CA2243769A1 - Novel bread improving composition - Google Patents
Novel bread improving composition Download PDFInfo
- Publication number
- CA2243769A1 CA2243769A1 CA002243769A CA2243769A CA2243769A1 CA 2243769 A1 CA2243769 A1 CA 2243769A1 CA 002243769 A CA002243769 A CA 002243769A CA 2243769 A CA2243769 A CA 2243769A CA 2243769 A1 CA2243769 A1 CA 2243769A1
- Authority
- CA
- Canada
- Prior art keywords
- lipase
- granule
- coated
- lipid
- composition
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
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Classifications
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
- A21D8/00—Methods for preparing or baking dough
- A21D8/02—Methods for preparing dough; Treating dough prior to baking
- A21D8/04—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes
- A21D8/042—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes with 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
- 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
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material 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)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Food Science & Technology (AREA)
- Dispersion Chemistry (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
This invention relates to a coated lipase granule comprising lipase coated with a material which is impervious to lipid.
Description
CA 02243769 l998-07-22 Gist-brocades B.V. S-2874 NOVEL BREAD IMPROVING COMPOSITION
The present invention relates to a novel bread improving composition and its uses.
In recent years enzymes have been used to an increasing extent as highly useful aids to facilitate baking processes and improve the quality of baked products.
The use of lipase (EC 3.1.1.3) combined with other enzymes in baking is known (see European Patent EP 0585 988 B1 or International application WO 94/04035). Lipase catalyses the hydrolysis of triglycerides (lipids) into mono- and diglycerides and free fatty acids. Whereas the amount of such lipids is relatively low (0.5-2%) in the flour made from most cereal crops.
Many compositions used in the baking industry to improve the properties of bread contain substantial amounts of fats. We have found that lipase, when present in such compositions, generates free fatty acids during storage which strongly shortens the shelf-life of the compositions.
Coating of enzyme granules is used to prevent the formation of enzyme dust, especially for enzymes used in detergents. The enzyme granules may be coated with a material which forms a film. Such a coating is used to prevent dust formation, rather than to form a barrier between the enzyme and for other compounds, such as fats.
Theoretical calculations show that such a coating would not prevent fat penetrating into the enzyme particle.
Lipase is an enzyme which is still active at very low water concentrations. Since the compositions added to improve bread properties have a concentration of water higher than the water concentrations at which lipase is active, lipase in these compositions would be active.
Although the diffusion coefficients of lipids in the coating material of enzym particles is not known, one can estimate the value of these coefficients based on the coefficients known for other materials.
For proteins (eg. enzymes) in cheese the diffusion constant is 1 0-'2m2/s.
So the lowest diffusion coefficient for lipids would be in the order of 1 0-l5m2/s (this is two orders of magnitude lower than diffusion coefficient in bitumen).
In reality the diffusion constant of lipids in the coating material is probably higher than this.
The thickness of the coating on the granule of course varies, but the 10 upper limit is in the range of 25 ,um.
Based on the assumption that the effective diffusion coefficient is 10-'5m2/s one can calculate the distance within the coating at which the lipid concentration is halved per unit time. As an example for one second this distance is 32 nm, for one hour 2 ,um. Similar calculations for 25 ,um of coating material the upper limit of the thickness of the coating layer show thatafter 7 days the lipid concentration at the lipase is already half of the concentration of that in the composition. Some granules have a coating which is less than 25 ,um. Therefore for these the time needed for the lipid concentration at the lipase to be half that in the composition would be much shorter, since the time and distance are related to each other by a power factor of 2 (so either square or square root depending on the formulation of the equation used).
From further calculations one can conclude that even after one day lipid has already reached the enzyme inside the coated particle and therefore the lipid break down products which cause rancidity are being formed. However the times which are being estimated in these calculations are the upper limits for how long it will be to the start of lipase activity. In practice one should expect shorter times, as the diffusion coefficient is probably at least one order of magnitude larger. In addition, there is variation in the thickness of the coating, therefore it will often be much less than 25,um and hydrolysis of the lipid will begin as soon as any lipid has reacted the enzyme.
CA 02243769 l998-07-22 Therefore, the use of materials which form films to coat the lipase would not be expected to solve the problem of how to substantially reduce fat hydrolysis .
Surprisingly, we have found a coat formulation for the lipase which substantially reduces the amount of fat degradation which occurs during the storage period of the composition. In addition, the enzyme becomes fully active as soon as water is added by the baker in the mixer.
o We found that the coat formulation for the lipase prevents the occurrence of rancidity when the lipase granules are added to compositions containing lipids. This is surprising because as discussed above understanding of the physical and biochemical aspects of the system would lead one to expect that rancidity would occur.
Therefore, the lipase granule is coated with a suitable coating layer which substantially prevents fat degradation during storage. Suitable coating materials are sugars, starch, hydrolysed starch, starch derivatives, polyols such as polyethylene glycol, cellulose acetate phthalate, polyvinyl acetate phthalate, hydroxypropyl methylcellulose phthalate, and cellulose or cellulose 20 based compounds containing e.g. hydroxypropylcellulose, methyl cellulose, hydroxypropyl methyl cellulose and/or hydroxyethyl cellulose, and mixtures thereof. Optionally coating improving agents may be added. The lipase can, for instance, be produced as a granule or can be transferred onto a core material (e.g. using spraying technologies). Both methods result in enzyme 25 particles having a granule shape. The production of such enzyme granules is known .
In general the core materials used would be of food grade quality. NaCI
is an example of a core material which may be used.
In general the amounts of coating material will be 1 to 25 w/w% of the 30 final enzyme granule, preferably 3 to 15 wlw%.
CA 02243769 l998-07-22 The coated lipase can be added to compositions to improve the properties of bread. Normally bread is made from a dough comprising flour, water, yeast and in general salt. In many cases additional ingredients (such as enzymes) are added to improve the quality of the dough or bread. These ingredients can be added separately or added as a premix. Such a premix would be included in the term composition as used in this application.
The lipase may be a plant, animal or microbial lipase, and may be obtained from these sources. Preferably microbial lipase is used. As an 10 example, lipase from ~hizopus oryzae, commercially available from Gist-brocades under the trademark Fermizyme L10000, may be used. Other suitable lipases can be obtained from Humicol~, Rhizomucor, Candida, Aspergillus, Rhizopus or Pseudomonas species.
Lipase activity can be measured by pH-stat monitoring the production of free fatty acids from olive oil. 1 PLi unit is the amount of enzyme needed toproduce 1,umole free fatty acid per minute at pH 7.5 and 37âC from a neutral olive oil/water emulsion.
The following examples illustrate the invention:
Example 1 367 kg liquid lipase ultrafiltrate (activity: 17500 PLi/g, dry matter:
135g/l) was sprayed in a fluidized bed granulator at 40âC under pressure (4 25 bars) and with a flow rate of 1300g/min on 295 kg sieved sodium chloride (granule size: 60,um < 95% < 300~m). In the meantime a solution was prepared by mixing 41 kg maltodextrin (DE12, commercially available from ROQUETTE, Lestrem, France) and 2.14 kg Pharmacoat (Hydroxypropyl methylcellulose, commercially available from SEPPIC, Paris, France) in 64 kg 30 demineralized water. This solution was sprayed (after the lipase had been applied to the NaCI carrier) at 40~C under pressure (4 bars) with a flow rate CA 02243769 l998-07-22 of 1300g/min. Continuous air flow (6500m3/h) was maintained during both spraying operations.
Drying was then carried out by heating at 42~C for 10 minutes while maintaining the same continuous air-flow (6500m3/hi. The temperature was then finally brought down to 25~C under continuous air-flow.
This yielded 439 kg coated lipase:
activity: 12700 PLi/g (i.e. enzymatic yield is 87%) moisture: 8.1 %
granule size distribution: 125~m < 41 % < 315,L~m o 315,um < 51 % < 400L/m thickness coating layer: 101~m .
Example 2 301 Kg liquid lipase ultrafiltrate (activity: 17500 PLI/g, dry matter:
15 135g/l) was sprayed at 40~C under pressure (5 bars) and with a flow rate of 1300g/min on 242 kg sieved sodium chloride (granule size:
60,um<95%<300~m). In the meantime a solution was prepared by mixing 33 kg maltodextrin and 1.75 kg Pharmacoat in 53 kg demineralized water.
This solution was sprayed (after the lipase had been applied to the NaCI
20 carrier) at 40~C under pressure (5 bars) with a flow rate of 1000g/min.
Continuous air flow (7000m31h) was maintained during both spraying operations.
Drying was then carried out by heating at 42~C for 12 minutes while maintaining the same continuous air-flow (7000m3/h). The temperature was 25 then finally brought down to 25~C under continuous air-flow (6500m31h).
This yielded 361 kg coated lipase:
activity: 13400 PLi/g (i.e. enzymatic yield is g2%) moisture: 7.2%
granule size distribution: 1251~m < 59% < 315,um 315~m< 37% <400,um thickness coating layer: 10~m.
Example 3 The following two compositions were prepared:
Salt 42 % 42 %
Hard fat soy 38 4.8 % 24 %
Fat kernels 80% soy fat 38 24 % 19 %
Soy flour 19 % 9.45 %
Starch 9.2 %
Fermizyme L10000 1 %
Coated lipase, 13400 Pli/g 0.75 %
These compositions are examples of compositions which may be used to o improve the properties of bread.
Fermizyme L10000 is a powder lipase standardized to 10000 PLi/g.
The coated lipase is from Example 2.
The compositions were stored at 25~C. Every two to three days the smell of the compositions was judged. The composition containing Fermizyme L10000 started getting rancid after two days. However, in the composition containing coated lipase no rancidity developed within 60 days. The lipase activity was not significantly decreased during storage.
The present invention relates to a novel bread improving composition and its uses.
In recent years enzymes have been used to an increasing extent as highly useful aids to facilitate baking processes and improve the quality of baked products.
The use of lipase (EC 3.1.1.3) combined with other enzymes in baking is known (see European Patent EP 0585 988 B1 or International application WO 94/04035). Lipase catalyses the hydrolysis of triglycerides (lipids) into mono- and diglycerides and free fatty acids. Whereas the amount of such lipids is relatively low (0.5-2%) in the flour made from most cereal crops.
Many compositions used in the baking industry to improve the properties of bread contain substantial amounts of fats. We have found that lipase, when present in such compositions, generates free fatty acids during storage which strongly shortens the shelf-life of the compositions.
Coating of enzyme granules is used to prevent the formation of enzyme dust, especially for enzymes used in detergents. The enzyme granules may be coated with a material which forms a film. Such a coating is used to prevent dust formation, rather than to form a barrier between the enzyme and for other compounds, such as fats.
Theoretical calculations show that such a coating would not prevent fat penetrating into the enzyme particle.
Lipase is an enzyme which is still active at very low water concentrations. Since the compositions added to improve bread properties have a concentration of water higher than the water concentrations at which lipase is active, lipase in these compositions would be active.
Although the diffusion coefficients of lipids in the coating material of enzym particles is not known, one can estimate the value of these coefficients based on the coefficients known for other materials.
For proteins (eg. enzymes) in cheese the diffusion constant is 1 0-'2m2/s.
So the lowest diffusion coefficient for lipids would be in the order of 1 0-l5m2/s (this is two orders of magnitude lower than diffusion coefficient in bitumen).
In reality the diffusion constant of lipids in the coating material is probably higher than this.
The thickness of the coating on the granule of course varies, but the 10 upper limit is in the range of 25 ,um.
Based on the assumption that the effective diffusion coefficient is 10-'5m2/s one can calculate the distance within the coating at which the lipid concentration is halved per unit time. As an example for one second this distance is 32 nm, for one hour 2 ,um. Similar calculations for 25 ,um of coating material the upper limit of the thickness of the coating layer show thatafter 7 days the lipid concentration at the lipase is already half of the concentration of that in the composition. Some granules have a coating which is less than 25 ,um. Therefore for these the time needed for the lipid concentration at the lipase to be half that in the composition would be much shorter, since the time and distance are related to each other by a power factor of 2 (so either square or square root depending on the formulation of the equation used).
From further calculations one can conclude that even after one day lipid has already reached the enzyme inside the coated particle and therefore the lipid break down products which cause rancidity are being formed. However the times which are being estimated in these calculations are the upper limits for how long it will be to the start of lipase activity. In practice one should expect shorter times, as the diffusion coefficient is probably at least one order of magnitude larger. In addition, there is variation in the thickness of the coating, therefore it will often be much less than 25,um and hydrolysis of the lipid will begin as soon as any lipid has reacted the enzyme.
CA 02243769 l998-07-22 Therefore, the use of materials which form films to coat the lipase would not be expected to solve the problem of how to substantially reduce fat hydrolysis .
Surprisingly, we have found a coat formulation for the lipase which substantially reduces the amount of fat degradation which occurs during the storage period of the composition. In addition, the enzyme becomes fully active as soon as water is added by the baker in the mixer.
o We found that the coat formulation for the lipase prevents the occurrence of rancidity when the lipase granules are added to compositions containing lipids. This is surprising because as discussed above understanding of the physical and biochemical aspects of the system would lead one to expect that rancidity would occur.
Therefore, the lipase granule is coated with a suitable coating layer which substantially prevents fat degradation during storage. Suitable coating materials are sugars, starch, hydrolysed starch, starch derivatives, polyols such as polyethylene glycol, cellulose acetate phthalate, polyvinyl acetate phthalate, hydroxypropyl methylcellulose phthalate, and cellulose or cellulose 20 based compounds containing e.g. hydroxypropylcellulose, methyl cellulose, hydroxypropyl methyl cellulose and/or hydroxyethyl cellulose, and mixtures thereof. Optionally coating improving agents may be added. The lipase can, for instance, be produced as a granule or can be transferred onto a core material (e.g. using spraying technologies). Both methods result in enzyme 25 particles having a granule shape. The production of such enzyme granules is known .
In general the core materials used would be of food grade quality. NaCI
is an example of a core material which may be used.
In general the amounts of coating material will be 1 to 25 w/w% of the 30 final enzyme granule, preferably 3 to 15 wlw%.
CA 02243769 l998-07-22 The coated lipase can be added to compositions to improve the properties of bread. Normally bread is made from a dough comprising flour, water, yeast and in general salt. In many cases additional ingredients (such as enzymes) are added to improve the quality of the dough or bread. These ingredients can be added separately or added as a premix. Such a premix would be included in the term composition as used in this application.
The lipase may be a plant, animal or microbial lipase, and may be obtained from these sources. Preferably microbial lipase is used. As an 10 example, lipase from ~hizopus oryzae, commercially available from Gist-brocades under the trademark Fermizyme L10000, may be used. Other suitable lipases can be obtained from Humicol~, Rhizomucor, Candida, Aspergillus, Rhizopus or Pseudomonas species.
Lipase activity can be measured by pH-stat monitoring the production of free fatty acids from olive oil. 1 PLi unit is the amount of enzyme needed toproduce 1,umole free fatty acid per minute at pH 7.5 and 37âC from a neutral olive oil/water emulsion.
The following examples illustrate the invention:
Example 1 367 kg liquid lipase ultrafiltrate (activity: 17500 PLi/g, dry matter:
135g/l) was sprayed in a fluidized bed granulator at 40âC under pressure (4 25 bars) and with a flow rate of 1300g/min on 295 kg sieved sodium chloride (granule size: 60,um < 95% < 300~m). In the meantime a solution was prepared by mixing 41 kg maltodextrin (DE12, commercially available from ROQUETTE, Lestrem, France) and 2.14 kg Pharmacoat (Hydroxypropyl methylcellulose, commercially available from SEPPIC, Paris, France) in 64 kg 30 demineralized water. This solution was sprayed (after the lipase had been applied to the NaCI carrier) at 40~C under pressure (4 bars) with a flow rate CA 02243769 l998-07-22 of 1300g/min. Continuous air flow (6500m3/h) was maintained during both spraying operations.
Drying was then carried out by heating at 42~C for 10 minutes while maintaining the same continuous air-flow (6500m3/hi. The temperature was then finally brought down to 25~C under continuous air-flow.
This yielded 439 kg coated lipase:
activity: 12700 PLi/g (i.e. enzymatic yield is 87%) moisture: 8.1 %
granule size distribution: 125~m < 41 % < 315,L~m o 315,um < 51 % < 400L/m thickness coating layer: 101~m .
Example 2 301 Kg liquid lipase ultrafiltrate (activity: 17500 PLI/g, dry matter:
15 135g/l) was sprayed at 40~C under pressure (5 bars) and with a flow rate of 1300g/min on 242 kg sieved sodium chloride (granule size:
60,um<95%<300~m). In the meantime a solution was prepared by mixing 33 kg maltodextrin and 1.75 kg Pharmacoat in 53 kg demineralized water.
This solution was sprayed (after the lipase had been applied to the NaCI
20 carrier) at 40~C under pressure (5 bars) with a flow rate of 1000g/min.
Continuous air flow (7000m31h) was maintained during both spraying operations.
Drying was then carried out by heating at 42~C for 12 minutes while maintaining the same continuous air-flow (7000m3/h). The temperature was 25 then finally brought down to 25~C under continuous air-flow (6500m31h).
This yielded 361 kg coated lipase:
activity: 13400 PLi/g (i.e. enzymatic yield is g2%) moisture: 7.2%
granule size distribution: 1251~m < 59% < 315,um 315~m< 37% <400,um thickness coating layer: 10~m.
Example 3 The following two compositions were prepared:
Salt 42 % 42 %
Hard fat soy 38 4.8 % 24 %
Fat kernels 80% soy fat 38 24 % 19 %
Soy flour 19 % 9.45 %
Starch 9.2 %
Fermizyme L10000 1 %
Coated lipase, 13400 Pli/g 0.75 %
These compositions are examples of compositions which may be used to o improve the properties of bread.
Fermizyme L10000 is a powder lipase standardized to 10000 PLi/g.
The coated lipase is from Example 2.
The compositions were stored at 25~C. Every two to three days the smell of the compositions was judged. The composition containing Fermizyme L10000 started getting rancid after two days. However, in the composition containing coated lipase no rancidity developed within 60 days. The lipase activity was not significantly decreased during storage.
Claims (14)
1. A coated lipase granule comprising lipase coated with a material which is impervious to lipid.
2. A granule according to claim 1 in which the lipase is present in granular form and then coated with the lipid impervious material.
3. A granule according to claim 1 in which the lipase is present on the outer surface of a particle and the lipase coated particle has an outer coat of the lipid impervious material.
4. A granule according to claim 1 in which the lipase has been absorbed by a particle and then coated with the lipid impervious material.
5. A granule according to any one of the preceding claims in which the coating is 1 to 25 w/w% of the coated lipase granule.
6. A granule according to any one of the preceding claims in which the lipase is from microbial origin.
7. A method of making a granule as defined in any one of the preceding claims, the method comprising coating either (i) a granule comprising a lipase;
or (ii) a carrier particle comprising a lipase with a lipid impervious material.
or (ii) a carrier particle comprising a lipase with a lipid impervious material.
8. A bread improver composition comprising a granule as defined in any one of claims 1 to 6 or a granule made by a method as defined in claim 7.
9. A composition according to claim 8 which further comprises fat.
10. Use of a granule as defined in any one of claims 1 to 6, a granule made by a method as defined in claim 7 or a composition as defined in claim 8 or 9 for hydrolysing a lipid present in dough.
11. A dough comprising a coated lipase granule as defined in any one of claims 1 to 6, a granule made by a method as defined in claim 7 or a composition as defined in claim 8 or 9.
12. A method of making a dough comprising adding together water, flour, yeast and optionally salt, and a granule as defined in any one of claims 1 to 6, a granule made by a method as defined in claim 7 or a composition as defined in claim 8 or 9; or supplementing a dough with such a granule or composition.
13. Use of a lipid-impervious material as a coating to prevent a lipase degrading a lipid in a composition as defined in claim 8 or 9.
14. Use of coated lipase to prevent the occurrence of rancidity when the lipase is brought into contact with a fat during storage, whereby the lipaseis coated with a fat-impervious material.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP97202292 | 1997-07-22 | ||
| EP97202292.5 | 1997-07-22 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2243769A1 true CA2243769A1 (en) | 1999-01-22 |
Family
ID=8228580
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002243769A Abandoned CA2243769A1 (en) | 1997-07-22 | 1998-07-22 | Novel bread improving composition |
Country Status (3)
| Country | Link |
|---|---|
| US (1) | US6083538A (en) |
| JP (1) | JPH11113479A (en) |
| CA (1) | CA2243769A1 (en) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2000226335A (en) * | 1998-12-04 | 2000-08-15 | Amano Pharmaceut Co Ltd | Oral enzyme preparation, enzyme-containing food material and method for internal use of enzyme preparation |
| PT1069832E (en) * | 1999-02-10 | 2004-08-31 | Basf Ag | FEEDING FOR ANIMALS OF A HIGHER NUTRIENT VALUE METHOD FOR THEIR PRODUCTION AND THEIR USE OF A POLYETHYLENE GLYCOL COMPOUND |
| DE19929257A1 (en) | 1999-06-25 | 2000-12-28 | Basf Ag | Production of polymer-coated granulated animal feed additive, useful in production of pelletized animal feed, involves granulating mixture of carrier and enzyme and coating with suitable organic polymer |
| WO2002019828A1 (en) * | 2000-09-08 | 2002-03-14 | Novozymes A/S | A dough composition comprising a lipid-encapsulated enzyme |
| PL362457A1 (en) * | 2000-12-20 | 2004-11-02 | Dsm Ip Assets B.V. | Liquid yeast compositions |
| BR0306917A (en) * | 2002-01-15 | 2004-11-09 | Basf Ag | Process for the preparation of a pellet, enzyme-containing pellet, process for the preparation of an animal feed, or a premix or precursor for an animal feed, feed composition, process for promoting the growth of an animal , and, use of a granulate |
| US6923994B2 (en) * | 2002-08-08 | 2005-08-02 | Bakery Technology Centre, B.V. | Process for producing bread with extended shelf life, bread dough and bread improver composition for producing such bread |
| CN101680172B (en) * | 2007-05-16 | 2013-04-17 | 巴科曼实验室国际公司 | Methods to control organic contaminants in fibers |
| JP5978676B2 (en) * | 2012-03-16 | 2016-08-24 | 三菱化学フーズ株式会社 | Method for dispersing glycolipid-degrading enzyme in fats and oils, fat composition and method for producing flour products |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6192570A (en) * | 1984-10-12 | 1986-05-10 | Showa Denko Kk | Enzyme granulation |
| US4849227A (en) * | 1986-03-21 | 1989-07-18 | Eurasiam Laboratories, Inc. | Pharmaceutical compositions |
| DK435687D0 (en) * | 1987-08-21 | 1987-08-21 | Novo Industri As | ENZYM containing granules and processes for their preparation |
| US5258132A (en) * | 1989-11-15 | 1993-11-02 | Lever Brothers Company, Division Of Conopco, Inc. | Wax-encapsulated particles |
| ATE135163T1 (en) * | 1992-07-27 | 1996-03-15 | Gist Brocades Nv | ENZYME PRODUCT AND METHOD FOR IMPROVING THE QUALITY OF BREAD |
| DK104592D0 (en) * | 1992-08-21 | 1992-08-21 | Novo Nordisk As | COURSE OF ACTION |
| KR950702625A (en) * | 1993-05-18 | 1995-07-29 | 한스 발터 라벤 | PROCESS FOR DUST-FREE ENZYME MANUFACTURE |
| DE4329463A1 (en) * | 1993-09-01 | 1995-03-02 | Cognis Bio Umwelt | More enzyme granules |
| CA2231667C (en) * | 1995-10-06 | 2007-08-21 | Genencor International, Inc. | Microgranule for food/feed applications |
-
1998
- 1998-07-22 JP JP10205925A patent/JPH11113479A/en active Pending
- 1998-07-22 CA CA002243769A patent/CA2243769A1/en not_active Abandoned
- 1998-07-22 US US09/120,420 patent/US6083538A/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPH11113479A (en) | 1999-04-27 |
| US6083538A (en) | 2000-07-04 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued | ||
| FZDE | Discontinued |
Effective date: 20041012 |