentrated to achieve the desired total solids concentration of about 4% to about 31% w/w of the broth.
- salts, stabilizers, etc. can also be added as desired, and the enzyme may be concentrated or purified as desired. It is further a preferred embodiment of the invention that the weight gain of the solids in the broth applied to the core over the initial dry weight of the core is about 1% to about 19% w/w.
- the desired total solids concentration is about 31% to about 55% w/w of the broth.
- the weight gain of the solids in the broth applied to the core over the initial dry weight of the core is about 1% to about 100% w/w.
- Handling the enzyme in liquid form in the fermentation broth has the advantage of lowering the possibility of dermatologic contact due to dusting and produces a product which is dust- free and minimizes losses due to any extra step of drying, since the drying process is confined to a single, well-contained reactor.
- the enzyme coated particles When sufficient enzyme is applied to the core particles to provide the desired enzyme activity, the enzyme coated particles while still suspended in the reaction chamber of the coater or later reintroduced therein, are coated with a layer of a water soluble or water dispersible coating agent. This is accomplished in a manner similar to that used for application of the enzyme/solids coating.
- Suitable coating agents include, for example, fatty acid esters, gum arabic and other natural gums, alkoxylated alcohols, pol vinyl alcohols, ethoxylated alkylphenols and more specifically, polyethylene glycols (PEG) (molecular weight (MW) 300 to 20,000), linear alcohol alkoxylate (MW 1,450 to 2,670), polyvinyl acetate phthalate (PVAP) , polymeric nonylphenyl ethoxylates (MW 1,975 to 4,315) dinonyl phenyl ethoxylate (average MW 6,900), hydroxypropylmethyl cellulose, and other modified celluloses.
- PEG polyethylene glycols
- VAP polyvinyl acetate phthalate
- PVAP polymeric nonylphenyl ethoxylates
- MW 1,975 to 4,315) dinonyl phenyl ethoxylate average MW 6,900
- hydroxypropylmethyl cellulose and other modified celluloses.
- coating agents include sugars, starches, salts, titanium dioxide, and other sealants, stabilizers, release agents, binders or pigments.
- the net result of the process is to provide an enzyme coated core particle having a layer of the coating agent on its surface to provide the desired dust-free enzyme-containing particle.
- the total weight gain of solids versus the initial core is preferably from about 1% to about 24% w/w when a coating is used, and preferably from about 1% to about 19% w/w when a coating is not used.
- the total weight gain of solids versus the initial core is about 1% to about 100% whether a coating is used or not.
- the dust-free enzyme particles of the present invention can be used wherever enzymes are needed in a dry system. Thus, they can be used as additives to dry detergent formulations, for removing gelatin coatings on photographic films to aid in silver recovery, in the digestion of wastes from food processing plants for nitrogen recovery, in denture cleansers for removing protein bound stains, in food preparation, and as a processing aid in waste water treatment.
- Example 1 Lab-Scale Spray-Coating of FNA Protease Onto Non Pareils, With Gum Arabic Coating Agent.
- a WSG-5 fluidized-bed granulator was charged with 3800 grams of -35/+40 mesh non-pareil cores or seeds and heated to 60°
- STITUTE SHEET concentrate containing 3.8% w/w enzyme and 10.5% w/w total solids (36.2% w/w of total solids were enzyme) was sprayed onto the suspended cores at a 95° C inlet temperature and a 40° - 50° C outlet temperature.
- the spray rate was about 45 ml/minute (min) and enzyme coating or plating took 37 minutes, resulting in an estimated weight gain of 210 grams, or 5.5% w/w.
- 230 grams of material was removed for subsequent analysis, leaving 3780 grams of enzyme coated active cores.
- a coating agent solution containing 60 grams gum arabic in 600 ml water was applied at 40 ml/min; the entire granulation or coating lasted 56 minutes.
- the final product weighed approximately 3840 grams, representing a 1.6% increase over the enzyme-plated cores, and a 7.2% net increase in weight over the initial core weight.
- Example 2 Lab-Scale Spray-Coating of FNA Protease Onto Non Pareils, With PEG 8000 and TiO_ Coating Agents.
- a WSG-5 fluidized-bed granulator was charged with 5000 grams of -20/+40 mesh non pareil cores or seeds which were fluidized.
- a 1786 ml aqueous protease concentrate containing 3.8% w/w enzyme and 10.5% w/w total solids (as in Example 1) was sprayed onto the cores at an inlet temperature of about 70° C and an outlet temperature of 40° - 50° C.
- the weight gain due to the protease was 188 grams, or 3.8% w/w.
- a coating agent solution containing 150 grams PEG 8000 and 250 grams Ti0 2 in 1 liter of water was sprayed on the enzyme-coated non pareils which were dried.
- the final product weighed 5560 grams, representing an 11.2% increase over the initial core weight.
- Example 3 Spray-Coating of Lipase Onto Non Pareils, With Hydroxypropylmethylcellulose (Opadry White) Coating Agent.
- a Uni-Glatt laboratory fluidized-bed spray-coater was charged with 960 grams of -20/+40 mesh non pareil cores or seeds which were fluidized.
- a 1700 ml aqueous lipase concentrate of 6.9 gram/liter lipase with 4.9% total solids was sprayed onto the non pareil cores at an inlet temperature of 50° - 66° C and an outlet temperature of 38° - 42° C and an atomization pressure of 2.5 bar.
- Enzyme was 14.1% of total solids.
- the enzyme-coated cores weighed 962 grams, an increase of 5.0% w/w.
- a Uni-Glatt laboratory fluidized-bed spray-coater was charged with 1000 grams of -20/+40 mesh non pareil cores or seeds which were fluidized.
- An 840 ml aqueous cellulase concentrate containing 172 gram/liter enzyme and 24.7% total solids was sprayed at an inlet temperature of 50° - 64°C and an outlet temperature of 38° - 46°C at a spray-rate of about 10 ml/min.
- Enzyme represented 69.6% of total broth solids.
- 1143 grams of product were recovered, representing a 14.3% w/w increase over the non pareil cores.
- Recovery of active enzyme was 98.8% of the ultrafiltration concentrate feed, as measured using bFPU units.
- Example 5 Large-Scale Spray-Coating of FNA Protease Onto Non Pareils, With PEG 8000 and TiO_ Coating Agents.
- a modified Aeromatic S-8 fluidized-bed granulator was used for a large-scale spray-coating run.
- the coater was loaded with 681.8 kg (1500 lbs) non pareil seeds of -20/+40 mesh.
- the bowl was raised into place and the cores fluidized with 65° C inlet air until the outlet air temperature reached 45° C.
- a 100.4 kg aqueous protease enzyme concentrate containing 5.94 w/w active enzyme and 21.3% w/w total solids was sprayed onto the cores using a 1.8 mm multiple-head Schlick nozzle at 4 bar atomization air pressure.
- TITUTE SHEET was maintained between 40° and 50°C. Enzyme represented 27.9% w/w of total feed solids. Enzyme coating or layering took about 80 minutes, excluding a 15 minute shutdown to examine the produc in the bowl for coating uniformity. The application rate was about 1.2 liters per minute. By calculation, this represented a weight gain of 3.1% w/w over the cores. The bowl was temporarily removed and the machine was cleaned. Overcoating was then applied to the enzyme granules in the same dryer/coater unit. The coating agent solution consisted of 123.6 kg of tap water heated to 50° C, in which 67.4 kg PEG 8000 and 33.7 kg TiO. were dissolved or suspended to give a 150 liter solution.
- the enzyme coated granules were fluidized and heated to 45° C as before. Atomization air pressure was held at 4 bar and outlet air temperature varied between 40° C and 50° C. The total coating run time was 136 minutes with an application rate of about 1.1 liter per minute. After coating, the product was dried for four minutes until the outlet temperature reached 48°C, then cooled for 14 more minutes until outlet temperature reached 32°C. The bowl was removed and the product sieved to a -16/+40 cut. The mass balance is shown in Table 1. The final product represented a net increase of 13.0% w/w over the core weight using the actual product weight or a net increase of 17.9% w/w over the core weight using the theoretical sum of ingredient weights. Product dust was extremely low. The product granules produced 0.3 milligrams total dust and 2.42 micrograras protease dust per 60 gram sample when subjected to a 40 minute
- a WSG 300 granulator is charged with 700 kg of non pareil seeds or cores of -20/+40 mesh and the cores are fluidized.
- a coating agent solution consisting of 3.5 kg hydroxypropylmethylcellulose 3.5 kg TiO ⁇ , and 30 kg water is sprayed on the fluidized enzyme coated cores.
- the total product weight is 717.4 kg, which represents a total weight gain of 2.49% w/w.
- a WSG 300 granulator is charged with 700 kg non pareil seeds of -20/+40 mesh and the seeds are fluidized.
- a coating agent solution containing 26% w/w cellulase and 39% w/w total solids, with enzyme 66.7% w/w of total solids.
- SUBSTITUTE SHEET consisting of 18.5 kg PEG 20,000, 18.5 kg Ti0 2 , and 100 kg water is sprayed on the fluidized enzyme coated seeds.
- the total product weight is 867.3 kg, which represents a total weight gain of 23.9% w/w.
- Example 8 Spray-Coating of High Solids Protease Onto Non Pareils, With PEG 8000 and TiO_ Coating Agents.
- a Glatt GPCG-5 fluidized-bed granulator is charged with 10.0 kg non pareil seeds.
- a 4766 gram aqueous Bacillus lichenformis subtilisin ultrafiltration concentrate containing 20% w/w enzyme solids and 32% w/w total solids, with enzyme 63% w/w of total solids, is sprayed onto the fluidized cores at a rate of 85 g/minute and an atomization air pressure of 2.5 bar.
- the inlet air temperature is about 70° C and the outlet temperature is about 48° C.
- a coating solution of 2000 grams PEG 8000 and 500 grams TiO_, suspended in 10 liters of water, is then sprayed onto the enzyme-coated cores under the same conditions.
- the final coated product weighs 14.0 kg, a weight gain of 40% w/w.
- Example 9 Spray-Coating of High Solids Cellulase Concentrate Onto Non Pareils, With PEG 8000 and TiO- Coating Agents.
- a Uni-Glatt laboratory spray-coater is charged with 600 grams non pareil seeds. At an inlet temperature of 60° C, an outlet temperature of 42° C, and an atomization air pressure of 3 bar, an aqueous cellulase concentrate of 455 grams containing 30.3% w/w enzyme and 39.5% w/w total solids, with enzyme 77% w/w of total solids, is sprayed onto the fluidized cores, increasing the weight of the cores to 780 grams, a 29.7% w/w increase. A coating solution containing 200 grams PEG 800 and 200 grams TiO_ in 1.5 liters of water is sprayed on the cores under the same conditions. The harvested product weighs 1180 grams, a net increase in weight of 97% over the original cores.
- Example 10 Spray-Coating of Protease Concentrate With Added Salts Onto Non Pareils, With Gum Arabic and TiO. Coating Agents.
- a Uni-Glatt laboratory spray-coater is charged with 800 grams non pareil seeds.
- a 500 ml aqueous protease concentrate weighing 520 grams and containing 8% w/w protease and 24% w/w total solids is modified by dissolving 100 grams of stabilizer salts in the concentrate. These additions increase the solution volume to 540 ml and the solution weight to 620 grams.
- the modified concentrate with 6.7% w/w enzyme solids and 36.3% w/w total solids, is sprayed onto the fluidized cores at an inlet temperature of 50° C, an outlet temperature of 40° C, and an atomization air pressure of 3.5 bar. This increases the product weight to 1025 grams, a 28.1% w/w increase over the core weight.
Abstract
Priority Applications (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
PCT/US1991/007675 WO1993007260A1 (fr) | 1991-10-10 | 1991-10-10 | Procede de fabrication d'enzymes depourvues de poussiere |
EP91919553A EP0620848A4 (fr) | 1991-10-10 | 1991-10-10 | Procede de fabrication d'enzymes depourvues de poussiere. |
CA002120611A CA2120611C (fr) | 1991-10-10 | 1991-10-10 | Procede pour la fabrication d'enzymes exemptes de poussiere |
JP3518511A JPH06511381A (ja) | 1991-10-10 | 1991-10-10 | 無粉塵酵素の製造方法 |
FI941645A FI941645A0 (fi) | 1991-10-10 | 1994-04-08 | Menetelmä pölyämättömän entsyymin valmistamiseksi |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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PCT/US1991/007675 WO1993007260A1 (fr) | 1991-10-10 | 1991-10-10 | Procede de fabrication d'enzymes depourvues de poussiere |
CA002120611A CA2120611C (fr) | 1991-10-10 | 1991-10-10 | Procede pour la fabrication d'enzymes exemptes de poussiere |
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WO1993007260A1 true WO1993007260A1 (fr) | 1993-04-15 |
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PCT/US1991/007675 WO1993007260A1 (fr) | 1991-10-10 | 1991-10-10 | Procede de fabrication d'enzymes depourvues de poussiere |
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EP0913468A2 (fr) * | 1997-07-22 | 1999-05-06 | Gist-Brocades B.V. | Composition pour l'amélioration du pain |
US6350728B1 (en) | 1996-12-11 | 2002-02-26 | Henkel Kommanditgesellschaft Auf Aktien (Kgaa) | Coated enzyme preparation with an improved solubility |
WO2002061427A1 (fr) | 2001-01-31 | 2002-08-08 | Novozymes A/S | Procede d'analyse d'une composition granulaire par fluorimetrie |
WO2003080827A2 (fr) | 2002-03-27 | 2003-10-02 | Novozymes A/S | Granules a enrobages filamenteux |
WO2004033083A2 (fr) | 2002-10-09 | 2004-04-22 | Novozymes A/S | Procede destine a ameliorer des compositions particulaires |
WO2004067739A2 (fr) | 2003-01-27 | 2004-08-12 | Novozymes A/S | Stabilisation de granules |
WO2005063975A1 (fr) * | 2003-12-20 | 2005-07-14 | Henkel Kommanditgesellschaft Auf Aktien | Granules enzymatique clairs, stables, inodores et exempts de poussieres |
US6924133B1 (en) * | 1999-10-01 | 2005-08-02 | Novozymes A/S | Spray dried enzyme product |
WO2005074705A1 (fr) * | 2004-01-30 | 2005-08-18 | Basf Aktiengesellschaft | Formulations enzymatiques stabilisees |
US6979669B2 (en) | 2001-08-30 | 2005-12-27 | Henkel Kommanditgesellschaft Auf Aktien | Encapsulated active ingredient preparation for use in particulate detergents and cleaning agents |
EP1700904A1 (fr) | 2005-03-11 | 2006-09-13 | Unilever N.V. | Composition detergente liquide |
US7153820B2 (en) | 2001-08-13 | 2006-12-26 | Ecolab Inc. | Solid detergent composition and method for solidifying a detergent composition |
US7186533B2 (en) | 1999-02-10 | 2007-03-06 | Basf Aktiengesellschaft | Granulates containing feed-enzymes |
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