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WO1994026883A2 - Procede de production d'enzyme exempte de poussiere - Google Patents

Procede de production d'enzyme exempte de poussiere Download PDF

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Publication number
WO1994026883A2
WO1994026883A2 PCT/EP1994/001642 EP9401642W WO9426883A2 WO 1994026883 A2 WO1994026883 A2 WO 1994026883A2 EP 9401642 W EP9401642 W EP 9401642W WO 9426883 A2 WO9426883 A2 WO 9426883A2
Authority
WO
WIPO (PCT)
Prior art keywords
enzyme
granule
coating
granules
under
Prior art date
Application number
PCT/EP1994/001642
Other languages
English (en)
Other versions
WO1994026883A3 (fr
WO1994026883A9 (fr
Inventor
Carl Sidonius Maria Andela
Jan Feijen
Marc Dillissen
Original Assignee
Gist-Brocades N.V.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Gist-Brocades N.V. filed Critical Gist-Brocades N.V.
Priority to JP6525000A priority Critical patent/JPH07509141A/ja
Priority to AU69705/94A priority patent/AU677342B2/en
Priority to PL94307854A priority patent/PL307854A1/xx
Priority to EP94918349A priority patent/EP0675952A1/fr
Priority to KR1019950700195A priority patent/KR950702625A/ko
Publication of WO1994026883A2 publication Critical patent/WO1994026883A2/fr
Publication of WO1994026883A9 publication Critical patent/WO1994026883A9/fr
Priority to FI950183A priority patent/FI950183A0/fi
Publication of WO1994026883A3 publication Critical patent/WO1994026883A3/fr

Links

Classifications

    • 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
    • C12N11/14—Enzymes or microbial cells immobilised on or in an inorganic carrier
    • 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
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6478—Aspartic endopeptidases (3.4.23)
    • C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
    • 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
    • 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
    • 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
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18—Carboxylic ester hydrolases (3.1.1)
    • C12N9/20—Triglyceride splitting, e.g. by means of lipase
    • 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
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
    • C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
    • 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
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/98—Preparation of granular or free-flowing enzyme compositions

Definitions

  • the present invention relates to novel enzyme granules and a process for the preparation thereof.
  • enzymes are produced by microorganisms such as bacteria, yeast and fungi. These enzymes are especially useful in detergents, starch and textile processing, and in feed and food applications. Examples of enzymes useful in detergent application include proteases, amylases, lipases and cellulases.
  • the enzymes are produced by fermentation and then recovered, purified and concentrated into a liquid or brought in dry form. Suitable recovery techniques include filtration, centrifug- ation, membrane filtration, precipitation, crystallisation, chromatography, spray drying, etc.
  • the dust levels in such preparations should be as low as possible.
  • the dry enzymes are usually brought in granule form, for which several granulation techniques have been developed. See, for example, U.S. Patents Nos. 4,009,076, 4,016,040, 4,078,368, 4,242,219, etc.
  • most of the granules are coated after their production with a film-forming macromolecular material.
  • JP 58-179492A discloses the preparation of enzyme granules with a protective coating.
  • a fluid bed dryer is used to first spray e.g. a liquid enzyme concentrate onto a core material and subsequently spray a coating material containing a cellulose derivative onto the granule, while drying takes place during the whole process.
  • EP-A-0193829 describes a method for the production of dust free enzyme containing particles by coating hydratable core particles with an enzyme and then with a film-forming material. Coating is carried out by suspending the core particles in a fluidized bed dryer, spraying an aqueous slurry of enzyme onto the core particles while suspended, and evaporating water to leave a dried enzyme coat on the particles. The resultant enzyme-coated particles, while still suspended in the fluidized bed, are sprayed with a solution or dispersion of the macromolecular material, and dried to remove solvent to leave a coating of the macromolecular material.
  • WO 90/09428 discloses a detergent additive granulate which comprises a core with a primary detergent additive, e.g. an enzyme, surrounded by a shell comprising a secondary detergent additive, e.g. another enzyme, a binder, and granulating agents, and optionally a filler, and a protective coating between the core and the shell, whereby the shell comprises cellulose or artificial fibres, and whereby the core optionally may also comprise cellulose or artificial fibres.
  • the detergent additive granulate is said to exhibit a high physical strength, and the primary and secondary detergent additives are separated from each other and/or from harmful environmental factors.
  • WO 93/07263 discloses a granular enzyme composition which comprises a core, an enzyme layer and an outer coating layer.
  • the granular enzyme composition is said to have reduced tendencies to form dust and leave residue, and exhibit improved stability and delayed release characteristics.
  • the method for making such enzyme- containing granules is said to have greatly reduced processing time.
  • the present invention provides new enzyme granules with improved properties. As compared to the prior art cited above the granules according to the present invention have the advantage that the compound of interest is not only located at the surface of the granule.
  • enzyme granules comprising porous core material in which the enzyme in solution is adsorbed.
  • the enzyme-containing granules are preferably coated with a film-forming macromolecular material. Such granules have an improved mechanical strength.
  • the invention further provides an efficient method of preparing the novel enzyme granules.
  • the granules according to the present invention are based on core particles having a good pore size and pore size distribution to allow an enzyme solution to enter into the particle. Accordingly, the core material comprises the enzyme in liquid form, thus eliminating the drawback of processing powdered enzymes.
  • the pore diameter should not be too big, since this will inter alia reduce the strength of the particle, and not too small, since this will prevent the compound of interest, e.g. an enzyme, entering into the pores.
  • European Patent Application EP-A-0542351 (published on May 19, 1993, i.e. after the priority date of the present patent application) discloses a process for the preparation of salt granulates.
  • the products which are obtainable by this process are very suitable for use as core material in enzyme applications.
  • the level of porosity is important with respect to the economics of the process.
  • a method for efficiently preparing the new enzyme granules which comprises the following steps: (a) preparing a non-aqueous enzyme solution
  • the enzyme solution may be prepared in various ways, mainly depending on the physical characteristics of the enzyme used. Suitable solvents for the purpose of the invention include ethylene glycol, propylene glycol, liquid polyethylene glycols (PEG's) such as PEG 200 and PEG 400, and glycerol. In certain cases it may be useful to prepare first an aqueous enzyme solution and to add the non-aqueous solvent. The water is then partly or entirely removed, for example by evaporation.
  • the "non-aqueous" enzyme solution may contain a certain amount of water, for example 10-20%, but this should not have an adverse affect on the various components of the granulate, in particular the porous core material.
  • an enzyme slurry may be used in certain instances which will be clear to the man skilled in the art.
  • the absorption of enzyme into the particle can be done in various way. Both from an enzyme containing aqueous liquid or slurry (e.g. a concentrated fermentation broth) as from an enzyme containing non-aqueous liquid or slurry (e.g. non ionics, alcohols etc.), or a combination thereof.
  • Suitable porous core material includes soda, NaCl and silica and is commercially available.
  • the porous core material is preferably prepared by the method described in EP-A-0542351.
  • the enzyme solution can be brought onto the porous 5 core material in various ways which are all known in the art, for example using mixing devices or a fluidized bed or a mixer- fluid bed dryer combination. Process steps (b) and (c) may suitably be combined.
  • one or more protective coating layer(s) o can be brought onto the core to yield a dust free enzyme containing particle.
  • Suitable coating materials are frequently described in the literature, see e.g. JP 58-179492A and EP-A- 0193829. They include cellulose coatings or cellulose based coatings containing hydroxypropylcellulose, methyl cellulose, s hydroxypropyl methyl cellulose and/or hydroxyethyl cellulose. Also acrylic polymers like EUDRAGIT ® (Rohm Pharma) can be applied. The amounts of coating to be applied may vary in fairly wide ranges but is usually between 0.1 and 25% by weight, for the cellulose based coatings preferably between 5 o and 25 wt%.
  • Coating layers can also be used to add other useful compounds to the granule. It is even possible to prepare multilayer granules wherein various coating layers have different functions, for example to stabilize the compounds 5 which are present, to add colour etc.
  • porous core material which dissolves slowly or which liberates the absorbed enzyme slowly.
  • This technology in combination with coating technology permits 0 a composition of a granule where several compounds can be released in a sequence according to demand.
  • An example hereof is a granule where a protease is absorbed into a porous core, a lipase is coated on the core and finally a coating layer is brougth onto the granule. 5
  • the entire process for preparing the enzyme granules according to the invention may be suitably carried out in one apparatus, for example a mixer or a fluidized bed.
  • the process according to the invention has several advantages.
  • the process is performed in more than one step the (enzyme) dust formation is reduced during transport of the particles between the apparatus.
  • the absorption of an enzyme solution or slurry in a porous particle is much faster than e.g. spraying an enzyme solution or slurry onto a core in a fluid bed or than mixing an enzyme with a non-porous carrier.
  • protease used in the examples is the high alkaline protease PB92, see U.S. Patent No. Re 30,602, which is commercially available from Gist-brocades N.V. under the trade mark MAXACAL ® .
  • the lipase used in the examples is the lipase which is obtainable from the strain Pseudomonas pseudoalcaligenes M-l (CBS 473.85), see e.g. EP-B-0218272, and U.S. Patents Nos. 4,933,287 and 5,153,135.
  • the chymosin used in the examples is produced by a transformed yeast strain of Kluyveromyces lactis and commercially available from Gist-brocades N.V. under the trade mark MAXIREN ® . See e.g. EP-B-0096430 and EP-B-0301669 and U.S. Patent No. 4,859,596.
  • Soda cores with a porosity of 6 (Soda ash Dense ® ), 16 (Soda ash Compact ® ) and 38% (Soda ash Sorbent ® ), respectively, were obtained from Akzo N.V. (see also EP-A-0542351) .
  • the soda was sieved to obtain a particle size between 315-710 ⁇ m.
  • Spraying and absorption were carried out in a rotating vessel (enzyme liquid inlet temperature 30-50°C) .
  • the material was then coated in a fluid bed dryer essentially according to the method described in JP 58-179492A or EP-A-0193829) and dust free enzyme granules were obtained.
  • the non-aqueous protease solutions with ethylene glycol, propylene glycol, PEG 400 and glycerol were produced with a protease activity varying from 3.4 to 3.7 MADU/g.
  • the liquid absorption process resulted in an enzyme yield of 61% to 98% based on enzyme activity, depending on the water content of the non-aqueous solution.
  • the tests were carried out with soda cores of 6%, 16 and 38% porosity (see above).
  • Protease granules were prepared in the same way as described in Example 1 but using porous NaCl cores instead of soda cores. These NaCl cores were prepared essentially according to the method described in EP-A-0542351 and had a porosity of 15%. These cores were filled with a non-aqueous liquid containing a protease with an activity of 3.4 MADU/g. This resulted in a granulate which had an activity of 440.000 ADU/g (enzyme yield >97%) . After coating in a fluidized bed with a cellulose based coating (20% w/w) under the same conditions as mentioned above, coated granules were obtained which had an activity of 397.500 ADU/g. Again a good mass yield was obtained (>92%) .
  • Chymosin was dissolved in propylene glycol.
  • the liquid absored well in the porous NaCl, which may absorb 15 % of its weight.
  • Porous core material (Soda ash Compact ® , 600 g) with a particle size of 300-710 ⁇ m was introduced in a fluid bed dryer.
  • the water was evaporated and the non-ionic and the lipase were absorbed into the particles.
  • a coating layer was then sprayed onto the particles and dust-free granules were obtained.
  • protease granules were made.
  • the protease containing solutions of ethylene glycol and propylene glycol, respectively, were sprayed into the fluid bed directly on top of the porous material, which was fluidized (particle size between 400 and 600 ⁇ m) . Both when the protease was dissolved in ethylene glycol and propylene glycol, the liquid was absorbed well into the material.
  • Enzyme dust [mg/20 g 0.45 0.31 0.14 0.20 of sample, based on
  • porous core materials such as, NaCl and silica
  • Ethylene glycol and polyethylene glycol were used as the solvents.
  • Soda ash Sorbent ® (see Example 1) is able to absorb a liquid upto 37% by weight (based on the soda) , the NaCl used may absorb 15% of its weight, while the silica may absorb 100%.
  • Table 2 shows the residual enzyme activity after absorption of various enzyme containing liquids into various core materials.
  • the obtained material was tested for its protease stability at 7°C (at ambient relative humidity) using various non-aqueous liquids.
  • Table 3 shows the results of the stability tests of the protease which is absorbed into the soda.
  • EG ethylene glycol
  • PG propylene glycol
  • PEG polyethylene glycol 400

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Wood Science & Technology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • Zoology (AREA)
  • Biomedical Technology (AREA)
  • General Health & Medical Sciences (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Inorganic Chemistry (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Detergent Compositions (AREA)
  • Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
  • Medicinal Preparation (AREA)
  • Glanulating (AREA)
  • Confectionery (AREA)

Abstract

Selon l'invention, on obtient de nouvelles granules d'enzyme présntant de propriétés améliorées. L'élément de base desdites granules est un noyau constitué d'une particule présentant une taille de pore et une distribution de la taille des pores telles qu'elles permettent à une solution enzymatique de pénétrer dans ladite particule. Ainsi, le matériau constituant le noyau comprend l'enzyme sous forme liquide, ce qui élimine l'inconvénient d'avoir à traiter les enzymes sous forme de poudre. De plus, on obtient une bonne aptitude à l'écoulement et au dosage. Les granules contenant l'enzyme sont de préférence revêtues d'un matériau macromoléculaire filmogène. Ces granules ont une faible teneur en poussière et leur résistance mécanique est améliorée. L'invention concerne également un procédé permettant de préparer ces granules d'enzyme.
PCT/EP1994/001642 1993-05-18 1994-05-18 Procede de production d'enzyme exempte de poussiere WO1994026883A2 (fr)

Priority Applications (6)

Application Number Priority Date Filing Date Title
JP6525000A JPH07509141A (ja) 1993-05-18 1994-05-18 細塵を含まない酵素の製造方法
AU69705/94A AU677342B2 (en) 1993-05-18 1994-05-18 Process for dust-free enzyme manufacture
PL94307854A PL307854A1 (en) 1993-05-18 1994-05-18 Method of obtaining dust-free enzyme
EP94918349A EP0675952A1 (fr) 1993-05-18 1994-05-18 Procede de production d'enzyme exempte de poussiere
KR1019950700195A KR950702625A (ko) 1993-05-18 1994-05-18 비살포성 효소의 제조방법(process for dust-free enzyme manufacture)
FI950183A FI950183A0 (fi) 1993-05-18 1995-01-16 Menetelmä pölyämättömän entsyymin valmistamiseksi

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP93201428 1993-05-18
NL93201428.5 1993-05-18

Publications (3)

Publication Number Publication Date
WO1994026883A2 true WO1994026883A2 (fr) 1994-11-24
WO1994026883A9 WO1994026883A9 (fr) 1995-01-05
WO1994026883A3 WO1994026883A3 (fr) 1995-03-02

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ID=8213835

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP1994/001642 WO1994026883A2 (fr) 1993-05-18 1994-05-18 Procede de production d'enzyme exempte de poussiere

Country Status (8)

Country Link
EP (1) EP0675952A1 (fr)
KR (1) KR950702625A (fr)
CN (1) CN1110059A (fr)
AU (1) AU677342B2 (fr)
CA (1) CA2140530A1 (fr)
FI (1) FI950183A0 (fr)
PL (1) PL307854A1 (fr)
WO (1) WO1994026883A2 (fr)

Cited By (17)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1995022606A1 (fr) * 1994-02-21 1995-08-24 Novo Nordisk A/S Procede pour la production d'une preparation enzymatique immobilisee et utilisation de cette preparation
WO1996038527A1 (fr) * 1995-05-29 1996-12-05 Kao Corporation Substance granulee contenant une enzyme et son procede de preparation
WO1999033964A1 (fr) * 1997-12-23 1999-07-08 Novo Nordisk A/S Procede servant a immobiliser des enzymes
WO2000026335A1 (fr) * 1998-10-30 2000-05-11 The Procter & Gamble Company Composant solide resistant aux chocs
US6083538A (en) * 1997-07-22 2000-07-04 Dsm N.V. Bread improving composition
US6136772A (en) * 1996-04-12 2000-10-24 Novo Nordisk A/S Enzyme-containing granules and process for the production thereof
US6156548A (en) * 1997-12-23 2000-12-05 Novo Nordisk A/S Immobilization of enzymes with a fluidized bed for use in an organic medium
WO2001000042A1 (fr) * 1999-06-25 2001-01-04 Basf Aktiengesellschaft Additifs granules, revetus de polymeres et contenant des enzymes, destines a des aliments pour animaux, et procede de production correspondant
EP0913468A3 (fr) * 1997-07-22 2001-06-13 Dsm N.V. Composition pour l'amélioration du pain
US6500426B1 (en) 1997-06-04 2002-12-31 Rudolf Carolus Maria Barendse Carbohydrate-based enzyme-containing granules for use in animal feed
US6630436B1 (en) 1998-10-30 2003-10-07 The Procter & Gamble Company Impact resistant solid component
US7186533B2 (en) 1999-02-10 2007-03-06 Basf Aktiengesellschaft Granulates containing feed-enzymes
WO2008055626A1 (fr) * 2006-11-10 2008-05-15 Ab Enzymes Gmbh Substance à base de protéine, à résistance thermique renforcée
US7501269B2 (en) 2002-01-15 2009-03-10 Basf Aktiengesellschaft Granulates containing feed-enzymes
US7611877B2 (en) 2002-01-15 2009-11-03 Basf Aktiengesellschaft Granulates containing feed-enzymes
US9560877B2 (en) 2012-03-13 2017-02-07 General Mills, Inc. Cereal-based product with improved eating quality fortified with dietary fiber and/or calcium
WO2019076834A1 (fr) * 2017-10-16 2019-04-25 Novozymes A/S Granulés à faible teneur en poussière

Families Citing this family (6)

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Publication number Priority date Publication date Assignee Title
US6936289B2 (en) 1995-06-07 2005-08-30 Danisco A/S Method of improving the properties of a flour dough, a flour dough improving composition and improved food products
DE69841719D1 (de) 1997-04-09 2010-07-22 Danisco Lipase und Verwendung davon zur Verbesserung von Teigen und Backwaren
EP1387616B1 (fr) 2001-05-18 2007-05-16 Danisco A/S Procede permettant d'ameliorer la qualite de la pate et du pain
DE602004030000D1 (de) 2003-01-17 2010-12-23 Danisco Verfahren zur in-situ-herstellung eines emulgators in einem nahrungsmittel
GB0405637D0 (en) 2004-03-12 2004-04-21 Danisco Protein
WO2006008653A2 (fr) 2004-07-16 2006-01-26 Danisco A/S Proteine

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FR2446317A1 (fr) * 1979-01-12 1980-08-08 Solvay Granules complexes contenant des substances proteiniques actives et procedes pour leur fabrication, leur utilisation, et leur regeneration
US4689297A (en) * 1985-03-05 1987-08-25 Miles Laboratories, Inc. Dust free particulate enzyme formulation
DE3682443D1 (de) * 1985-06-28 1991-12-19 Procter & Gamble Granulierte zusammensetzung enthaltend ein trockenes bleichmittel und ein stabiles enzym.
US5177013A (en) * 1989-07-31 1993-01-05 Ajinomoto Co., Inc. Preparation of an immobilized lipase having a low water content without drying
EP0430395A1 (fr) * 1989-11-24 1991-06-05 Kingston Diagnostics, L.P. Enzymes stabilisées dispersées
ES2167319T3 (es) * 1991-10-07 2002-05-16 Genencor Int Granulo que contiene una enzima revestida.
DE69207727T2 (de) * 1991-11-11 1996-09-19 Akzo Nobel Nv Verfahren zur Herstellung von Salzgranulaten

Cited By (26)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5776741A (en) * 1994-02-21 1998-07-07 Novo Nordisk A/S Method of enzyme immobilization on a particulate silica carrier for synthesis inorganic media
WO1995022606A1 (fr) * 1994-02-21 1995-08-24 Novo Nordisk A/S Procede pour la production d'une preparation enzymatique immobilisee et utilisation de cette preparation
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WO1994026883A3 (fr) 1995-03-02
FI950183L (fi) 1995-01-16
FI950183A0 (fi) 1995-01-16
KR950702625A (ko) 1995-07-29
PL307854A1 (en) 1995-06-26
AU6970594A (en) 1994-12-12
CN1110059A (zh) 1995-10-11
EP0675952A1 (fr) 1995-10-11
CA2140530A1 (fr) 1994-11-24
AU677342B2 (en) 1997-04-17

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