CA2892021A1 - Engineered secreted proteins and methods - Google Patents
Engineered secreted proteins and methods Download PDFInfo
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- CA2892021A1 CA2892021A1 CA2892021A CA2892021A CA2892021A1 CA 2892021 A1 CA2892021 A1 CA 2892021A1 CA 2892021 A CA2892021 A CA 2892021A CA 2892021 A CA2892021 A CA 2892021A CA 2892021 A1 CA2892021 A1 CA 2892021A1
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- 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
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
-
- 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
- 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)
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- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2445—Beta-glucosidase (3.2.1.21)
-
- 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
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- 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
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
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- Biotechnology (AREA)
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- Biomedical Technology (AREA)
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- Animal Behavior & Ethology (AREA)
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- Biophysics (AREA)
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- Chemical Kinetics & Catalysis (AREA)
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- Marine Sciences & Fisheries (AREA)
- Diabetes (AREA)
- Obesity (AREA)
- Hematology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
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| US201261728427P | 2012-11-20 | 2012-11-20 | |
| US61/728,427 | 2012-11-20 | ||
| PCT/US2013/071091 WO2014081884A1 (en) | 2012-11-20 | 2013-11-20 | Engineered secreted proteins and methods |
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| CA2892021A1 true CA2892021A1 (en) | 2014-05-30 |
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| EP (1) | EP2922416A4 (enExample) |
| JP (1) | JP2016500250A (enExample) |
| CN (1) | CN104936466A (enExample) |
| CA (1) | CA2892021A1 (enExample) |
| HK (1) | HK1214739A1 (enExample) |
| WO (1) | WO2014081884A1 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP3217807A4 (en) * | 2014-11-11 | 2018-09-12 | Clara Foods Co. | Methods and compositions for egg white protein production |
Families Citing this family (45)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BR112015029580A2 (pt) * | 2013-05-31 | 2017-09-19 | Dsm Ip Assets Bv | Microrganismo recombinante, processo para a preparação de um diterpeno ou diterpeno glicosilado, diterpeno ou diterpeno glicosilado, gêneros alimentícios, alimentos para animais ou bebidas e método para converter um primeiro diterpeno glicosilado em um segundo diterpeno glicosilado |
| CN105916981A (zh) | 2013-07-29 | 2016-08-31 | 丹尼斯科美国公司 | 变体酶 |
| EP3048904A2 (en) * | 2013-09-25 | 2016-08-03 | Pronutria Biosciences, Inc. | Compositions and formulations for treatment of gastrointestinal tract malabsorption diseases and inflammatory conditions and methods of production and use thereof |
| GB201401699D0 (en) * | 2014-01-31 | 2014-03-19 | Dupont Nutrition Biosci Aps | Protein |
| CN103881994B (zh) * | 2014-04-14 | 2020-03-27 | 中国农业科学院生物技术研究所 | 一种具有高转糖苷活性的β-半乳糖苷酶突变体及其制备方法和应用 |
| FR3022558B1 (fr) | 2014-06-20 | 2019-01-25 | Proteus | Variants d'exoglucanases a activite amelioree et leurs utilisations |
| ES2896401T3 (es) * | 2014-09-22 | 2022-02-24 | Tanea Medical Ab | Proteínas recombinantes exentas de Phe para su uso en el tratamiento de la fenilcetonuria |
| CN107135653A (zh) * | 2014-10-01 | 2017-09-05 | 安迅生物制药公司 | 大肠杆菌素变体 |
| DK3234143T5 (da) | 2014-12-19 | 2024-10-14 | Novozymes As | Sammensætninger omfattende polypeptider med xylanaseaktivitet og polypeptider med arabinofuranosidaseaktivitet |
| GB201501565D0 (en) * | 2015-01-30 | 2015-03-18 | Dupont Nutrition Biosci Aps | Method |
| WO2016149482A2 (en) * | 2015-03-17 | 2016-09-22 | Vanderbilt University | Cs21 and lnga protein vaccines |
| DK3313193T3 (da) * | 2015-06-26 | 2021-06-07 | Novozymes As | Fremgangsmåde til fremstilling af en kaffeekstrakt |
| US10188135B2 (en) * | 2015-11-04 | 2019-01-29 | Stokley-Van Camp, Inc. | Method for inducing satiety |
| WO2017142080A1 (ja) | 2016-02-18 | 2017-08-24 | 天野エンザイム株式会社 | 腸内菌叢改善剤 |
| WO2017202997A1 (en) * | 2016-05-24 | 2017-11-30 | Novozymes A/S | Compositions comprising polypeptides having galactanase activity and polypeptides having beta-galactosidase activity |
| EP3462904B1 (en) * | 2016-05-24 | 2024-12-18 | Novozymes A/S | Gastric stable polypeptides having alpha-galactosidase activity and polynucleotides encoding same |
| WO2017202966A1 (en) | 2016-05-24 | 2017-11-30 | Novozymes A/S | Polypeptides having alpha-galactosidase activity and polynucleotides encoding same |
| US11273455B2 (en) | 2016-06-27 | 2022-03-15 | Novozymes A/S | Method of dewatering post fermentation fluids |
| DK3481948T5 (da) * | 2016-07-08 | 2024-09-02 | Novozymes As | Xylanasevarianter og polynukleotider, der koder for dem |
| JP6845244B2 (ja) * | 2016-07-19 | 2021-03-17 | サントリーホールディングス株式会社 | モグロールまたはモグロール配糖体の生産方法 |
| PT3290436T (pt) | 2016-09-01 | 2019-08-30 | Metax Inst Fuer Diaetetik Gmbh | Proteína livre de fenilalanina para o tratamento de pku |
| EA201891926A1 (ru) * | 2017-02-03 | 2019-04-30 | Киверди, Инк. | Микроорганизмы и искусственные экосистемы для производства белка, продуктов питания и полезных побочных продуктов из субстратов c1 |
| EP3592429A1 (en) * | 2017-03-06 | 2020-01-15 | DuPont Nutrition Biosciences ApS | Novel fungal fucosidases and their use in preventing and/or treating a pathogenic infection in an animal |
| EP3840582A4 (en) * | 2018-08-21 | 2022-08-03 | Clara Foods Co. | MODIFICATION OF PROTEIN GLYCOSYLATION IN MICROORGANISMS |
| EP3877519B1 (en) | 2018-11-09 | 2026-03-11 | Ginkgo Bioworks, Inc. | Biosynthesis of mogrosides |
| MX2021011361A (es) * | 2019-03-19 | 2021-10-13 | Bayer Cropscience Lp | Proteinas de fusion, bacterias recombinantes y fragmentos de exosporios para la salud de las plantas. |
| SI3997118T1 (sl) | 2019-07-11 | 2025-06-30 | Clara Foods Co. | Sestavek napitka, ki obsega rekombinantni ovomukoidni protein |
| US12096784B2 (en) | 2019-07-11 | 2024-09-24 | Clara Foods Co. | Protein compositions and consumable products thereof |
| US10927360B1 (en) | 2019-08-07 | 2021-02-23 | Clara Foods Co. | Compositions comprising digestive enzymes |
| PY2055454A (es) | 2019-09-16 | 2022-03-31 | Novozymes As | Polipéptidos que poseen actividad de beta-glucanasa y polinucleótidos que los codifican |
| EP3892290A1 (en) * | 2020-04-08 | 2021-10-13 | NUMAFERM GmbH | Variants of hlya and uses thereof |
| US12612436B2 (en) | 2020-03-18 | 2026-04-28 | Numaferm Gmbh | Variants of hlya and uses thereof |
| WO2021207679A1 (en) * | 2020-04-10 | 2021-10-14 | Liberty Biosecurity, Llc | Polypeptide compositions and uses thereof |
| CA3198703A1 (en) * | 2020-11-13 | 2022-05-19 | Timothy GEISTLINGER | Methods and compositions for producing recombinant components for use in food and other products |
| US20240117331A1 (en) * | 2021-02-10 | 2024-04-11 | Novozymes A/S | Polypeptides having pectinase activity, polynucleotides encoding same, and uses thereof |
| MX2023011028A (es) * | 2021-03-25 | 2023-09-27 | Bio Cat Inc | Mezclas de proteasas micoticas y usos de las mismas. |
| CN114015678A (zh) * | 2021-09-30 | 2022-02-08 | 中南民族大学 | 一种球形赖氨酸芽孢杆菌C3-41来源的氨肽酶Amp0279及其重组菌株和应用 |
| MX2021014268A (es) * | 2021-11-19 | 2022-02-16 | Univ Mexico Nac Autonoma | Proteina optimizada que comprende los aminoacidos esenciales para la nutricion humana. |
| US20230281444A1 (en) * | 2022-03-04 | 2023-09-07 | Cella Farms Inc | Computational system and algorithm for selecting nutritional microorganisms based on in silico protein quality determination |
| KR20250005200A (ko) | 2022-04-20 | 2025-01-09 | 노보자임스 에이/에스 | 유리 지방산을 제조하는 방법 |
| WO2023215798A1 (en) * | 2022-05-04 | 2023-11-09 | Locus Biosciences, Inc. | Phage compositions for escherichia comprising crispr-cas systems and methods of use thereof |
| US20250311734A1 (en) | 2022-05-14 | 2025-10-09 | Novozymes A/S | Compositions and Methods for Preventing, Treating, Suppressing and/or Eliminatting Phytopathogenic Infestations and Infections |
| CN115160420B (zh) * | 2022-06-24 | 2023-06-02 | 西南大学 | 盔形毕赤酵母scp类分泌蛋白及其应用 |
| WO2024220717A1 (en) * | 2023-04-20 | 2024-10-24 | Ginkgo Bioworks, Inc. | Biosynthesis of mogrosides |
| WO2025155915A1 (en) * | 2024-01-17 | 2025-07-24 | Anagram Therapeutics, Inc. | Methods and compositions for treating congenital sucrase-isomaltase deficiency |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6800726B1 (en) * | 1996-11-01 | 2004-10-05 | Pioneer Hi-Bred International, Inc. | Proteins with increased levels of essential amino acids |
| AR017831A1 (es) * | 1997-12-10 | 2001-10-24 | Pioneer Hi Bred Int | Metodo para alterar la composicion de aminoacidos de una proteina nativa de interes, proteina elaborada, y polinucleotido |
| US20060159724A1 (en) * | 2000-08-08 | 2006-07-20 | Bell Stacey J | Nutritional supplement for the management of weight |
| BR0212530A (pt) * | 2001-09-17 | 2005-04-12 | Monsanto Technology Llc | Proteìnas reforçadas e métodos para seu uso |
| US7273738B2 (en) * | 2002-10-01 | 2007-09-25 | Novozymes A/S | Family GH-61 polypeptides |
| CN1557475A (zh) * | 2004-02-04 | 2004-12-29 | 高春平 | 美容、减肥营养组合物 |
| EP2327316B1 (en) * | 2009-11-29 | 2016-11-16 | Premier Nutrition Corporation | Method of enhancing muscle protein synthesis |
| CA2786001A1 (en) * | 2009-12-31 | 2011-07-07 | Pioneer Hi-Bred International, Inc. | Engineering plant resistance to diseases caused by pathogens |
| WO2012128260A1 (ja) * | 2011-03-24 | 2012-09-27 | 旭硝子株式会社 | シゾサッカロミセス属酵母の形質転換体、該形質転換体の製造方法、β－グルコシダーゼの製造方法、およびセルロースの分解方法 |
| WO2013148329A1 (en) * | 2012-03-26 | 2013-10-03 | Pronutria, Inc. | Charged nutritive proteins and methods |
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- 2013-11-20 CA CA2892021A patent/CA2892021A1/en not_active Abandoned
- 2013-11-20 EP EP13856957.9A patent/EP2922416A4/en not_active Withdrawn
- 2013-11-20 JP JP2015543148A patent/JP2016500250A/ja not_active Withdrawn
- 2013-11-20 WO PCT/US2013/071091 patent/WO2014081884A1/en not_active Ceased
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- 2013-11-20 HK HK16102843.7A patent/HK1214739A1/zh unknown
- 2013-11-20 US US14/443,773 patent/US20150307562A1/en not_active Abandoned
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP3217807A4 (en) * | 2014-11-11 | 2018-09-12 | Clara Foods Co. | Methods and compositions for egg white protein production |
| US20240083977A1 (en) * | 2014-11-11 | 2024-03-14 | Clara Foods Co. | Methods and compositions for egg white protein production |
Also Published As
| Publication number | Publication date |
|---|---|
| HK1214739A1 (zh) | 2016-09-30 |
| JP2016500250A (ja) | 2016-01-12 |
| WO2014081884A9 (en) | 2015-05-21 |
| US20150307562A1 (en) | 2015-10-29 |
| WO2014081884A1 (en) | 2014-05-30 |
| EP2922416A4 (en) | 2016-07-20 |
| EP2922416A1 (en) | 2015-09-30 |
| CN104936466A (zh) | 2015-09-23 |
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Legal Events
| Date | Code | Title | Description |
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| EEER | Examination request |
Effective date: 20160809 |
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| FZDE | Discontinued |
Effective date: 20181023 |