BRPI0616721A2 - métodos para degradar ou converter um material celulósico e para produzir uma substáncia, e, composição detergente - Google Patents
métodos para degradar ou converter um material celulósico e para produzir uma substáncia, e, composição detergente Download PDFInfo
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- BRPI0616721A2 BRPI0616721A2 BRPI0616721-7A BRPI0616721A BRPI0616721A2 BR PI0616721 A2 BRPI0616721 A2 BR PI0616721A2 BR PI0616721 A BRPI0616721 A BR PI0616721A BR PI0616721 A2 BRPI0616721 A2 BR PI0616721A2
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Classifications
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- C—CHEMISTRY; METALLURGY
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
- C12P7/04—Preparation of oxygen-containing organic compounds containing a hydroxy group acyclic
- C12P7/06—Ethanol, i.e. non-beverage
- C12P7/08—Ethanol, i.e. non-beverage produced as by-product or from waste or cellulosic material substrate
- C12P7/10—Ethanol, i.e. non-beverage produced as by-product or from waste or cellulosic material substrate substrate containing cellulosic material
-
- 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)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
-
- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
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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
- 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)
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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
- 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)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/04—Alpha- or beta- amino acids
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/24—Preparation of oxygen-containing organic compounds containing a carbonyl group
- C12P7/26—Ketones
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
-
- 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)
- C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
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- 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)
- C12Y302/01021—Beta-glucosidase (3.2.1.21)
-
- C—CHEMISTRY; METALLURGY
- C13—SUGAR INDUSTRY
- C13K—SACCHARIDES OBTAINED FROM NATURAL SOURCES OR BY HYDROLYSIS OF NATURALLY OCCURRING DISACCHARIDES, OLIGOSACCHARIDES OR POLYSACCHARIDES
- C13K1/00—Glucose; Glucose-containing syrups
- C13K1/02—Glucose; Glucose-containing syrups obtained by saccharification of cellulosic materials
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
- Y02E50/00—Technologies for the production of fuel of non-fossil origin
- Y02E50/10—Biofuels, e.g. bio-diesel
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
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- Health & Medical Sciences (AREA)
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- General Engineering & Computer Science (AREA)
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- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
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- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Emergency Medicine (AREA)
- Virology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Detergent Compositions (AREA)
- Compositions Of Macromolecular Compounds (AREA)
Applications Claiming Priority (3)
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| US72257905P | 2005-09-30 | 2005-09-30 | |
| US60/722579 | 2005-09-30 | ||
| PCT/US2006/038556 WO2007089290A2 (en) | 2005-09-30 | 2006-09-29 | Methods for enhancing the degradation or conversion of cellulosic material |
Publications (1)
| Publication Number | Publication Date |
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| BRPI0616721A2 true BRPI0616721A2 (pt) | 2011-06-28 |
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Country Status (9)
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| US (3) | US7608689B2 (enExample) |
| JP (1) | JP5129142B2 (enExample) |
| KR (1) | KR20080069980A (enExample) |
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| AU (1) | AU2006337184B2 (enExample) |
| BR (1) | BRPI0616721A2 (enExample) |
| CA (1) | CA2623908A1 (enExample) |
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| WO (1) | WO2007089290A2 (enExample) |
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| US7883872B2 (en) * | 1996-10-10 | 2011-02-08 | Dyadic International (Usa), Inc. | Construction of highly efficient cellulase compositions for enzymatic hydrolysis of cellulose |
| AU771539C (en) * | 1998-10-06 | 2005-01-13 | Dyadic International (Usa), Inc. | Transformation system in the field of filamentous fungal hosts |
| US7045331B2 (en) * | 2001-12-18 | 2006-05-16 | Genencor International, Inc. | EGVII endoglucanase and nucleic acids encoding the same |
| EP2532684A3 (en) | 2003-11-28 | 2013-03-20 | Eastman Chemical Company | Cellulose interpolymers and method of oxidation |
| CN1946835A (zh) | 2004-04-27 | 2007-04-11 | 巴克斯特国际公司 | 搅拌罐反应器系统 |
| MX2008014052A (es) * | 2006-05-01 | 2009-01-28 | Bnt Force Biodegradable Polyme | Composición de polímero biodegradable novedosa, útil para la preparacion de plástico biodegradable y proceso para la preparación de dicha composición. |
| DK2046819T3 (da) | 2006-07-21 | 2015-06-22 | Novozymes Inc | Fremgangsmåder til forøgelse af secernering af polypeptider med biologisk aktivitet |
| US20080090283A1 (en) * | 2006-10-13 | 2008-04-17 | Rowan Universtity | Ethanol resistant and furfural resistant strains of E. coli FBR5 for production of ethanol from cellulosic biomass |
| NZ606220A (en) | 2006-10-26 | 2014-05-30 | Xyleco Inc | Processing biomass |
| US9862956B2 (en) | 2006-12-10 | 2018-01-09 | Danisco Us Inc. | Expression and high-throughput screening of complex expressed DNA libraries in filamentous fungi |
| US8680252B2 (en) | 2006-12-10 | 2014-03-25 | Dyadic International (Usa), Inc. | Expression and high-throughput screening of complex expressed DNA libraries in filamentous fungi |
| DK2069491T3 (en) | 2007-05-10 | 2018-04-09 | Novozymes Inc | COMPOSITIONS AND PROCEDURES FOR IMPROVING THE DECOMPOSITION OR CONVERSION OF CELLULOSE SUBSTANCES |
| BRPI0812267A2 (pt) * | 2007-05-31 | 2014-10-14 | Novozymes Inc | Célula hospedeira fúngica filamentosa, método para produzir uma composição de proteína celulolítica, composição de proteína celulolítica, e, métodos para degradar ou converter um material, contendo celulose e para produzir um produto de fermentação |
| EP2064323B2 (en) * | 2007-05-31 | 2024-06-19 | Novozymes Inc. | Methods of increasing the cellulolytic enhancing activity of a polypeptide |
| AU2012204055B2 (en) * | 2007-05-31 | 2013-11-14 | Novozymes, Inc. | Methods of increasing the cellulolytic enhancing activity of a polypeptide |
| CN101784659B (zh) | 2007-05-31 | 2016-05-18 | 诺维信股份有限公司 | 具有纤维素分解增强活性的多肽和编码它的多核苷酸 |
| MX2009013188A (es) * | 2007-06-27 | 2010-02-24 | Novozymes As | Metodos para producir productos de fermentacion. |
| US7923236B2 (en) * | 2007-08-02 | 2011-04-12 | Dyadic International (Usa), Inc. | Fungal enzymes |
| US20090043686A1 (en) * | 2007-08-10 | 2009-02-12 | Archer-Daniels-Midland Company | Processing arrangements for biomass byproducts and biomass derivative products |
| GB0716702D0 (en) * | 2007-08-28 | 2007-10-10 | Biocatalysts Ltd | Enzyme productions |
| WO2009033071A2 (en) | 2007-09-07 | 2009-03-12 | Dyadic International, Inc. | Novel fungal enzymes |
| WO2009079634A1 (en) * | 2007-12-18 | 2009-06-25 | Georgia Tech Research Corporation | Systems and methods for altering rates of enzymatic processes |
| CN101945889A (zh) | 2007-12-19 | 2011-01-12 | 诺维信公司 | 具有纤维素分解增强活性的多肽和编码该多肽的多核苷酸 |
| BRPI0821230A2 (pt) | 2007-12-19 | 2019-09-24 | Novozymes As | "constructo de ácido nucleico, cédula microbiana hospedeira recombinante, métodos para priduzir um polipeptídeo tendo atividade intensificadora celulolítica, para produzir um mutante de uma cédula precursora, para inibir a expressão de um polipeptídeo com atividade de intensificação celulolítica em uma célula, para produzir uma proteína, para degradar ou converter um material celulósico, e, para fermentar um material celulósico" |
| CA2709367A1 (en) | 2007-12-19 | 2009-07-09 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US20110039311A1 (en) | 2008-03-27 | 2011-02-17 | Novozymes A/S | Process for producing fermentation product from lignocellulose-containing material |
| DE102008024084A1 (de) * | 2008-05-17 | 2009-11-19 | Clariant International Ltd. | Wasch- und Reinigungsmittel |
| BRPI0916567A2 (pt) * | 2008-07-29 | 2015-08-18 | Dsm Ip Assets Bv | Método para modificar material de carboidrato de não amido com o uso de enzimas peroxidase |
| FR2935986B1 (fr) * | 2008-09-12 | 2012-11-23 | Inst Francais Du Petrole | Variants de beta-glucosidase a activite amelioree et leurs utilisations. |
| WO2010045576A2 (en) * | 2008-10-17 | 2010-04-22 | Mascoma Corporation | Production of pure lignin from lignocellulosic biomass |
| US8518684B2 (en) | 2008-11-18 | 2013-08-27 | Novozymes, Inc. | Methods and compositions for degrading cellulosic material |
| WO2010065830A1 (en) | 2008-12-04 | 2010-06-10 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US8337663B2 (en) | 2008-12-19 | 2012-12-25 | Novozymes, Inc. | Methods for increasing hydrolysis of cellulosic material |
| EP2379732A2 (en) * | 2008-12-19 | 2011-10-26 | Novozymes Inc. | Methods for increasing enzymatic hydrolysis of cellulosic material in the presence of a peroxidase |
| WO2010080527A1 (en) | 2008-12-19 | 2010-07-15 | Novozymes, Inc. | Methods for determining cellulolytic enhancing activity of a polypeptide |
| WO2010078392A2 (en) | 2008-12-31 | 2010-07-08 | Novozymes North America, Inc. | Processes of producing fermentation products |
| US8604277B2 (en) | 2009-01-28 | 2013-12-10 | Novozymes, Inc. | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
| US8629324B2 (en) | 2009-01-30 | 2014-01-14 | Novozymes, Inc. | Polypeptides having expansin activity and polynucleotides encoding same |
| RU2394102C1 (ru) * | 2009-04-30 | 2010-07-10 | Учреждение Российской Академии Наук Институт Биохимической Физики Им. Н.М. Эмануэля Ран (Ибхф Ран) | Средство для повышения целлюлазной активности |
| CN104480088A (zh) * | 2009-06-02 | 2015-04-01 | 诺维信股份有限公司 | 具有纤维二糖水解酶活性的多肽和编码该多肽的多核苷酸 |
| CN102803194B (zh) | 2009-06-13 | 2016-01-20 | 莱诺维亚公司 | 由含碳水化合物的物质生产戊二酸和衍生物 |
| US8669397B2 (en) | 2009-06-13 | 2014-03-11 | Rennovia, Inc. | Production of adipic acid and derivatives from carbohydrate-containing materials |
| BRPI1010708B1 (pt) | 2009-06-13 | 2018-04-03 | Rennovia, Inc. | "processos para preparar um produto de ácido adípico, e ácido adípico ou derivado do mesmo" |
| EP2451957B1 (en) | 2009-07-07 | 2017-11-15 | Novozymes Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| EP2454590B1 (en) | 2009-07-17 | 2016-09-07 | Novozymes A/S | A method of analyzing cellulose decay in cellulosic material hydrolysis |
| BR112012006032A2 (pt) | 2009-09-17 | 2015-09-08 | Novozymes Inc | polipetídeo isolado, composição, célula hospedeira recombinante, métodos para produzir o polipetídeo, um polipetídeo tendo atividade realçadora celulolítica, um mutante de uma célula precursora, uma proteína e um produto de fermentação, planta transgênica, parte de planta ou célula de planta, molécula de rna inibidora de filamento duplo(rsrna), e, métodos para inibir a expressão de um polipetídeo tendo atividade realçadora celulolítica em uma célula, degradar ou converter um polipetídeo isolado, composição, célula hospedeira recombinante, métodos para produzir o polipetídeo, um polipetídeo tendo atividade realçadora celulolítica, um mutante de uma célula precursora, uma proteína e um produto de fermentação, planta transgênica, parte de planta ou célula de planta, molécula de rna inibidora de filamento duplo (dsrna), e, métodos para inibir a expressão de um polipetídeo tendo atividade realçadora celulolítica em uma célula, degradar ou converter um material celulósico e fermentar um material celulósico. |
| EP2478095A1 (en) | 2009-09-18 | 2012-07-25 | Novozymes Inc. | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
| EP2480660B1 (en) | 2009-09-23 | 2020-08-05 | Danisco US Inc. | Novel glycosyl hydrolase enzymes and uses thereof |
| US8211665B2 (en) | 2009-09-29 | 2012-07-03 | Novozymes, Inc. | Polypeptides having xylanase activity and polynucleotides encoding same |
| WO2011041397A1 (en) | 2009-09-29 | 2011-04-07 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US8586829B2 (en) | 2009-09-30 | 2013-11-19 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| EP2977382A3 (en) | 2009-09-30 | 2016-05-11 | Novozymes Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US20110183389A1 (en) * | 2009-10-26 | 2011-07-28 | Van Walsum G Peter | Production of lactic acid from hemicellulose extracts |
| BR112012008260A2 (pt) | 2009-11-06 | 2015-09-15 | Novozymes Inc E Novozymes As | polipeptídeo, polinucleotídeo, métodos para produzir o polipeptídeo, para produzir um mutante de uma célula precursora, para inibir a expressão de um polipeptídeo, para produzir uma proteína, para degradar ou converter um material celulósico, para produzir um produto de fermentação, para fermentar um material celulósico, planta transgênica, parte da planta ou célula da planta,e, molécula de rna inibitória de filamento duplo. |
| ES2574054T3 (es) | 2009-11-06 | 2016-06-14 | Novozymes, Inc. | Polipéptidos con actividad de xilanasa y polinucleótidos que los codifican |
| WO2011067349A1 (en) | 2009-12-03 | 2011-06-09 | Novozymes A/S | Variants of a polypeptide with lipolytic activity and improved stability |
| CN107287250A (zh) | 2009-12-23 | 2017-10-24 | 丹尼斯科美国公司 | 提高同步糖化发酵反应效率的方法 |
| US20120220513A1 (en) | 2009-12-29 | 2012-08-30 | Novozymes A/S | Polypeptides Having Detergency Enhancing Effect |
| BR112012018422A2 (pt) | 2010-01-29 | 2015-09-15 | Novozymes As | processo para produção de biogás com pré-tratamento enzimático. |
| CN102781587A (zh) | 2010-03-01 | 2012-11-14 | 诺维信公司 | 粘压测定 |
| US8669393B2 (en) | 2010-03-05 | 2014-03-11 | Rennovia, Inc. | Adipic acid compositions |
| US8828701B2 (en) | 2010-03-31 | 2014-09-09 | Novozymes, Inc. | Cellobiohydrolase variants and polynucleotides encoding same |
| US8759064B2 (en) | 2010-05-14 | 2014-06-24 | Codexis, Inc. | Cellobiohydrolase variants |
| US9770705B2 (en) | 2010-06-11 | 2017-09-26 | Rennovia Inc. | Oxidation catalysts |
| US8581042B2 (en) | 2010-06-30 | 2013-11-12 | Novozymes A/S | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
| DK2591119T4 (da) | 2010-07-07 | 2022-12-12 | Novozymes North America Inc | Fermenteringsproces |
| US9458483B2 (en) | 2010-08-12 | 2016-10-04 | Novozymes, Inc. | Compositions comprising a polypeptide having cellulolytic enhancing activity and a bicyclic compound and uses thereof |
| MX2013001540A (es) | 2010-08-12 | 2013-04-24 | Novozymes Inc | Composiciones que comprende un polipeptido que tiene actividad de incremento celulolititico y un compuesto de quinona, y uso de las mismas. |
| WO2012030858A2 (en) | 2010-08-30 | 2012-03-08 | Novozymes A/S | Polypeptides having hemicellulolytic activity and polynucleotides encoding same |
| US8624082B2 (en) | 2010-08-30 | 2014-01-07 | Novozymes A/S | Polypeptides having xylanase activity and polynucleotides encoding same |
| WO2012030845A2 (en) | 2010-08-30 | 2012-03-08 | Novozymes A/S | Polypeptides having beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity and polynucleotides encoding same |
| US9187742B2 (en) | 2010-08-30 | 2015-11-17 | Novozymes, Inc. | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
| WO2012030844A1 (en) | 2010-08-30 | 2012-03-08 | Novozymes A/S | Polypeptides having endoglucanase activity and polynucleotides encoding same |
| BR112013007699B1 (pt) | 2010-09-30 | 2021-12-21 | Novozymes, Inc. | Variante, polinucleotídeo isolado, célula hospedeira microbiana recombinante, métodos para produzir uma variante, para degradar um material celulósico, para produzir um produto de fermentação, para fermentar um material celulósico, e, composição enzimática, formulação do caldo completo ou composição de cultura de células |
| ES2594528T3 (es) | 2010-09-30 | 2016-12-20 | Novozymes, Inc. | Variantes de polipéptidos con actividad de mejora celulolítica y polinucleótidos que las codifican |
| CN102002486A (zh) * | 2010-10-22 | 2011-04-06 | 北京理工大学 | 一种来源于荧光假单胞菌的磷脂酶b及其生产方法 |
| WO2012058293A1 (en) | 2010-10-26 | 2012-05-03 | Novozymes North America, Inc. | Methods of saccharifying sugarcane trash |
| EP2635689B1 (en) * | 2010-11-02 | 2015-04-15 | Novozymes, Inc. | Methods of pretreating cellulosic material with a gh61 polypeptide |
| US9212354B2 (en) | 2010-11-04 | 2015-12-15 | Novozymes Inc. | Polypeptides having cellobiohydrolase activitiy and polynucleotides encoding same |
| WO2012062220A1 (en) | 2010-11-12 | 2012-05-18 | Novozymes A/S | Polypeptides having endoglucanase activity and polynucleotides encoding same |
| WO2012068509A1 (en) | 2010-11-18 | 2012-05-24 | Novozymes, Inc. | Chimeric polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| CN103403249B (zh) * | 2010-12-30 | 2016-11-23 | 诺维信公司 | 用具有纤维素分解增强活性的多肽处理纺织品的工艺 |
| MX348697B (es) * | 2010-12-30 | 2017-06-26 | Novozymes As | Procesos para tratar textiles con polipeptido que tiene actividad de mejoramiento de enzima celulolitica. |
| US20130330797A1 (en) | 2011-01-04 | 2013-12-12 | Novozymes A/S | Process for Producing Biogas from Pectin and Lignocellulose Containing Material |
| DK2668266T3 (en) | 2011-01-26 | 2018-03-26 | Novozymes Inc | POLYPEPTIDES WITH CELLOBIO HYDROASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
| BR112013018695B1 (pt) | 2011-01-26 | 2021-03-30 | Novozymes A / S | Célula hospedeira microbiana recombinante, processos para produzir um polipeptídeo, para produzir uma proteína, para degradar um material celulósico, e, construto de ácido nucleico ou vetor de expressão |
| WO2012103322A1 (en) | 2011-01-26 | 2012-08-02 | Novozymes A/S | Polypeptides having endoglucanase activity and polynucleotides encoding same |
| EP3235903B1 (en) | 2011-01-26 | 2021-07-07 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
| WO2012103350A1 (en) | 2011-01-26 | 2012-08-02 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
| US9096859B2 (en) * | 2011-01-26 | 2015-08-04 | The Regents Of The University Of California | Microbial conversion of plant biomass to advanced biofuels |
| EP2678352B1 (en) | 2011-02-23 | 2017-12-06 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US9051376B2 (en) | 2011-02-23 | 2015-06-09 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| DK3339442T3 (da) | 2011-03-09 | 2022-06-20 | Novozymes Inc | Fremgangsmåder til forøgelse af den cellulolyseforbedrende aktivitet af et polypeptid |
| US9409958B2 (en) | 2011-03-10 | 2016-08-09 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| EP2686434B1 (en) * | 2011-03-17 | 2021-07-14 | Danisco US Inc. | Method for reducing viscosity in saccharification process |
| WO2012130120A1 (en) | 2011-03-25 | 2012-10-04 | Novozymes A/S | Method for degrading or converting cellulosic material |
| CN108467877A (zh) * | 2011-03-25 | 2018-08-31 | 诺维信公司 | 用于降解或转化纤维素材料的方法 |
| US20140080182A1 (en) | 2011-03-31 | 2014-03-20 | Novozymes, Inc. | Cellulose Binding Domain Variants and Polynucleotides Encoding Same |
| US9410136B2 (en) | 2011-03-31 | 2016-08-09 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
| CN102199568B (zh) * | 2011-04-15 | 2012-03-21 | 石家庄金太阳生物有机肥有限公司 | 用于污泥堆肥的发酵剂的制备方法 |
| US9340810B2 (en) | 2011-04-25 | 2016-05-17 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| DK2702153T3 (en) | 2011-04-28 | 2019-03-18 | Novozymes Inc | Polypeptides with endoglucanase activity and polynucleotides encoding them |
| CN103797126A (zh) * | 2011-04-29 | 2014-05-14 | 诺维信股份有限公司 | 用于增强纤维素材料的降解或转化的方法 |
| EP2710132A1 (en) | 2011-05-19 | 2014-03-26 | Novozymes, Inc. | Methods for enhancing the degradation of cellulosic material with chitin binding proteins |
| US8993286B2 (en) | 2011-05-19 | 2015-03-31 | Novozymes, Inc. | Methods for enhancing the degradation of cellulosic material with chitin binding proteins |
| US20140106427A1 (en) | 2011-06-28 | 2014-04-17 | Novozymes A/S | Biogas From Enzyme-Treated Bagasse |
| US20140147895A1 (en) | 2011-07-22 | 2014-05-29 | Novozymes A/S | Processes for Pretreating Cellulosic Material and Improving Hydrolysis Thereof |
| EP2739728B1 (en) | 2011-08-04 | 2017-07-12 | Novozymes A/S | Polypeptides having endoglucanase activity and polynucleotides encoding same |
| WO2013019827A2 (en) | 2011-08-04 | 2013-02-07 | Novozymes A/S | Polypeptides having xylanase activity and polynucleotides encoding same |
| BR112014003740A2 (pt) | 2011-08-23 | 2018-08-14 | Codexis Inc | variantes da celobiohidrolase |
| US9404101B2 (en) | 2011-08-24 | 2016-08-02 | Novozymes, Inc. | Methods for obtaining positive transformants of a filamentous fungal host cell |
| IN2014CN02136A (enExample) | 2011-08-24 | 2015-05-29 | Novozymes Inc | |
| WO2013043910A1 (en) | 2011-09-20 | 2013-03-28 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US10017753B2 (en) | 2011-09-29 | 2018-07-10 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| DK2760885T3 (en) | 2011-09-30 | 2017-10-30 | Novozymes Inc | CHEMICAL POLYPEPTIDES WITH BETA-GLUCOSIDASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
| DK2773656T3 (da) | 2011-10-31 | 2019-09-09 | Novozymes Inc | Polypeptider med cellulolyseforbedrende aktivitet og polynukleotider, som koder for dem |
| US9562222B2 (en) | 2011-11-18 | 2017-02-07 | Novozymes A/S | Polypeptides having beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity and polynucleotides encoding same |
| EP3219794B1 (en) | 2011-11-21 | 2019-09-11 | Novozymes A/S | Gh61 polypeptide variants and polynucleotides encoding same |
| WO2013075644A1 (en) | 2011-11-22 | 2013-05-30 | Novozymes, Inc. | Polypeptides having beta-xylosidase activity and polynucleotides encoding same |
| KR101324677B1 (ko) * | 2011-11-25 | 2013-11-19 | 인그리디언코리아 유한회사 | 고순도 겐티오올리고당의 제조방법, 그로부터 얻어지는 고순도 겐티오올리고당 및 그의 용도 |
| US9624481B2 (en) | 2011-12-01 | 2017-04-18 | Novozymes, Inc. | Polypeptides having beta-xylosidase activity and polynucleotides encoding same |
| WO2013083801A2 (en) | 2011-12-09 | 2013-06-13 | Novozymes A/S | Biogas from substrates comprising animal manure and enzymes |
| EP3272862A1 (en) | 2011-12-16 | 2018-01-24 | Novozymes, Inc. | Polypeptides having laccase activity and polynucleotides encoding same |
| WO2013096369A1 (en) | 2011-12-19 | 2013-06-27 | Novozymes A/S | Processes and compositions for increasing the digestibility of cellulosic materials |
| EP2794870A4 (en) | 2011-12-19 | 2015-06-17 | Novozymes Inc | POLYPEPTIDES WITH XYLANASE ACTIVITY AND POLYNUCLEOTIDES THAT CODE |
| DK2794869T3 (en) | 2011-12-20 | 2018-01-02 | Novozymes Inc | CELLOBIO HYDROLASE VARIABLES AND POLYNUCLEOTIDES CODING THEM |
| EP2794899A1 (en) | 2011-12-21 | 2014-10-29 | Novozymes, Inc. | Methods for determining the degradation of a biomass material |
| CN102559763B (zh) * | 2012-01-12 | 2014-03-19 | 湖南大学 | 一种利用活性介体组合促进复合酶催化降解稻草秸秆的方法 |
| CN103224884B (zh) * | 2012-01-29 | 2015-04-29 | 中国科学院大连化学物理研究所 | 一种产油微生物的培养方法 |
| US20150010959A1 (en) * | 2012-02-16 | 2015-01-08 | Jgc Corporation | Method for producing saccharides containing glucose as main component |
| BR112014026268A2 (pt) | 2012-04-23 | 2017-07-18 | Novozymes As | polipeptídeo isolado, composição, polinucleotídeo isolado, construção de ácido nucleico ou vetor de expressão, célula hospedeira recombinante, e, métodos de produção de um polipeptídeo e de degradação ou conversão de um material celulósico |
| BR112014024804A2 (pt) | 2012-04-23 | 2017-07-11 | Novozymes As | polipeptídeo isolado tendo atividade de glucuronil esterase, composição, polinucleotídeo isolado, construção de ácido nucleico ou vetor de expressão, célula hospedeira recombinante, métodos para a produção de um polipeptídeo, para a degradação ou conversão de um material celulósico e para a produção de um produto de fermentação |
| CN102643868B (zh) * | 2012-04-27 | 2013-11-20 | 浙江大学 | 一种生产丁醇的方法 |
| CN113234695A (zh) | 2012-04-27 | 2021-08-10 | 诺维信股份有限公司 | Gh61多肽变体以及编码其的多核苷酸 |
| CA2872907A1 (en) * | 2012-05-09 | 2013-11-14 | The University Of Akron | Enzyme-based protein separation and enrichment from soy meal, wheat meal, and other protein-rich materials derived from plant seeds, fruits and other biomass |
| FI124477B (en) | 2012-06-07 | 2014-09-15 | Roal Oy | New proteins for the treatment of cellulose materials |
| US9458440B2 (en) | 2012-06-07 | 2016-10-04 | Roal Oy | Proteins for the treatment of cellulosic material |
| UA116630C2 (uk) | 2012-07-03 | 2018-04-25 | Ксілеко, Інк. | Спосіб перетворення цукру на фурфуриловий спирт |
| WO2014092832A2 (en) | 2012-09-19 | 2014-06-19 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
| US9708592B2 (en) | 2012-09-28 | 2017-07-18 | Novosymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| WO2014058896A1 (en) | 2012-10-08 | 2014-04-17 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| AU2013329146B2 (en) | 2012-10-10 | 2017-03-09 | Xyleco, Inc. | Processing materials |
| EA031822B1 (ru) | 2012-10-10 | 2019-02-28 | Ксилеко, Инк. | Способ обработки материала биомассы |
| US20150275194A1 (en) | 2012-10-24 | 2015-10-01 | Novozymes A/S | Polypeptides Having Cellulolytic Enhancing Activity And Polynucleotides Encoding Same |
| DK2917359T3 (da) | 2012-11-09 | 2019-09-23 | Dsm Ip Assets Bv | Fremgangsmåde til enzymatisk hydrolyse af lignocellulosematerialer ved anvendelse af oxygen |
| RS65279B1 (sr) | 2012-11-09 | 2024-03-29 | Versalis Spa | Postupak enzimske hidrolize lignoceluloznog materijala i fermentacije šećera |
| US20160002690A1 (en) * | 2012-11-27 | 2016-01-07 | Novozymes A/S | Milling Process |
| CN104812907A (zh) * | 2012-11-27 | 2015-07-29 | 诺维信公司 | 研磨方法 |
| WO2014093835A1 (en) | 2012-12-14 | 2014-06-19 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US20150337280A1 (en) | 2012-12-19 | 2015-11-26 | Novozymes A/S | Polypeptides Having Cellulolytic Enhancing Activity And Polynucleotides Encoding Same |
| CN105164254B (zh) | 2013-03-08 | 2019-06-28 | 诺维信公司 | 纤维二糖水解酶变体和编码它们的多核苷酸 |
| NZ706072A (en) | 2013-03-08 | 2018-12-21 | Xyleco Inc | Equipment protecting enclosures |
| WO2014140165A1 (en) | 2013-03-14 | 2014-09-18 | Dsm Ip Assets B.V. | Cell wall deconstruction enzymes of paecilomyces byssochlamydoides and uses thereof |
| WO2014140167A1 (en) | 2013-03-14 | 2014-09-18 | Dsm Ip Assets B.V. | Cell wall deconstruction enzymes of malbranchea cinnamomea and uses thereof |
| US9556465B2 (en) | 2013-05-10 | 2017-01-31 | Novozymes A/S | Polypeptides having xylanase activity and polynucleotides encoding same |
| EP3027742B1 (en) | 2013-07-29 | 2019-11-20 | Danisco US Inc. | Variant enzymes |
| JP2015037389A (ja) * | 2013-08-19 | 2015-02-26 | 独立行政法人産業技術総合研究所 | 脂質分解酵素及び非イオン性界面活性剤添加によるリグノセルロース系バイオマスからの酵素糖化反応および同時糖化発酵の改善方法 |
| DK3052620T3 (da) | 2013-09-04 | 2020-09-07 | Novozymes As | Fremgangsmåder til forøgelse af enzymatisk hydrolyse af celluloseholdigt materiale |
| EP3074513A1 (en) | 2013-11-26 | 2016-10-05 | Novozymes A/S | Enzyme compositions and uses thereof |
| DK3092312T3 (en) | 2014-01-07 | 2019-03-04 | Novozymes As | INSURANCE OF MAN-MADE CELLULOSE-CONTAINING MATERIALS |
| KR20230155591A (ko) | 2014-04-30 | 2023-11-10 | 베르살리스 에스.피.에이. | 리그노셀룰로스 물질을 효소적으로 가수분해하고 당을 발효시키는 방법 |
| DK3152315T3 (en) | 2014-06-06 | 2018-11-26 | Novozymes As | ENZYME COMPOSITIONS AND APPLICATIONS THEREOF |
| DK3183352T3 (da) | 2014-08-22 | 2021-06-14 | Cysbio Aps | Fremgangsmåde til fremstilling af et fermenteringsprodukt ud fra et lignocelluloseholdigt materiale |
| CA2958034A1 (en) | 2014-08-28 | 2016-03-03 | Renescience A/S | Solubilization of msw with blend enzymes |
| WO2016037096A1 (en) | 2014-09-05 | 2016-03-10 | Novozymes A/S | Carbohydrate binding module variants and polynucleotides encoding same |
| CA2961280C (en) | 2014-09-23 | 2022-08-30 | Liuyang DIAO | Processes for producing ethanol and fermenting organisms |
| CN104531807B (zh) * | 2014-12-23 | 2017-08-22 | 中国科学院广州能源研究所 | 一种高效糖化草本能源植物的方法 |
| DK3250698T3 (da) | 2015-01-28 | 2020-02-24 | Dsm Ip Assets Bv | Fremgangsmåde til enzymatisk hydrolyse af lignocellulosemateriale og fermentering af sukker |
| WO2016120298A1 (en) | 2015-01-28 | 2016-08-04 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
| PL3640336T3 (pl) | 2015-01-28 | 2022-08-01 | Dsm Ip Assets B.V. | Sposób enzymatycznej hydrolizy materiału lignocelulozowego i fermentacji cukrów |
| DK3262165T3 (da) | 2015-02-24 | 2020-08-24 | Novozymes As | Cellobiohydrolasevarianter og polynukleotider, som koder for dem |
| WO2016145363A1 (en) | 2015-03-12 | 2016-09-15 | Novozymes A/S | Multi-stage enzymatic hydrolysis of lignocellulosic biomass employing an oxidoreductase with an aa9 polypeptide |
| EP3268484B1 (en) | 2015-03-12 | 2020-06-17 | Novozymes A/S | Multi-stage enzymatic hydrolysis of lignocellulosic biomass |
| US20180051306A1 (en) | 2015-03-12 | 2018-02-22 | Novozymes A/S | Enzymatic Hydrolysis with Hemicellulolytic Enzymes |
| MY200191A (en) | 2015-04-10 | 2023-12-12 | Comet Biorefining Inc | Method and compositions for the treatment of cellulosic biomass and products produced thereby |
| WO2016169892A1 (en) | 2015-04-20 | 2016-10-27 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
| WO2016169893A1 (en) | 2015-04-20 | 2016-10-27 | Dsm Ip Assets B.V. | Whole fermentation broth |
| US10519520B2 (en) | 2015-05-27 | 2019-12-31 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
| WO2016207144A1 (en) | 2015-06-22 | 2016-12-29 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
| BR112018001041A2 (pt) | 2015-07-24 | 2018-09-11 | Novozymes Inc | polipeptídeo isolado, composição, formulação de caldo inteiro ou composição de cultura de células, célula hospedeira recombinante, métodos para produção de um polipeptídeo e para produção de uma proteína, planta, parte de planta ou célula de planta transgênica, e, processos para degradação de um material celulósico ou hemicelulósico, para produção de um produto de fermentação e para fermentação de um material celulósico ou hemicelulósico. |
| US20180216089A1 (en) | 2015-07-24 | 2018-08-02 | Novozymes, Inc. | Polypeptides Having Beta-Xylosidase Activity And Polynucleotides Encoding Same |
| US20180202011A1 (en) | 2015-09-04 | 2018-07-19 | Novozymes A/S | Methods of inhibiting aa9 lytic polysaccharide monooxygenase catalyzed inactivation of enzyme compositions |
| EP3353195B1 (en) | 2015-09-22 | 2021-11-10 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
| WO2017070219A1 (en) | 2015-10-20 | 2017-04-27 | Novozymes A/S | Lytic polysaccharide monooxygenase (lpmo) variants and polynucleotides encoding same |
| CN108136452A (zh) | 2015-11-02 | 2018-06-08 | 雷内科学有限公司 | 用混合酶溶解城市固体废物 |
| EP3416740B1 (en) | 2016-02-19 | 2021-01-06 | Intercontinental Great Brands LLC | Processes to create multiple value streams from biomass sources |
| WO2017144670A1 (en) | 2016-02-24 | 2017-08-31 | Danmarks Tekniske Universitet | Improved process for producing a fermentation product from a lignocellulose-containing material |
| US10738293B2 (en) | 2016-03-02 | 2020-08-11 | Novozymes A/S | Cellobiohydrolase variants and polynucleotides encoding same |
| EP3433358B1 (en) | 2016-03-24 | 2022-07-06 | Novozymes A/S | Cellobiohydrolase variants and polynucleotides encoding same |
| WO2017205535A1 (en) | 2016-05-27 | 2017-11-30 | Novozymes, Inc. | Polypeptides having endoglucanase activity and polynucleotides encoding same |
| CA3026325A1 (en) | 2016-06-09 | 2017-12-14 | Dsm Ip Assets B.V. | Seed train for large scale enzyme production |
| US10913938B2 (en) | 2016-07-29 | 2021-02-09 | Dsm Ip Assets B.V. | Polypeptides having cellulolytic enhancing activity and uses thereof |
| WO2018026868A1 (en) | 2016-08-01 | 2018-02-08 | Novozymes, Inc. | Polypeptides having endoglucanase activity and polynucleotides encoding same |
| WO2018085370A1 (en) | 2016-11-02 | 2018-05-11 | Novozymes A/S | Processes for reducing production of primeverose during enzymatic saccharification of lignocellulosic material |
| WO2018096017A1 (en) | 2016-11-24 | 2018-05-31 | Dsm Ip Assets B.V. | Enzyme composition |
| MY198644A (en) | 2016-11-24 | 2023-09-13 | Dsm Ip Assets Bv | Enzyme composition |
| WO2018185071A1 (en) | 2017-04-03 | 2018-10-11 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
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| WO2019074828A1 (en) | 2017-10-09 | 2019-04-18 | Danisco Us Inc | CELLOBIOSE DEHYDROGENASE VARIANTS AND METHODS OF USE |
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| CN115992111B (zh) * | 2022-10-31 | 2024-10-11 | 河南省健康元生物医药研究院有限公司 | 一种具有头孢菌素c乙酰水解酶活性的蛋白及其应用 |
| WO2025103765A1 (en) | 2023-11-17 | 2025-05-22 | Novozymes A/S | Lytic polysaccharide monooxygenases and their use in detergent |
| CN119464077B (zh) * | 2024-11-11 | 2025-07-15 | 山东农业大学 | 一种高效降解秸秆纤维的圆弧青霉及其应用 |
Family Cites Families (4)
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| RU2001949C1 (ru) * | 1991-12-19 | 1993-10-30 | Синицын Аркадий Пантелеймонович | Штамм гриба TRICHODERMA REESEI - продуцент целлюлолитических ферментов |
| PL196594B1 (pl) * | 2000-06-12 | 2008-01-31 | Inst Biopolimerow Wlokien Chem | Sposób wytwarzania włókien, folii i innych produktów z modyfikowanej, rozpuszczalnej celulozy |
| US7045331B2 (en) * | 2001-12-18 | 2006-05-16 | Genencor International, Inc. | EGVII endoglucanase and nucleic acids encoding the same |
| BRPI0507431B1 (pt) * | 2004-02-06 | 2021-07-27 | Novozymes, Inc | Célula hospedeira microbiana recombinante, construto de ácido nucleico, vetor de expressão recombinante, composição detergente, e, métodos para produzir o polipeptídeo gh61, para degradar um material celulósico e para produzir um produto de fermentação |
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- 2006-09-29 BR BRPI0616721-7A patent/BRPI0616721A2/pt not_active Application Discontinuation
- 2006-09-29 CA CA002623908A patent/CA2623908A1/en not_active Abandoned
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| US7608689B2 (en) | 2009-10-27 |
| AU2006337184A1 (en) | 2007-08-09 |
| US8148495B2 (en) | 2012-04-03 |
| AU2006337184B2 (en) | 2012-08-16 |
| JP5129142B2 (ja) | 2013-01-23 |
| US20120190099A1 (en) | 2012-07-26 |
| JP2009509546A (ja) | 2009-03-12 |
| WO2007089290A2 (en) | 2007-08-09 |
| CN104404106A (zh) | 2015-03-11 |
| CA2623908A1 (en) | 2007-08-09 |
| WO2007089290A3 (en) | 2007-11-15 |
| RU2008117116A (ru) | 2009-11-10 |
| RU2441912C2 (ru) | 2012-02-10 |
| KR20080069980A (ko) | 2008-07-29 |
| US20090311755A1 (en) | 2009-12-17 |
| CN101321857A (zh) | 2008-12-10 |
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