KR20130119945A - 3-히드록시프로피온산 생산을 위한 조성물 및 방법 - Google Patents
3-히드록시프로피온산 생산을 위한 조성물 및 방법 Download PDFInfo
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- KR20130119945A KR20130119945A KR1020137015983A KR20137015983A KR20130119945A KR 20130119945 A KR20130119945 A KR 20130119945A KR 1020137015983 A KR1020137015983 A KR 1020137015983A KR 20137015983 A KR20137015983 A KR 20137015983A KR 20130119945 A KR20130119945 A KR 20130119945A
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- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
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- C12Y206/01001—Aspartate transaminase (2.6.1.1), i.e. aspartate-aminotransferase
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| US61/535,181 | 2011-09-15 | ||
| PCT/US2011/061717 WO2012074818A2 (en) | 2010-11-22 | 2011-11-21 | Compositions and methods for 3-hydroxypropionic acid production |
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20190096229A (ko) * | 2018-02-08 | 2019-08-19 | 주식회사 엘지화학 | 고농도 3-하이드록시프로피온산 수용액의 제조 방법 |
| KR20220061044A (ko) * | 2020-11-05 | 2022-05-12 | 주식회사 엘지화학 | 3-하이드록시프로피온산의 생산 방법 |
| WO2025165198A1 (ko) * | 2024-01-31 | 2025-08-07 | 주식회사 엘지화학 | 3-하이드록시프로피온산의 생산 방법 |
Families Citing this family (89)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2001992B1 (en) | 2006-03-13 | 2016-07-20 | Cargill Inc. | Yeast cells having disrupted pathway from dihydroxyacetone phosphate to glycerol |
| CA2807561C (en) | 2010-08-06 | 2022-04-12 | Mascoma Corporation | Production of malonyl-coa derived products via anaerobic pathways |
| CA2885934C (en) * | 2010-11-22 | 2018-05-01 | Cargill, Incorporated | Compositions and methods for increased ethanol titer from biomass |
| MX2013005654A (es) | 2010-11-22 | 2013-07-17 | Novozymes Inc | Composiciones y metodos para la produccion de acido 3-hidroxipropionico. |
| CA2840525A1 (en) * | 2011-06-28 | 2013-01-03 | Brookhaven Science Associates, Llc | Modified plants with increased oil content |
| IN2014CN02136A (enExample) * | 2011-08-24 | 2015-05-29 | Novozymes Inc | |
| EP2751261B1 (en) | 2011-09-30 | 2018-08-29 | Novozymes, Inc. | Dehydrogenase variants and polynucleotides encoding same |
| CN118086086A (zh) * | 2012-03-06 | 2024-05-28 | 利戈斯股份有限公司 | 用于产生丙二酸的重组宿主细胞 |
| KR102098849B1 (ko) * | 2012-05-30 | 2020-04-09 | 란자테크 뉴질랜드 리미티드 | 재조합 미생물 및 이의 용도 |
| BR112015002940A2 (pt) | 2012-08-10 | 2018-04-24 | Opx Biotechnologies Inc | microorganismos e métodos para a produção de ácidos graxos e produtos derivados de ácidos graxos. |
| JP2015531237A (ja) * | 2012-10-11 | 2015-11-02 | テクニカル・ユニヴァーシティ・オブ・デンマーク | 遺伝子組換え酵母 |
| JP2015536669A (ja) * | 2012-11-30 | 2015-12-24 | ノボザイムス,インコーポレイティド | 組換え酵母による3−ヒドロキシプロピオン酸の生産 |
| WO2014160050A1 (en) * | 2013-03-14 | 2014-10-02 | Butamax Advanced Biofuels Llc | Glycerol 3- phosphate dehydrogenase for butanol production |
| JP2016518821A (ja) | 2013-03-15 | 2016-06-30 | カーギル・インコーポレイテッド | 3−ヒドロキシプロピオン酸の回収 |
| US9447438B2 (en) | 2013-03-15 | 2016-09-20 | Cargill, Incorporated | Acetyl-coA carboxylases |
| US20150044746A1 (en) * | 2013-03-15 | 2015-02-12 | Opx Biotechnologies, Inc. | Method of enhanced bioproduction |
| EP3008178A1 (en) | 2013-06-14 | 2016-04-20 | Technical University of Denmark | Microbial production of 3-hydroxypropionic acid |
| EP3008179A1 (en) | 2013-06-14 | 2016-04-20 | Technical University of Denmark | 3hp tolerance |
| WO2015010103A2 (en) | 2013-07-19 | 2015-01-22 | Opx Biotechnologies, Inc. | Microorganisms and methods for the production of fatty acids and fatty acid derived products |
| US11408013B2 (en) | 2013-07-19 | 2022-08-09 | Cargill, Incorporated | Microorganisms and methods for the production of fatty acids and fatty acid derived products |
| US9556443B2 (en) | 2013-07-19 | 2017-01-31 | Samsung Electronics Co., Ltd. | Yeast cell with inactivated NADH dehydrogenase and method of producing lactate using the yeast cell |
| US9845484B2 (en) | 2013-07-31 | 2017-12-19 | Novozymes A/S | 3-hydroxypropionic acid production by recombinant yeasts expressing an insect aspartate 1-decarboxylase |
| WO2015031504A1 (en) * | 2013-08-27 | 2015-03-05 | The Regents Of The University Of California | RECOMBINANT PATHWAY AND ORGANISMS FOR MALONYL-CoA SYNTHESIS |
| WO2015036278A1 (de) | 2013-09-12 | 2015-03-19 | Basf Se | Verfahren zur dehydratisierung von 3-hydroxypropionsäure zu acrylsäure |
| WO2015036273A1 (de) | 2013-09-12 | 2015-03-19 | Basf Se | Verfahren zur herstellung von acrylsäure |
| US10252970B2 (en) | 2013-09-12 | 2019-04-09 | Basf Se | Method of dehydrating 3-hydroxypropionic acid to form acrylic acid |
| JP6499587B2 (ja) | 2013-11-22 | 2019-04-10 | Jmtcエンザイム株式会社 | 形質転換体およびその製造方法、ならびに乳酸の製造方法 |
| JP6488666B2 (ja) * | 2013-11-22 | 2019-03-27 | Agc株式会社 | クローニングベクター、発現ベクターおよび形質転換体の製造方法 |
| KR101555867B1 (ko) | 2014-04-18 | 2015-10-01 | 부산대학교 산학협력단 | 3-하이드록시프로피온산을 분해하지 않는 슈도모나스 데니트리피칸스 결실 변이균주 및 이를 이용한 3-하이드록시프로피온산의 생산방법 |
| WO2015200545A1 (en) * | 2014-06-26 | 2015-12-30 | Lygos, Inc. | Recombinant host cells for the production of malonate |
| WO2016026763A1 (en) | 2014-08-18 | 2016-02-25 | Basf Se | Process for preparing acrylic acid using a heterogeneous alumina catalyst |
| JP6786477B2 (ja) | 2014-08-29 | 2020-11-18 | エスケー イノベーション カンパニー リミテッドSk Innovation Co.,Ltd. | 3−hpを生産することができる組換え酵母およびこれを利用した3−hpの製造方法 |
| EP2993228B1 (en) | 2014-09-02 | 2019-10-09 | Cargill, Incorporated | Production of fatty acid esters |
| US10214754B2 (en) | 2014-10-10 | 2019-02-26 | Jmtc Enzyme Corporation | Transformant and its production process, and method for producing lactic acid |
| US20170362613A1 (en) * | 2014-12-19 | 2017-12-21 | Novozymes A/S | Recombinant Host Cells For The Production Of 3-Hydroxypropionic Acid |
| US20180273915A1 (en) * | 2014-12-19 | 2018-09-27 | Novozymes A/S | Recombinant Host Cells For The Production Of 3-Hydroxypropionic Acid |
| WO2016135020A1 (de) | 2015-02-24 | 2016-09-01 | Basf Se | Verfahren zur kontinuierlichen dehydratisierung von 3-hydroxypropionsäure zu acrylsäure |
| WO2016138303A1 (en) | 2015-02-27 | 2016-09-01 | Novozymes A/S | Mutant host cells for the production of 3-hydroxypropionic acid |
| WO2016162175A1 (de) | 2015-04-07 | 2016-10-13 | Basf Se | Verfahren zur dehydratisierung von 3-hydroxypropionsäure zu acrylsäure |
| WO2016200239A1 (ko) * | 2015-06-11 | 2016-12-15 | 부산대학교 산학협력단 | 3-하이드록시프로피온산에 의해 발현이 유도되는 프로모터 시스템 및 이를 이용한 3-하이드록시프로피온산의 생물학적 생산방법 |
| EP3321364B1 (en) | 2015-06-11 | 2022-12-28 | Noroo IC Co., Ltd. | Promoter system inducing expression by 3-hydroxypropionic acid and method for biological production of 3-hydroxypropionic acid using same |
| EP3325608B1 (en) * | 2015-07-21 | 2021-11-24 | The Governing Council of the University of Toronto | Methods and microorganisms for the production of 1,3-butanediol |
| WO2017035270A1 (en) | 2015-08-24 | 2017-03-02 | Novozymes A/S | Beta-alanine aminotransferases for the production of 3-hydroxypropionic acid |
| WO2017083683A1 (en) * | 2015-11-12 | 2017-05-18 | Lygos, Inc. | Recombinant host cells and methods for the anaerobic production of l-aspartate and beta-alanine |
| US20180258437A1 (en) * | 2015-11-12 | 2018-09-13 | Lygos, Inc. | Recombinant host cells and methods for the production of l-aspartate and beta-alanine |
| DE102016114555A1 (de) | 2016-08-05 | 2018-02-08 | Thyssenkrupp Ag | Prozess zur Herstellung von Acrylsäure aus einer wässrigen 3-Hydroxypropanol-Lösung |
| US20190345522A1 (en) | 2016-12-06 | 2019-11-14 | Novozymes A/S | Improved Processes For Production Of Ethanol From Xylose-Containing Cellulosic Substrates Using Engineered Yeast Strains |
| CN110494566A (zh) | 2017-02-02 | 2019-11-22 | 嘉吉公司 | 产生c6-c10脂肪酸衍生物的经遗传修饰的细胞 |
| US11091753B2 (en) | 2017-05-31 | 2021-08-17 | Novozymes A/S | Xylose fermenting yeast strains and processes thereof for ethanol production |
| CA3064042A1 (en) | 2017-06-02 | 2018-12-06 | Novozymes A/S | Improved yeast for ethanol production |
| CN110997619B (zh) | 2017-08-17 | 2023-06-27 | 巴斯夫欧洲公司 | 连续制备丙烯酸正丁酯或丙烯酸异丁酯的方法 |
| US11834484B2 (en) | 2017-08-29 | 2023-12-05 | Novozymes A/S | Bakers's yeast expressing anti-staling/freshness amylases |
| AU2019213033A1 (en) | 2018-01-29 | 2020-09-17 | Microbiogen Pty. Ltd. | Microorganisms with improved nitrogen utilization for ethanol production |
| BR112020024347A2 (pt) | 2018-05-31 | 2021-02-23 | Novozymes A/S | processos para aumentar o crescimento e a produtividade de levedura |
| CA3143683A1 (en) * | 2018-06-25 | 2020-01-02 | Lygos, Inc. | Recombinant host cells and methods for the production of aspartic acid and s-alanine |
| BR112021001282A2 (pt) | 2018-07-25 | 2021-04-27 | Novozymes A/S | levedura expressando enzimas para produção de etanol |
| CA3114783A1 (en) | 2018-10-08 | 2020-04-16 | Novozymes A/S | Enzyme-expressing yeast for ethanol production |
| JP7370587B2 (ja) * | 2018-10-30 | 2023-10-30 | GreenEarthInstitute株式会社 | 有機化合物の製造方法およびコリネ型細菌 |
| EP3877525A2 (en) | 2018-12-18 | 2021-09-15 | Braskem S.A. | Co-production pathway for 3-hp and acetyl-coa derivatives from malonate semialdehyde |
| CN109852605A (zh) * | 2019-01-16 | 2019-06-07 | 徐州工程学院 | 一种诱变筛选高产3-羟基丙酸菌株的方法 |
| CA3143381A1 (en) | 2019-07-26 | 2021-02-04 | Novozymes A/S | Microorganisms with improved nitrogen transport for ethanol production |
| CN112390855B (zh) * | 2019-07-31 | 2022-04-29 | 上海交通大学医学院附属仁济医院 | Pretide-146a在制备缓解或治疗自身免疫性疾病的药物中的应用 |
| MX2022000831A (es) | 2019-08-05 | 2022-02-10 | Novozymes As | Mezclas de enzimas y procesos para producir un ingrediente alimenticio de alto contenido proteico a partir de un subproducto de la vinaza entera. |
| BR112021026477A2 (pt) | 2019-08-06 | 2022-02-08 | Novozymes As | Célula hospedeira recombinante, métodos de produção de um produto de fermentação a partir de um material contendo amido ou contendo celulose, de produção do polipeptídeo maduro, de produção de um derivado de uma célula hospedeira recombinante e de produção de etanol, construto de ácido nucleico ou vetor de expressão, composição, e, uso de uma célula hospedeira recombinante |
| MX2022002834A (es) | 2019-09-16 | 2022-04-06 | Novozymes As | Polipeptidos con actividad beta-glucanasa y polinucleotidos que los codifican. |
| EP4073089A1 (en) | 2019-12-10 | 2022-10-19 | Novozymes A/S | Microorganism for improved pentose fermentation |
| EP4103709A2 (en) | 2020-02-10 | 2022-12-21 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
| CA3188324A1 (en) | 2020-06-29 | 2022-01-06 | Basf Se | Device for carrying out material exchange processes |
| EP4190907A4 (en) * | 2020-07-31 | 2023-12-06 | LG Chem, Ltd. | PROCESS FOR PREPARING 3-HYDROXYPROPIONIC ACID IN TWO STEP |
| CN111985041B (zh) * | 2020-09-17 | 2021-03-30 | 青岛理工大学 | 一种加固边坡挡墙高度确定方法及加固边坡挡墙 |
| EP4222167A1 (en) | 2020-09-30 | 2023-08-09 | Nobell Foods, Inc. | Recombinant milk proteins and food compositions comprising the same |
| KR20230076829A (ko) * | 2020-09-30 | 2023-05-31 | 게노미엄, 아이엔씨. | 바이오아크롤레인 및 바이오아크릴산을 생산하는 발효 공정 |
| US10894812B1 (en) | 2020-09-30 | 2021-01-19 | Alpine Roads, Inc. | Recombinant milk proteins |
| US10947552B1 (en) | 2020-09-30 | 2021-03-16 | Alpine Roads, Inc. | Recombinant fusion proteins for producing milk proteins in plants |
| EP4237555A1 (en) | 2020-11-02 | 2023-09-06 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| CN116323929A (zh) * | 2020-11-05 | 2023-06-23 | 株式会社Lg化学 | 具有从葡萄糖生产3-羟基丙酸能力的微生物及其用途 |
| AU2022218205A1 (en) | 2021-02-08 | 2023-05-25 | Lanzatech, Inc. | Recombinant microorganisms and uses therefor |
| AU2022288057A1 (en) | 2021-06-07 | 2023-12-21 | Novozymes A/S | Engineered microorganism for improved ethanol fermentation |
| FR3125042B1 (fr) | 2021-07-09 | 2024-04-12 | Snf Sa | Procédé d’obtention d’alkyl(méth)acrylamide substitué biosourcé |
| FR3125048B1 (fr) | 2021-07-09 | 2024-04-19 | Snf Sa | Polymère biosourcé à biodégradabilité améliorée |
| FR3125040B1 (fr) | 2021-07-09 | 2024-04-26 | Snf Sa | Procédé d’obtention de bio-monomère à partir de diméthylaminoethanol d’origine renouvelable |
| WO2023168244A1 (en) | 2022-03-03 | 2023-09-07 | Cargill, Incorporated | Genetically modified yeast and fermentation processes for the production of 3-hydroxypropionate |
| WO2023168233A1 (en) | 2022-03-03 | 2023-09-07 | Cargill, Incorporated | Genetically modified yeast and fermentation processes for the production of 3-hydroxypropionate |
| CN115595328A (zh) * | 2022-03-07 | 2023-01-13 | 中国科学院微生物研究所(Cn) | 天冬氨酸脱羧酶在发酵生产维生素b5中的应用 |
| CN116024184B (zh) * | 2022-07-26 | 2024-03-15 | 南京科技职业学院 | 醛脱氢酶突变体及其在制备5-羟甲基-2-呋喃甲酸中的应用 |
| EP4638768A2 (en) | 2022-12-19 | 2025-10-29 | Novozymes A/S | Processes for producing fermentation products using fiber-degrading enzymes with engineered yeast |
| WO2024226289A1 (en) | 2023-04-26 | 2024-10-31 | Cargill, Incorporated | Methods for producing propionic acid |
| WO2024258820A2 (en) | 2023-06-13 | 2024-12-19 | Novozymes A/S | Processes for producing fermentation products using engineered yeast expressing a beta-xylosidase |
| WO2025058922A1 (en) | 2023-09-15 | 2025-03-20 | Cargill, Incorporated | Rising film evaporator clean-in-place method and system |
Family Cites Families (67)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL39710A (en) | 1972-06-19 | 1975-04-25 | Imi Inst For Res & Dev | Recovery of acids from aqueous solutions by solvent extraction |
| US4771001A (en) | 1986-03-27 | 1988-09-13 | Neurex Corp. | Production of lactic acid by continuous fermentation using an inexpensive raw material and a simplified method of lactic acid purification |
| US5210296A (en) | 1990-11-19 | 1993-05-11 | E. I. Du Pont De Nemours And Company | Recovery of lactate esters and lactic acid from fermentation broth |
| US5132456A (en) | 1991-05-07 | 1992-07-21 | The Regents Of The University Of California | Sorption of carboxylic acid from carboxylic salt solutions at PHS close to or above the pKa of the acid, with regeneration with an aqueous solution of ammonia or low-molecular-weight alkylamine |
| US5420304A (en) | 1992-03-19 | 1995-05-30 | Biopak Technology, Ltd. | Method to produce cyclic esters |
| AT398982B (de) | 1993-02-18 | 1995-02-27 | Vogelbusch Gmbh | Verfahren zur abtrennung und reinigung von milchsäure |
| US5510526A (en) | 1993-06-29 | 1996-04-23 | Cargill, Incorporated | Lactic acid production, separation and/or recovery process |
| IL109003A (en) | 1994-03-16 | 1999-09-22 | Yissum Res Dev Co | Process and extractant composition for extracting water-soluble carboxylic and mineral acids |
| IT1294728B1 (it) | 1997-09-12 | 1999-04-12 | Biopolo S C A R L | Ceppi di lievito per la riproduzione di acido lattico |
| WO1999053035A1 (en) | 1998-04-13 | 1999-10-21 | The University Of Georgia Research Foundation, Inc. | Pyruvate carboxylase overexpression for enhanced production of oxaloacetate-derived biochemicals in microbial cells |
| DE69938105T2 (de) * | 1998-08-04 | 2009-01-29 | Metabolix, Inc., Cambridge | Herstellung von polyhydroxyalkanoaten aus polyolen |
| CA2374482C (en) | 1999-05-21 | 2012-09-18 | Cargill Dow Llc | Methods and materials for the synthesis of organic products |
| WO2001016346A1 (en) | 1999-08-30 | 2001-03-08 | Wisconsin Alumni Research Foundation | Production of 3-hydroxypropionic acid in recombinant organisms |
| US6852517B1 (en) | 1999-08-30 | 2005-02-08 | Wisconsin Alumni Research Foundation | Production of 3-hydroxypropionic acid in recombinant organisms |
| JP4098455B2 (ja) | 2000-03-10 | 2008-06-11 | 株式会社日立製作所 | マーク画像中の電子透かし情報の参照方法及び計算機 |
| JP4490628B2 (ja) | 2000-11-20 | 2010-06-30 | カーギル インコーポレイテッド | 3−ヒドロキシプロピオン酸および他の有機化合物 |
| US7109010B2 (en) | 2000-11-22 | 2006-09-19 | Nature Works Llc | Methods and materials for the synthesis of organic products |
| CA2474152A1 (en) | 2001-11-23 | 2003-06-19 | Cargill Dow Llc | Methods and materials for the production of organic products in cells of candida species |
| DE60327804D1 (de) | 2002-01-18 | 2009-07-09 | Novozymes As | Alanin-2,3-aminomutase |
| JP2005521718A (ja) | 2002-03-25 | 2005-07-21 | カーギル,インコーポレイティド | β−ヒドロキシカルボン酸の誘導体の製造方法 |
| WO2003102200A2 (en) | 2002-05-30 | 2003-12-11 | Cargill Dow Llc | Fermentation process using specific oxygen uptake rates as a process control |
| US7126034B2 (en) | 2002-11-01 | 2006-10-24 | Cargill, Incorporated | Process for preparation of 1,3-propanediol |
| CA2516913A1 (en) | 2003-02-24 | 2004-09-10 | Cargill, Incorporated | Process for preparing 3-hydroxycarboxylic acids |
| BRPI0411925A (pt) | 2003-06-26 | 2006-08-15 | Cargill Inc | processo para separação e recuperação de ácido 3-hidroxipropiÈnico e ácido acrìlico |
| CN100422131C (zh) | 2003-06-26 | 2008-10-01 | 嘉吉有限公司 | 分离和回收3-羟基丙酸和丙烯酸的方法 |
| US7326557B2 (en) | 2003-11-14 | 2008-02-05 | Rice University | Increasing intracellular NADPH availability in E. coli |
| DK1706457T3 (da) | 2003-12-04 | 2012-05-21 | Novozymes As | Fremstilling af 3-hydroxypropionsyre ved anvendelse af beta-alanin/pyruvataminotransferase |
| WO2006022664A2 (en) | 2004-07-30 | 2006-03-02 | Cargill Incorporated | Alanine 2, 3 aminomutases |
| US7987056B2 (en) | 2004-09-20 | 2011-07-26 | The Regents Of The University Of Colorado, A Body Corporate | Mixed-library parallel gene mapping quantitative micro-array technique for genome-wide identification of trait conferring genes |
| MX2007004980A (es) | 2004-10-25 | 2007-06-14 | Codexis Inc | Alanina 2,3-aminomutasas mejoradas, y polinucleotidos relacionados. |
| DK1760156T3 (da) | 2005-08-10 | 2013-03-18 | Univ Florida | Materialer og fremgangsmåder til effektiv mælkesyrefremstilling |
| US7846688B2 (en) | 2005-08-15 | 2010-12-07 | The Regents Of The University Of Colorado | Broad host range vectors for shotgun and expression library cloning in Gram negative bacteria |
| DE102005048818A1 (de) | 2005-10-10 | 2007-04-12 | Degussa Ag | Mikrobiologische Herstellung von 3-Hydroxypropionsäure |
| EP2001992B1 (en) | 2006-03-13 | 2016-07-20 | Cargill Inc. | Yeast cells having disrupted pathway from dihydroxyacetone phosphate to glycerol |
| WO2007130745A1 (en) | 2006-03-15 | 2007-11-15 | Regents Of The University Of Colorado | Enhanced alcohol tolerant microorganism and methods of use thereof |
| US20080103060A1 (en) | 2006-08-08 | 2008-05-01 | Regents Of The University Of Colorado | Compositions and methods for chemical reporter vectors |
| BRPI0716212A2 (pt) * | 2006-08-30 | 2013-10-15 | Cargill Inc | Beta-alanina/alfa-cetoglutarato aminotransferase para produção de ácido 3-hidroxipropiônico |
| US8938765B2 (en) | 2006-12-22 | 2015-01-20 | Time Warner Cable Enterprises Llc | Methods, apparatus and user interface for providing content on demand |
| AU2008206403A1 (en) | 2007-01-12 | 2008-07-24 | The Regents Of The University Of Colorado, A Body Corporate | Compositions and methods for enhancing tolerance for the production of organic chemicals produced by microorganisms |
| US8673601B2 (en) | 2007-01-22 | 2014-03-18 | Genomatica, Inc. | Methods and organisms for growth-coupled production of 3-hydroxypropionic acid |
| US8048624B1 (en) | 2007-12-04 | 2011-11-01 | Opx Biotechnologies, Inc. | Compositions and methods for 3-hydroxypropionate bio-production from biomass |
| 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" |
| WO2009089457A1 (en) | 2008-01-11 | 2009-07-16 | Novozymes A/S | Methods for producing 3-hydroxypropionic acid and compounds thereof |
| EP2313491A4 (en) | 2008-07-08 | 2011-12-07 | Opx Biotechnologies Inc | METHODS, COMPOSITIONS AND SYSTEMS FOR BIOSYNTHETIC BIOPRODUCTION OF 1,4-BUTANEDIOL |
| US20100021978A1 (en) * | 2008-07-23 | 2010-01-28 | Genomatica, Inc. | Methods and organisms for production of 3-hydroxypropionic acid |
| US20110244575A1 (en) * | 2008-07-23 | 2011-10-06 | Lipscomb Tanya E W | Methods, systems and compositions for increased microorganism tolerance to and production of 3-hydroxypropionic acid (3-hp) |
| US20110281314A1 (en) | 2008-08-04 | 2011-11-17 | Lynch Michael D | Methods, systems and compositions related to microbial bio-production of butanol and/or isobutanol |
| EP2326709A4 (en) * | 2008-09-15 | 2013-01-23 | Opx Biotechnologies Inc | METHODS, SYSTEMS AND COMPOSITIONS RELATED TO REDUCED MICROBIAL PRODUCTION OF 3-HYDROXYPROPIONIC ACID (3-HP) IN ALDEHYDMETABOLITE |
| US8518684B2 (en) | 2008-11-18 | 2013-08-27 | Novozymes, Inc. | Methods and compositions for degrading cellulosic material |
| US20110144377A1 (en) | 2009-06-16 | 2011-06-16 | E. I. Du Pont Nemours And Company | Process for the biological production of 3-hydroxypropionic acid with high yield |
| WO2011038364A1 (en) | 2009-09-27 | 2011-03-31 | Opx Biotechnologies, Inc. | Method for producing 3-hydroxypropionic acid and other products |
| US8809027B1 (en) | 2009-09-27 | 2014-08-19 | Opx Biotechnologies, Inc. | Genetically modified organisms for increased microbial production of 3-hydroxypropionic acid involving an oxaloacetate alpha-decarboxylase |
| EP2491122A1 (en) | 2009-10-23 | 2012-08-29 | Novozymes Inc. | Cellobiohydrolase variants and polynucleotides encoding same |
| BR112012006847A2 (pt) | 2009-10-29 | 2015-09-08 | Novozymes As | polipeptídeo polinucleotídeo, célula hospedeira recombinante, métodos para produzir o polipeptídeo para produzir um mutante de uma célula parental, 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 produzir um produto de fermentação e pra fermentar um material celulósico, planta transgênica, parte da planta ou célula da planta, molécula de rna inibitória de filamento duplo, e, composição. |
| WO2011063363A2 (en) | 2009-11-20 | 2011-05-26 | Opx Biotechnologies, Inc. | Production of an organic acid and/or related chemicals |
| CA2788045A1 (en) | 2010-01-27 | 2011-08-04 | Opx Biotechnologies, Inc. | Microorganism production of high-valve chemical products, and related compositions, methods and systems |
| US20130052702A1 (en) | 2010-03-30 | 2013-02-28 | Novozymes North America, Inc. | Methods for Enhancing By-Products From Fermentation Processes |
| 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. |
| MX2013005654A (es) * | 2010-11-22 | 2013-07-17 | Novozymes Inc | Composiciones y metodos para la produccion de acido 3-hidroxipropionico. |
| US20140121118A1 (en) | 2010-11-23 | 2014-05-01 | Opx Biotechnologies, Inc. | Methods, systems and compositions regarding multiplex construction protein amino-acid substitutions and identification of sequence-activity relationships, to provide gene replacement such as with tagged mutant genes, such as via efficient homologous recombination |
| EP2864282A4 (en) | 2012-06-20 | 2016-01-20 | Opx Biotechnologies Inc | CLEANING OF 3-HYDROXYPROPIONIC ACID FROM RAW CELLBOUILLON AND DEHYDRATION TO ACRYLIC ACID |
| US20130345470A1 (en) | 2012-06-20 | 2013-12-26 | Opx Biotechnologies, Inc. | Purification of 3-Hydroxypropionic Acid from Crude Cell Broth and Production of Acrylamide |
| JP2016518821A (ja) | 2013-03-15 | 2016-06-30 | カーギル・インコーポレイテッド | 3−ヒドロキシプロピオン酸の回収 |
| US9447438B2 (en) | 2013-03-15 | 2016-09-20 | Cargill, Incorporated | Acetyl-coA carboxylases |
| WO2014145343A1 (en) | 2013-03-15 | 2014-09-18 | Opx Biotechnologies, Inc. | Bioproduction of chemicals |
| US20150044746A1 (en) | 2013-03-15 | 2015-02-12 | Opx Biotechnologies, Inc. | Method of enhanced bioproduction |
| EP2976141A4 (en) | 2013-03-15 | 2016-10-05 | Cargill Inc | FLASHING FOR PRODUCTION CLEANING AND RECOVERY |
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20190096229A (ko) * | 2018-02-08 | 2019-08-19 | 주식회사 엘지화학 | 고농도 3-하이드록시프로피온산 수용액의 제조 방법 |
| KR20220061044A (ko) * | 2020-11-05 | 2022-05-12 | 주식회사 엘지화학 | 3-하이드록시프로피온산의 생산 방법 |
| WO2025165198A1 (ko) * | 2024-01-31 | 2025-08-07 | 주식회사 엘지화학 | 3-하이드록시프로피온산의 생산 방법 |
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| US11118187B2 (en) | 2021-09-14 |
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| EP3287519B1 (en) | 2020-03-18 |
| JP2013542747A (ja) | 2013-11-28 |
| US9090918B2 (en) | 2015-07-28 |
| ZA201303544B (en) | 2014-11-26 |
| BR112013012630A2 (pt) | 2020-09-24 |
| US20180044684A1 (en) | 2018-02-15 |
| CN103502432A (zh) | 2014-01-08 |
| EP2643450A2 (en) | 2013-10-02 |
| US10260072B2 (en) | 2019-04-16 |
| EP3287519A1 (en) | 2018-02-28 |
| CA2818499A1 (en) | 2012-06-07 |
| US12054721B2 (en) | 2024-08-06 |
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| US20120135481A1 (en) | 2012-05-31 |
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| US20200291408A1 (en) | 2020-09-17 |
| US20140065681A1 (en) | 2014-03-06 |
| US9777280B2 (en) | 2017-10-03 |
| CN107828671B (zh) | 2022-03-08 |
| WO2012074818A3 (en) | 2012-09-27 |
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