FI108944B - Sieniperäisten ksylanaasigeenien kloonaus ja ilmentäminen - Google Patents
Sieniperäisten ksylanaasigeenien kloonaus ja ilmentäminen Download PDFInfo
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- FI108944B FI108944B FI921231A FI921231A FI108944B FI 108944 B FI108944 B FI 108944B FI 921231 A FI921231 A FI 921231A FI 921231 A FI921231 A FI 921231A FI 108944 B FI108944 B FI 108944B
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- dna sequence
- xylanase
- dna
- gene
- expression
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- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
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- DRTQHJPVMGBUCF-UHFFFAOYSA-N uracil arabinoside Natural products OC1C(O)C(CO)OC1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-UHFFFAOYSA-N 0.000 description 1
- 229940116269 uric acid Drugs 0.000 description 1
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Classifications
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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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K10/00—Animal feeding-stuffs
- A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
- A23K10/14—Pretreatment of feeding-stuffs with enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/189—Enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K30/00—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs
- A23K30/10—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder
- A23K30/15—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder using chemicals or microorganisms for ensilaging
- A23K30/18—Processes specially adapted for preservation of materials in order to produce animal feeding-stuffs of green fodder using chemicals or microorganisms for ensilaging using microorganisms or 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2477—Hemicellulases not provided in a preceding group
- C12N9/248—Xylanases
- C12N9/2482—Endo-1,4-beta-xylanase (3.2.1.8)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01008—Endo-1,4-beta-xylanase (3.2.1.8)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01032—Xylan endo-1,3-beta-xylosidase (3.2.1.32), i.e. endo-1-3-beta-xylanase
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- Microbiology (AREA)
- Genetics & Genomics (AREA)
- Polymers & Plastics (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Animal Husbandry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Physiology (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Fodder In General (AREA)
- Detergent Compositions (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Food Preservation Except Freezing, Refrigeration, And Drying (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Professional, Industrial, Or Sporting Protective Garments (AREA)
- Earth Drilling (AREA)
- Auxiliary Devices For And Details Of Packaging Control (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Treatment Of Sludge (AREA)
- Processing Of Solid Wastes (AREA)
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP90202020 | 1990-07-24 | ||
EP90202020 | 1990-07-24 | ||
NL9100137 | 1991-01-28 | ||
PCT/NL1991/000137 WO1992001793A1 (en) | 1990-07-24 | 1991-07-24 | Cloning and expression of xylanase genes from fungal origin |
Publications (3)
Publication Number | Publication Date |
---|---|
FI921231A0 FI921231A0 (fi) | 1992-03-20 |
FI921231A FI921231A (fi) | 1992-03-20 |
FI108944B true FI108944B (fi) | 2002-04-30 |
Family
ID=8205086
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
FI921231A FI108944B (fi) | 1990-07-24 | 1992-03-20 | Sieniperäisten ksylanaasigeenien kloonaus ja ilmentäminen |
FI921232A FI921232A0 (fi) | 1990-07-24 | 1992-03-20 | Enzymatisk behandling av ensilage. |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
FI921232A FI921232A0 (fi) | 1990-07-24 | 1992-03-20 | Enzymatisk behandling av ensilage. |
Country Status (19)
Country | Link |
---|---|
US (1) | US5358864A (xx) |
EP (3) | EP0468596B1 (xx) |
JP (2) | JPH05500907A (xx) |
KR (1) | KR100212232B1 (xx) |
AT (2) | ATE124844T1 (xx) |
AU (2) | AU647170B2 (xx) |
CA (2) | CA2067329A1 (xx) |
DE (3) | DE69111148T2 (xx) |
DK (2) | DK0463706T3 (xx) |
ES (1) | ES2086267T3 (xx) |
FI (2) | FI108944B (xx) |
HU (2) | HU215234B (xx) |
IE (3) | IE912582A1 (xx) |
IL (1) | IL98941A (xx) |
NO (2) | NO921133D0 (xx) |
NZ (2) | NZ239083A (xx) |
PL (2) | PL171271B1 (xx) |
PT (1) | PT98419B (xx) |
WO (2) | WO1992001793A1 (xx) |
Families Citing this family (89)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5837515A (en) * | 1990-05-16 | 1998-11-17 | Alko-Yhtiot Oy | Enzyme preparations and methods for their production |
NL9001388A (nl) * | 1990-06-19 | 1992-01-16 | Unilever Nv | Recombinant dna, cel die daarvan afgeleid dna bevat, enzym waarvoor het recombinant dna codeert en toepassingen daarvan. |
NZ239083A (en) * | 1990-07-24 | 1993-08-26 | Gist Brocades Nv | Endo-xylanase-containing silage composition |
GB9027303D0 (en) * | 1990-12-17 | 1991-02-06 | Enzymatix Ltd | Enzyme formulation |
US5863783A (en) * | 1991-03-27 | 1999-01-26 | Gist-Brocades, N.V. | Cloning and expression of DNA molecules encoding arabinan-degrading enzymes of fungal origin |
DK0672149T3 (da) * | 1991-12-09 | 2001-11-05 | Unilever Nv | Fremgangsmåde til fremstilling/udskilning af et protein med en transformeret skimmelsvamp ved anvendelse af ekspressions/udskilningsregulerende regioner afledt af et Aspergillus-endoxylanase II-gen |
CA2138383A1 (en) * | 1992-06-17 | 1993-12-23 | Geoffrey Peter Hazlewood | Recombinant xylanases |
BR9306576A (pt) * | 1992-06-17 | 1999-01-12 | Commw Scient Ind Res Org | Xilanase recombinante |
IL108175A0 (en) * | 1992-12-24 | 1994-04-12 | Gist Brocades Nv | Cloning and expression of xylanase B |
DE69435154D1 (de) * | 1993-03-10 | 2008-12-04 | Novozymes As | Enzyme mit Xylanaseaktivität aus Aspergillus aculeatus |
GB2279955B (en) * | 1993-07-15 | 1998-02-18 | Solvay | Xylanase derived from a Bacillus species, expression vectors for such xylanase and other proteins, host organisms therefor and use thereof |
FR2715802B1 (fr) * | 1994-02-04 | 1996-03-15 | Rhone Poulenc Nutrition Animal | Utilisation d'enzymes dans l'alimentation des animaux pour réduire les rejets azotés. |
US5448645A (en) * | 1994-02-28 | 1995-09-05 | Raymond Guerci International, Inc. | Active fan blade noise cancellation system |
DE69533473T2 (de) * | 1994-03-02 | 2005-01-20 | Novozymes A/S | Verarbeitung von pflantzlichem material mit xylanase |
WO1995023515A1 (en) * | 1994-03-02 | 1995-09-08 | Novo Nordisk A/S | Use of xylanase in baking |
GB9406317D0 (en) * | 1994-03-30 | 1994-05-25 | Finnfeeds Int Ltd | Use of an enzyme for assisting an animal to digest protein |
US6051431A (en) * | 1994-07-22 | 2000-04-18 | Dsm N.V. | Selection marker gene free recombinant strains: a method for obtaining them and the use of these strains |
US5871730A (en) * | 1994-07-29 | 1999-02-16 | Universite De Sherbrooke | Thermostable xylanase DNA, protein and methods of use |
US6300114B1 (en) | 1994-07-29 | 2001-10-09 | Rohm Enzyme Finland Oy | Sequences of xylanase and xylanase expression vectors |
US7816129B2 (en) | 1994-07-29 | 2010-10-19 | Ab Enzymes Gmbh | Production and secretion of proteins of bacterial origin in filamentous fungi |
US5935836A (en) * | 1994-07-29 | 1999-08-10 | Rohm Enzyme Finland Oy | Actinomadura xylanase sequences and methods of use |
GB9416841D0 (en) * | 1994-08-19 | 1994-10-12 | Finnfeeds Int Ltd | An enzyme feed additive and animal feed including it |
US5849559A (en) * | 1994-08-26 | 1998-12-15 | Gist-Brocades, B.V. | Arabinoxylan degrading enzymes |
ES2169219T5 (es) | 1995-01-26 | 2009-09-01 | Novozymes A/S | Aditivos alimenticios para animales que comprenden xilanasa. |
GB9505479D0 (en) * | 1995-03-17 | 1995-05-03 | Danisco | Enzyme |
EP0833928A1 (en) * | 1995-06-23 | 1998-04-08 | Danisco Ingredients A/S (Danisco A/S) | Novel beta-xylosidase, nucleotide sequence encoding it, and use thereof |
US5720971A (en) † | 1995-07-05 | 1998-02-24 | Her Majesty The Queen In Right Of Canada, As Represented By The Department Of Agriculture And Agri-Food Canada | Enzyme additives for ruminant feeds |
AU7294396A (en) * | 1995-10-13 | 1997-04-30 | Gist-Brocades B.V. | Protein detection |
US5902581A (en) * | 1995-12-04 | 1999-05-11 | Genencor International, Inc. | Xylanase from acidothermus cellulolyticus |
US6635464B1 (en) | 1995-12-18 | 2003-10-21 | Rohm Enzyme Finland Oy | Xylanases, genes encoding them, and uses thereof |
WO1997027290A1 (en) * | 1996-01-22 | 1997-07-31 | Novo Nordisk A/S | An enzyme with xylanase activity |
ES2111495B1 (es) * | 1996-07-19 | 1998-11-01 | Consejo Superior Investigacion | Cepa de levadura de panaderia cect10868 y cepa de panaderia cect10869. su metodo de obtencion por tecnicas de adn recombinante y su aplicacion como levaduras de panaderia. |
GB9704157D0 (en) | 1997-02-28 | 1997-04-16 | Danisco | Expression element |
WO1998039423A1 (fr) * | 1997-03-04 | 1998-09-11 | Meiji Seika Kaisha Ltd. | Xylanases mesophiles |
NZ502444A (en) | 1997-07-31 | 2001-11-30 | Dsm N | Polypeptides with cellobiohydrolase activity (CBH A and CBH B) from Aspergillus |
US7220542B2 (en) | 2000-07-17 | 2007-05-22 | Van Den Brink Johannes Maarten | Expression cloning in filamentous fungi |
BRPI9916507B1 (pt) * | 1998-12-23 | 2015-09-08 | Danisco | uso de xilanase bacteriana para a produção de um produto de panificação ou massa para preparação do mesmo e uso de uma sequência de aminoácidos |
WO2002003805A1 (en) | 2000-07-06 | 2002-01-17 | Novozymes A/S | Method of preparing a dough or a baked product made from a dough, with addition of lipolytic enzymes |
EP1301618A1 (en) | 2000-07-13 | 2003-04-16 | Danisco Sweeteners Oy | Method for the production of xylitol |
DK1319079T3 (da) | 2000-09-21 | 2013-01-07 | Basf Se | Talaromyces-xylanase |
AU2002331469B2 (en) | 2001-08-20 | 2008-04-24 | Cargill, Incorporated | Non-starch-polysaccharides |
US8022170B2 (en) | 2002-12-17 | 2011-09-20 | Ems-Chemie Ag | Copolyamides |
WO2004099400A2 (en) | 2003-05-09 | 2004-11-18 | Novozymes A/S | Variant lipolytic ensymes |
EP1482050A1 (en) * | 2003-05-28 | 2004-12-01 | Facultés Universitaires Notre-Dame de la Paix | Enzyme with xylanase activity at acidic ph |
WO2006078256A2 (en) | 2004-02-12 | 2006-07-27 | Novozymes, Inc. | Polypeptides having xylanase activity and polynucleotides encoding same |
JP2006219767A (ja) * | 2005-02-08 | 2006-08-24 | Univ Of Tsukuba | 製紙用化学パルプ中の不飽和ウロン酸の除去方法 |
AU2006247618A1 (en) | 2005-05-12 | 2006-11-23 | Martek Biosciences Corporation | Biomass hydrolysate and uses and production thereof |
US8268956B2 (en) | 2006-12-08 | 2012-09-18 | Ems-Chemie Ag | Transparent mold made of a polyamide molding material |
BRPI0806219A2 (pt) | 2007-01-16 | 2011-08-30 | Puratos Nv | método para aumentar num produto cozido no forno o nìvel de arabinoxilanos solúveis em água, produto cozido no forno, composição adequada para a preparação de um produto cozido no forno, massa para um produto cozido no forno e utilização de uma massa |
US7850382B2 (en) | 2007-01-18 | 2010-12-14 | Sanford, L.P. | Valve made from two materials and writing utensil with retractable tip incorporating same |
US7488130B2 (en) | 2007-02-01 | 2009-02-10 | Sanford, L.P. | Seal assembly for retractable instrument |
WO2008112459A2 (en) | 2007-03-09 | 2008-09-18 | Danisco Us Inc., Genencor Division | Alkaliphilic bacillus species a-amylase variants, compositions comprising a-amylase variants, and methods of use |
DK2132308T3 (da) | 2007-03-14 | 2012-03-05 | Danisco Us Inc | Trichoderma reesei a-amylase øger forsukring af majsstivelse |
US8143039B2 (en) | 2007-06-01 | 2012-03-27 | Sapphire Energy, Inc. | Use of genetically modified organisms to generate biomass degrading enzymes |
GB0718974D0 (en) | 2007-09-28 | 2007-11-07 | Univ Leuven Kath | oligosaccharides derived from arabinoxylan for prevention of gastrointestinal infection |
EP2060607B2 (de) | 2007-11-16 | 2019-11-27 | Ems-Patent Ag | Gefüllte Polyamidformmassen |
EP2554666B1 (en) | 2008-01-02 | 2015-08-05 | Danisco US Inc. | A process of obtaining ethanol without glucoamylase using pseudomonas saccharophila G4-amylase and variants thereof |
GB0805360D0 (en) | 2008-03-25 | 2008-04-30 | Univ Leuven Kath | Arabinoxylan oligosaccharide preparation |
US8226312B2 (en) | 2008-03-28 | 2012-07-24 | Sanford, L.P. | Valve door having a force directing component and retractable instruments comprising same |
JP5702714B2 (ja) | 2008-04-30 | 2015-04-15 | ダニスコ・ユーエス・インク | 新規キメラアルファアミラーゼ変異体 |
WO2009149271A2 (en) | 2008-06-06 | 2009-12-10 | Danisco Us Inc. | Production of glucose from starch using alpha-amylases from bacillus subtilis |
CN102112618A (zh) | 2008-06-06 | 2011-06-29 | 丹尼斯科美国公司 | 糖化酶组合物及其糖化方法 |
DK2297312T3 (da) | 2008-06-06 | 2013-12-16 | Danisco Us Inc | Alpha-amylasevarianter af Bacillus subtilis og fremgangsmåder til anvendelse heraf |
US8221012B2 (en) | 2008-11-07 | 2012-07-17 | Sanford, L.P. | Retractable instruments comprising a one-piece valve door actuating assembly |
US20110274786A1 (en) | 2009-01-16 | 2011-11-10 | Danisco A/S | Enzymatic generation of oligasaccharides from cereals or cereal bi-streams |
AR075137A1 (es) | 2009-01-16 | 2011-03-09 | Danisco | Generacion enzimatica de lipidos funcionales a partir de cereales o flujos secundarios de cereales |
US8393814B2 (en) | 2009-01-30 | 2013-03-12 | Sanford, L.P. | Retractable instrument having a two stage protraction/retraction sequence |
BRPI1012562B1 (pt) | 2009-03-31 | 2020-10-27 | Dupont Nutrition Biosciences Aps | método para reduzir a cor e/ou sabor desagradável e/ou desenvolvimento de mau cheiro em um farelo de cereal solubilizado |
DK3620518T3 (da) | 2009-05-19 | 2021-11-15 | Dupont Nutrition Biosci Aps | Amylasepolypeptid |
PL2365033T3 (pl) | 2010-03-12 | 2013-12-31 | Ems Patent Ag | Poliamidowa masa do formowania o modyfikowanej udarności oraz wytworzony z niej zbiornik |
FR2959515A1 (fr) | 2010-05-03 | 2011-11-04 | Puratos | Compositions riches en oligosaccharides d'arabinoxylane |
EP2412757B1 (de) | 2010-07-30 | 2013-11-13 | Ems-Patent Ag | Polyamidformmasse zur Herstellung von Formkörpern mit einer Weichgriffoberfläche sowie entsprechende Formkörper |
WO2012130969A1 (en) | 2011-03-29 | 2012-10-04 | Novozymes A/S | Process for production of a baked product |
SI2535365T1 (sl) | 2011-06-17 | 2014-02-28 | Ems-Patent Ag | Delno aromatične oblikovalne mase in njihova uporaba |
EP2666803B1 (de) | 2012-05-23 | 2018-09-05 | Ems-Patent Ag | Kratzfeste, transparente und zähe Copolyamidformmassen, hieraus hergestellte Formkörper und deren Verwendung |
EP2716716B1 (de) | 2012-10-02 | 2018-04-18 | Ems-Patent Ag | Polyamid-Formmassen und deren Verwendung bei der Herstellung von Formkörpern |
ES2527403T3 (es) | 2012-12-18 | 2015-01-23 | Ems-Patent Ag | Masa para moldeo de poliamida y cuerpos moldeados producidos a partir de ella |
US8759041B1 (en) * | 2013-02-12 | 2014-06-24 | Novozymes Inc. | Polypeptides having xylanase activity and polynucleotides encoding same |
EP2778190B1 (de) | 2013-03-15 | 2015-07-15 | Ems-Patent Ag | Polyamidformmasse sowie hieraus hergestellter Formkörper |
EP3126509A1 (en) | 2014-04-01 | 2017-02-08 | DuPont Nutrition Biosciences ApS | Method for increasing crude palm oil yields |
EP3234083B1 (en) | 2014-12-19 | 2018-12-12 | DuPont Nutrition Biosciences ApS | Recovery of oil from palm sludge |
BR112017018667A2 (pt) | 2015-03-04 | 2018-04-17 | Dupont Nutrition Biosci Aps | processamento de grão de cereal |
GB201522603D0 (en) | 2015-12-22 | 2016-02-03 | Dupont Nutrition Biosci Aps | Composition |
JP7094652B2 (ja) * | 2016-03-31 | 2022-07-04 | 日油株式会社 | 製パン用油脂組成物および製パン用穀粉生地 |
KR101898246B1 (ko) * | 2016-11-18 | 2018-09-13 | 전북대학교 산학협력단 | 케나프 사일리지의 제조방법 및 이에 따른 케나프 사일리지 |
JP7491542B2 (ja) * | 2019-09-09 | 2024-05-28 | 株式会社フジワラテクノアート | 基質培養物の製造方法及び基質培養物 |
JP7160071B2 (ja) * | 2020-08-17 | 2022-10-25 | 日油株式会社 | 製パン用油脂組成物および製パン用穀粉生地 |
WO2024019057A1 (ja) * | 2022-07-20 | 2024-01-25 | 天野エンザイム株式会社 | 腸内菌叢改善剤 |
EP4389906A1 (en) | 2022-12-21 | 2024-06-26 | Basf Se | Methods for the enzymatic treatment of whole stillage |
Family Cites Families (11)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IT1109471B (it) * | 1976-08-17 | 1985-12-16 | Deral Sa | Procedimento e prodotto per la conservazione e la valorizzazione di vegetali a verde e dei sotto prodotti umidi delle industrie agro alimentari |
US4212420A (en) * | 1979-06-18 | 1980-07-15 | International Business Machines Corporation | Ribbon storage device |
CA1280704C (en) * | 1985-12-03 | 1991-02-26 | Paul Ducroo | Production of beer |
FI84970C (fi) * | 1988-04-22 | 1992-02-25 | Suomen Sokeri Oy | Foerfarande foer foerbaettring av degens egenskaper och broedets kvalitet. |
FI881962A (fi) * | 1988-04-26 | 1989-10-27 | Cultor Oy | Foerfarande foer foerbaettring av fodrets smaeltbarhet och med foerfarandet framstaellt foder. |
CA1341226C (en) * | 1988-08-16 | 2001-05-01 | Wim Van Hartingsveldt | Gene replacement as a tool for the construction of aspergillus strains |
FI884668A (fi) * | 1988-10-11 | 1990-04-12 | Suomen Sokeri Oy | Foerfarande foer foerbaettrande av framstaellningsprocessen hos torra saedesprodukter med hjaelp av enzymbehandling. |
US5179021A (en) * | 1989-02-10 | 1993-01-12 | Gil Inc. (Now Ici Canada Inc.) | Pulp bleaching process comprising oxygen delignification and xylanase enzyme treatment |
WO1991015966A1 (en) * | 1990-04-18 | 1991-10-31 | Ssv-Development Oy | Enzyme treated forage for silage |
NL9001388A (nl) * | 1990-06-19 | 1992-01-16 | Unilever Nv | Recombinant dna, cel die daarvan afgeleid dna bevat, enzym waarvoor het recombinant dna codeert en toepassingen daarvan. |
NZ239083A (en) * | 1990-07-24 | 1993-08-26 | Gist Brocades Nv | Endo-xylanase-containing silage composition |
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