TWI575072B - 用於丁二烯生物合成之微生物及方法 - Google Patents
用於丁二烯生物合成之微生物及方法 Download PDFInfo
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- TWI575072B TWI575072B TW100115805A TW100115805A TWI575072B TW I575072 B TWI575072 B TW I575072B TW 100115805 A TW100115805 A TW 100115805A TW 100115805 A TW100115805 A TW 100115805A TW I575072 B TWI575072 B TW I575072B
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- Prior art keywords
- butadiene
- enzyme
- reductase
- microbial organism
- naturally occurring
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- C07C11/00—Aliphatic unsaturated hydrocarbons
- C07C11/12—Alkadienes
- C07C11/16—Alkadienes with four carbon atoms
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- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08F—MACROMOLECULAR COMPOUNDS OBTAINED BY REACTIONS ONLY INVOLVING CARBON-TO-CARBON UNSATURATED BONDS
- C08F136/00—Homopolymers of compounds having one or more unsaturated aliphatic radicals, at least one having two or more carbon-to-carbon double bonds
- C08F136/02—Homopolymers of compounds having one or more unsaturated aliphatic radicals, at least one having two or more carbon-to-carbon double bonds the radical having only two carbon-to-carbon double bonds
- C08F136/04—Homopolymers of compounds having one or more unsaturated aliphatic radicals, at least one having two or more carbon-to-carbon double bonds the radical having only two carbon-to-carbon double bonds conjugated
- C08F136/06—Butadiene
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- C12N1/18—Baker's yeast; Brewer's yeast
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| US8129154B2 (en) | 2008-06-17 | 2012-03-06 | Genomatica, Inc. | Microorganisms and methods for the biosynthesis of fumarate, malate, and acrylate |
| KR20110097951A (ko) | 2008-12-16 | 2011-08-31 | 게노마티카 인코포레이티드 | 합성가스와 다른 탄소원을 유용 제품으로 전환시키기 위한 미생물 및 방법 |
| JP2012529889A (ja) | 2009-06-10 | 2012-11-29 | ゲノマチカ, インク. | Mek及び2−ブタノールの炭素効率のよい生合成のための微生物及び方法 |
| CN109136161A (zh) | 2009-12-10 | 2019-01-04 | 基因组股份公司 | 合成气或其他气态碳源和甲醇转化为1,3-丁二醇的方法和有机体 |
| US8637286B2 (en) | 2010-02-23 | 2014-01-28 | Genomatica, Inc. | Methods for increasing product yields |
| MX336229B (es) * | 2010-05-05 | 2016-01-08 | Genomatica Inc | Microorganismos y metodos para la biosintesis de butadieno. |
| JP2013535203A (ja) | 2010-07-26 | 2013-09-12 | ジェノマティカ・インコーポレイテッド | 芳香族、2,4−ペンタジエノエートおよび1,3−ブタジエンを生合成するための微生物および方法 |
| MX348334B (es) * | 2011-02-02 | 2017-06-07 | Genomatica Inc | Microorganismo y metodos para la biosintesis de butadieno. |
| WO2013188546A2 (en) * | 2012-06-15 | 2013-12-19 | Invista Technologies S.À.R.L. | Methods for biosynthesizing 1,3 butadiene |
| US9422578B2 (en) | 2011-06-17 | 2016-08-23 | Invista North America S.A.R.L. | Methods for biosynthesizing 1,3 butadiene |
| US9663801B2 (en) | 2011-06-17 | 2017-05-30 | Invista North America S.A.R.L. | Methods of producing four carbon molecules |
| US9169486B2 (en) | 2011-06-22 | 2015-10-27 | Genomatica, Inc. | Microorganisms for producing butadiene and methods related thereto |
| SG11201400113XA (en) * | 2011-08-19 | 2014-08-28 | Genomatica Inc | Microorganisms and methods for producing 2,4-pentadienoate, butadiene, propylene, 1,3-butanediol and related alcohols |
| BR112014008061A2 (pt) * | 2011-10-19 | 2017-04-11 | Scientist Of Fortune Sa | método para a produção enzimática de butadieno |
| DK2776571T3 (en) | 2011-11-09 | 2017-06-26 | Amyris Inc | PREPARATION OF ACETYL-COENZYM A-DERIVED ISOPRENOIDS |
| CN104321434A (zh) * | 2011-12-02 | 2015-01-28 | 英威达技术有限责任公司 | 生物合成1,3丁二烯的方法 |
| EP2791342B1 (en) * | 2011-12-16 | 2020-04-29 | Braskem S.A. | Modified microorganisms and methods of making butadiene using same |
| EP2794891A2 (en) * | 2011-12-20 | 2014-10-29 | Scientist of Fortune S.A. | Production of 1,3-dienes by enzymatic conversion of 3-hydroxyalk-4-enoates and/or 3-phosphonoxyalk-4-enoates |
| US20150017698A1 (en) * | 2012-03-02 | 2015-01-15 | Codexis, Inc. a corporation | Recombinant host cells and processes for producing 1,3-butadiene through a 5-hydroxypent-3-enoate intermediate |
| WO2013130481A1 (en) * | 2012-03-02 | 2013-09-06 | Codexis, Inc. | Recombinant host cells and processes for producing 1,3-butadiene through a crotonol intermediate |
| US9803209B2 (en) | 2012-05-18 | 2017-10-31 | Novozymes A/S | Bacterial mutants with improved transformation efficiency |
| US20150152440A1 (en) * | 2012-06-18 | 2015-06-04 | Braskem S.A. | Modified microorganisms and methods of co-producing butadiene with 1-propanol and/or 1,2-propanediol |
| BR112015004488A2 (pt) * | 2012-08-28 | 2018-11-21 | Braskem Sa | método de coprodução de um terpeno e pelo menos um coproduto a partir de uma fonte de carbono fermentável |
| WO2014052630A1 (en) | 2012-09-27 | 2014-04-03 | Novozymes, Inc. | Bacterial mutants with improved transformation efficiency |
| WO2014055649A1 (en) * | 2012-10-02 | 2014-04-10 | Braskem S/A Ap 09 | Modified microorganisms and methods of using same for producing butadiene and succinate |
| WO2014063156A2 (en) * | 2012-10-19 | 2014-04-24 | Braskem S/A Ap 09 | Modified microorganisms and methods of using same for producing butadiene and one or more of 1,3-butanediol, 1,4-butanediol, and/or 1,3-propanediol |
| US11535874B2 (en) * | 2012-10-22 | 2022-12-27 | Genomatica, Inc. | Microorganisms and methods for enhancing the availability of reducing equivalents in the presence of methanol, and for producing succinate related thereto |
| EP2920314A1 (en) * | 2012-11-13 | 2015-09-23 | Global Bioenergies | Process for the enzymatic preparation of isoprene from isoprenol |
| WO2014081973A1 (en) * | 2012-11-21 | 2014-05-30 | The Regents Of The University Of California | Nucleic acids useful for integrating into and gene expression in hyperthermophilic acidophilic archaea |
| CN104903455A (zh) | 2012-11-28 | 2015-09-09 | 英威达技术有限责任公司 | 用于异丁烯生物合成的方法 |
| JP6304924B2 (ja) * | 2012-11-29 | 2018-04-04 | 住友ゴム工業株式会社 | サイドウォール用ゴム組成物、及び空気入りタイヤ |
| WO2014089025A1 (en) * | 2012-12-04 | 2014-06-12 | Genomatica, Inc. | Increased yields of biosynthesized products |
| WO2014106122A1 (en) * | 2012-12-31 | 2014-07-03 | Genomatica, Inc. | Compositions and methods for bio-butadiene production screening |
| JP2014155455A (ja) * | 2013-02-15 | 2014-08-28 | Sekisui Chem Co Ltd | 組換え細胞、並びに、クロトニルCoA又はクロチルアルコールの生産方法 |
| JP2014161252A (ja) * | 2013-02-22 | 2014-09-08 | Sekisui Chem Co Ltd | 組換え細胞 |
| EP2971021A4 (en) | 2013-03-15 | 2016-12-21 | Genomatica Inc | MICROORGANISMS AND METHOD FOR THE PRODUCTION OF BUTADIENE AND RELATED COMPOUNDS BY FORMATASSIMILATION |
| ES2728307T3 (es) | 2013-06-21 | 2019-10-23 | Danisco Us Inc | Composiciones y métodos para la transformación clostridial |
| US10294496B2 (en) | 2013-07-19 | 2019-05-21 | Invista North America S.A.R.L. | Methods for biosynthesizing 1,3 butadiene |
| EP3030668A1 (en) | 2013-08-05 | 2016-06-15 | Invista Technologies S.A R.L. | Methods for biosynthesis of isobutene |
| CN105683385A (zh) | 2013-08-05 | 2016-06-15 | 英威达技术有限责任公司 | 用于生物合成异戊二烯的方法 |
| PL3077501T3 (pl) | 2013-12-03 | 2022-01-31 | Genomatica, Inc. | Mikroorganizmy i sposoby poprawy wydajności produktu na metanolu z użyciem syntezy acetylo-coa |
| WO2015100338A2 (en) | 2013-12-27 | 2015-07-02 | Genomatica, Inc. | Methods and organisms with increased carbon flux efficiencies |
| WO2015147644A1 (en) * | 2014-03-27 | 2015-10-01 | Photanol B.V. | Erythritol production in cyanobacteria |
| CN106795519A (zh) | 2014-06-16 | 2017-05-31 | 英威达技术有限责任公司 | 用于生成戊二酸和戊二酸甲酯的方法 |
| US10487342B2 (en) | 2014-07-11 | 2019-11-26 | Genomatica, Inc. | Microorganisms and methods for the production of butadiene using acetyl-CoA |
| EP3741865B1 (en) | 2014-09-18 | 2024-03-13 | Genomatica, Inc. | Non-natural microbial organisms with improved energetic efficiency |
| CN104298866B (zh) * | 2014-09-30 | 2017-06-06 | 杭州电子科技大学 | 一种克劳斯硫磺回收过程中反应炉动态建模方法 |
| JP6432774B2 (ja) * | 2014-12-25 | 2018-12-05 | 江南化工株式会社 | 細胞賦活剤 |
| MX387737B (es) | 2015-02-27 | 2025-03-18 | White Dog Labs Inc | Método de fermentación mixotrófica para producir acetona, isopropanol, acido butírico y otros bioproductos, y mezclas de los mismos. |
| WO2016160812A1 (en) * | 2015-03-31 | 2016-10-06 | White Dog Labs, Inc. | Method of producing bioproducts |
| KR20170134682A (ko) * | 2015-04-09 | 2017-12-06 | 게노마티카 인코포레이티드 | 향상된 크로틸 알코올 생성을 위한 유전자조작 미생물 및 방법 |
| CN108026214B (zh) | 2015-05-30 | 2021-03-02 | 基因组股份公司 | 乙烯基异构酶-脱水酶、烯醇脱水酶、芳樟醇脱水酶和/或巴豆醇脱水酶及其制备和使用 |
| WO2017064606A1 (en) * | 2015-10-12 | 2017-04-20 | Reliance Industries Limited | Process for preparation of 1,3-butadiene |
| SG11201803164SA (en) | 2015-10-30 | 2018-05-30 | Genomatica Inc | Methanol dehydrogenase fusion proteins |
| GB201605354D0 (en) | 2016-03-30 | 2016-05-11 | Zuvasyntha Ltd | Modified enzyme |
| US10919030B2 (en) | 2016-09-30 | 2021-02-16 | Regents Of The University Of Minnesota | Forming dienes from cyclic ethers and diols, including tetrahydrofuran and 2-methyl-1,4-butanediol |
| JP6317497B2 (ja) * | 2017-03-22 | 2018-04-25 | 住友ゴム工業株式会社 | トレッド用ゴム組成物、及び空気入りタイヤ |
| JP6317498B2 (ja) * | 2017-03-22 | 2018-04-25 | 住友ゴム工業株式会社 | スタッドレスタイヤ用トレッド用ゴム組成物、及びスタッドレスタイヤ |
| JP2020512351A (ja) * | 2017-03-31 | 2020-04-23 | ジェノマティカ, インコーポレイテッド | 発酵ブロスから1,3−ブタンジオールを取得するためのプロセスおよびシステム |
| US11634733B2 (en) | 2017-06-30 | 2023-04-25 | Inv Nylon Chemicals Americas, Llc | Methods, materials, synthetic hosts and reagents for the biosynthesis of hydrocarbons and derivatives thereof |
| WO2019006257A1 (en) | 2017-06-30 | 2019-01-03 | Invista North America .S.A.R.L. | METHODS, SYNTHETIC HOSTS AND REAGENTS FOR HYDROCARBON BIOSYNTHESIS |
| US11505809B2 (en) | 2017-09-28 | 2022-11-22 | Inv Nylon Chemicals Americas Llc | Organisms and biosynthetic processes for hydrocarbon synthesis |
| US20210079334A1 (en) | 2018-01-30 | 2021-03-18 | Genomatica, Inc. | Fermentation systems and methods with substantially uniform volumetric uptake rate of a reactive gaseous component |
| US11541105B2 (en) | 2018-06-01 | 2023-01-03 | The Research Foundation For The State University Of New York | Compositions and methods for disrupting biofilm formation and maintenance |
| EP3814515A2 (en) | 2018-06-26 | 2021-05-05 | Genomatica, Inc. | Engineered microorganisms with g3p---> 3pg enzyme and/or fructose-1,6-bisphosphatase including those having synthetic or enhanced methylotrophy |
| US20220258100A1 (en) * | 2019-07-16 | 2022-08-18 | San Diego State University (SDSU) Foundation, dba San Diego State University Research Foundation | Products of manufacture and methods for methane capturing using biofiltration |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TW200630333A (en) * | 2005-01-17 | 2006-09-01 | Basf Ag | Preparation of butadiene from n-butane |
| US20100003716A1 (en) * | 2008-04-23 | 2010-01-07 | Cervin Marguerite A | Isoprene synthase variants for improved microbial production of isoprene |
| TW201016854A (en) * | 2008-09-10 | 2010-05-01 | Genomatica Inc | Microorganisms for the production of 1,4-butanediol |
Family Cites Families (155)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4076948A (en) | 1968-10-10 | 1978-02-28 | El Paso Products Company | Process for treatment of adipic acid mother liquor |
| US3513209A (en) | 1968-08-19 | 1970-05-19 | Du Pont | Method of making 1,4-cyclohexadiene |
| GB1230276A (enExample) | 1968-12-09 | 1971-04-28 | ||
| US3965182A (en) | 1969-10-02 | 1976-06-22 | Ethyl Corporation | Preparation of aniline from phenol and ammonia |
| JPS4831084B1 (enExample) | 1970-09-04 | 1973-09-26 | ||
| GB1344557A (en) | 1972-06-23 | 1974-01-23 | Mitsubishi Petrochemical Co | Process for preparing 1,4-butanediol |
| JPS5543759B2 (enExample) | 1972-06-28 | 1980-11-07 | ||
| DE2455617C3 (de) | 1974-11-23 | 1982-03-18 | Basf Ag, 6700 Ludwigshafen | Verfahren zur Herstellung von Butandiol und/oder Tetrahydrofuran über die Zwischenstufe des γ-Butyrolactons |
| DE2501499A1 (de) | 1975-01-16 | 1976-07-22 | Hoechst Ag | Verfahren zur herstellung von butandiol-(1.4) |
| US4190495A (en) | 1976-09-27 | 1980-02-26 | Research Corporation | Modified microorganisms and method of preparing and using same |
| US4301077A (en) | 1980-12-22 | 1981-11-17 | Standard Oil Company | Process for the manufacture of 1-4-butanediol and tetrahydrofuran |
| JPS60114197A (ja) | 1983-11-25 | 1985-06-20 | Agency Of Ind Science & Technol | 微生物によるジカルボン酸の製造法 |
| US4871667A (en) | 1984-11-26 | 1989-10-03 | Agency Of Industrial Science & Technology | Process for preparing muconic acid |
| US4652685A (en) | 1985-11-15 | 1987-03-24 | General Electric Company | Hydrogenation of lactones to glycols |
| US5168055A (en) | 1986-06-11 | 1992-12-01 | Rathin Datta | Fermentation and purification process for succinic acid |
| ES2036188T3 (es) | 1986-06-11 | 1993-05-16 | Michigan Biotechnology Institute | Un procedimiento para la produccion de acido succinico por fermentacion anaerobia. |
| US5143834A (en) | 1986-06-11 | 1992-09-01 | Glassner David A | Process for the production and purification of succinic acid |
| US5182199A (en) | 1987-05-27 | 1993-01-26 | Hartley Brian S | Thermophilic ethanol production in a two-stage closed system |
| JPH01195596A (ja) | 1988-01-30 | 1989-08-07 | Casio Comput Co Ltd | 値札システム |
| US5219757A (en) | 1988-04-27 | 1993-06-15 | Daicel Chemical Industries, Ltd. | Production of optically active 1,3-butanediol by asymmetric assimilation or reduction of 4-hydroxy-2-butanone |
| CA2062753C (en) | 1989-04-27 | 2005-04-26 | N. Robert Ward, Jr. | Precipitate test for microorganisms |
| US5192673A (en) | 1990-04-30 | 1993-03-09 | Michigan Biotechnology Institute | Mutant strain of C. acetobutylicum and process for making butanol |
| US5079143A (en) | 1990-05-02 | 1992-01-07 | The Upjohn Company | Method of indentifying compounds useful as antiparasitic drugs |
| EP0769557B1 (en) | 1990-10-15 | 2000-11-15 | Daicel Chemical Industries, Ltd. | Process for producing optically active 1,3-butanediol |
| US5173429A (en) | 1990-11-09 | 1992-12-22 | The Board Of Trustees Of The University Of Arkansas | Clostridiumm ljungdahlii, an anaerobic ethanol and acetate producing microorganism |
| IL100572A (en) | 1991-01-03 | 1997-01-10 | Lepetit Spa | Amides of antibiotic ge 2270 factors their preparation and pharmaceutical compositions containing them |
| US5416020A (en) | 1992-09-29 | 1995-05-16 | Bio-Technical Resources | Lactobacillus delbrueckii ssp. bulgaricus strain and fermentation process for producing L-(+)-lactic acid |
| US5807722A (en) | 1992-10-30 | 1998-09-15 | Bioengineering Resources, Inc. | Biological production of acetic acid from waste gases with Clostridium ljungdahlii |
| US6136577A (en) | 1992-10-30 | 2000-10-24 | Bioengineering Resources, Inc. | Biological production of ethanol from waste gases with Clostridium ljungdahlii |
| FR2702492B1 (fr) | 1993-03-12 | 1995-05-24 | Rhone Poulenc Chimie | Procédé de production par fermentation d'acide itaconique. |
| US5487987A (en) | 1993-09-16 | 1996-01-30 | Purdue Research Foundation | Synthesis of adipic acid from biomass-derived carbon sources |
| US5521075A (en) | 1994-12-19 | 1996-05-28 | Michigan Biotechnology Institute | Method for making succinic acid, anaerobiospirillum succiniciproducens variants for use in process and methods for obtaining variants |
| US5504004A (en) | 1994-12-20 | 1996-04-02 | Michigan Biotechnology Institute | Process for making succinic acid, microorganisms for use in the process and methods of obtaining the microorganisms |
| US5700934A (en) | 1995-03-01 | 1997-12-23 | Dsm N.V. | Process for the preparation of epsilon-caprolactam and epsilon-caprolactam precursors |
| US5478952A (en) | 1995-03-03 | 1995-12-26 | E. I. Du Pont De Nemours And Company | Ru,Re/carbon catalyst for hydrogenation in aqueous solution |
| US5863782A (en) | 1995-04-19 | 1999-01-26 | Women's And Children's Hospital | Synthetic mammalian sulphamidase and genetic sequences encoding same |
| US5686276A (en) | 1995-05-12 | 1997-11-11 | E. I. Du Pont De Nemours And Company | Bioconversion of a fermentable carbon source to 1,3-propanediol by a single microorganism |
| US5849970A (en) * | 1995-06-23 | 1998-12-15 | The Regents Of The University Of Colorado | Materials and methods for the bacterial production of isoprene |
| FR2736927B1 (fr) | 1995-07-18 | 1997-10-17 | Rhone Poulenc Fibres & Polymer | Enzymes a activite amidase, outils genetiques et microorganismes hotes permettant leur obtention et procede d'hydrolyse mettant en oeuvre lesdites enzymes |
| US5573931A (en) | 1995-08-28 | 1996-11-12 | Michigan Biotechnology Institute | Method for making succinic acid, bacterial variants for use in the process, and methods for obtaining variants |
| US5869301A (en) | 1995-11-02 | 1999-02-09 | Lockhead Martin Energy Research Corporation | Method for the production of dicarboxylic acids |
| US5770435A (en) | 1995-11-02 | 1998-06-23 | University Of Chicago | Mutant E. coli strain with increased succinic acid production |
| JP2000506012A (ja) | 1996-02-27 | 2000-05-23 | ミシガン ステイト ユニヴァーシティー | サーモアンエアロバクター・エタノリカス39eの第二級アルコールデヒドロゲナーゼをコードする遺伝子のクローニング及び発現並びに酵素の生化学的特徴付け |
| US5958745A (en) | 1996-03-13 | 1999-09-28 | Monsanto Company | Methods of optimizing substrate pools and biosynthesis of poly-β-hydroxybutyrate-co-poly-β-hydroxyvalerate in bacteria and plants |
| JP4101295B2 (ja) | 1996-07-01 | 2008-06-18 | バイオエンジニアリング・リソーシズ・インコーポレーテツド | 廃ガスからの酢酸の生物学的生産 |
| KR100459818B1 (ko) | 1996-09-02 | 2004-12-03 | 이. 아이. 두퐁 드 느무르 앤드 컴퍼니 | ε-카프로락탐의 제조방법 |
| US6117658A (en) | 1997-02-13 | 2000-09-12 | James Madison University | Methods of making polyhydroxyalkanoates comprising 4-hydroxybutyrate monomer units |
| KR100516986B1 (ko) | 1997-02-19 | 2005-09-26 | 코닌클리즈케 디에스엠 엔.브이. | 6-아미노카프론산 유도체를 과열 수증기와 접촉시킴으로써 촉매 없이 카프로락탐을 제조하는 방법 |
| US6274790B1 (en) | 1997-04-14 | 2001-08-14 | The University Of British Columbia | Nucleic acids encoding a plant enzyme involved in very long chain fatty acid synthesis |
| KR19990013007A (ko) | 1997-07-31 | 1999-02-25 | 박원훈 | 형질전환된 대장균 ss373(kctc 8818p)과 이를 이용한숙신산의 생산방법 |
| JPH11103863A (ja) | 1997-10-08 | 1999-04-20 | Nippon Shokubai Co Ltd | マレイン酸異性化酵素遺伝子 |
| US6280986B1 (en) | 1997-12-01 | 2001-08-28 | The United States Of America As Represented By The Secretary Of Agriculture | Stabilization of pet operon plasmids and ethanol production in bacterial strains lacking lactate dehydrogenase and pyruvate formate lyase activities |
| US20030087381A1 (en) | 1998-04-13 | 2003-05-08 | University Of Georgia Research Foundation, Inc. | Metabolically engineered organisms for enhanced production of oxaloacetate-derived biochemicals |
| 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 |
| US6159738A (en) | 1998-04-28 | 2000-12-12 | University Of Chicago | Method for construction of bacterial strains with increased succinic acid production |
| DE19820652A1 (de) | 1998-05-08 | 1999-11-11 | Basf Ag | Kationische Rutheniumkomplexe, Verfahren zu ihrer Herstellung und ihre Verwendung |
| US6432686B1 (en) | 1998-05-12 | 2002-08-13 | E. I. Du Pont De Nemours And Company | Method for the production of 1,3-propanediol by recombinant organisms comprising genes for vitamin B12 transport |
| US6444784B1 (en) | 1998-05-29 | 2002-09-03 | Exxonmobil Research & Engineering Company | Wax crystal modifiers (LAW657) |
| WO2000004163A1 (en) | 1998-07-15 | 2000-01-27 | E.I. Du Pont De Nemours And Company | Tetrahydrofolate metabolism enzymes |
| DE19856136C2 (de) | 1998-12-04 | 2002-10-24 | Pasteur Institut | Verfahren und Vorrichtung zur Selektion beschleunigter Proliferation lebender Zellen in Suspension |
| WO2000046405A2 (en) | 1999-02-02 | 2000-08-10 | Bernhard Palsson | Methods for identifying drug targets based on genomic sequence data |
| US6686310B1 (en) | 1999-02-09 | 2004-02-03 | E. I. Du Pont De Nemours And Company | High surface area sol-gel route prepared hydrogenation catalysts |
| US6365376B1 (en) | 1999-02-19 | 2002-04-02 | E. I. Du Pont De Nemours And Company | Genes and enzymes for the production of adipic acid intermediates |
| US6448473B1 (en) | 1999-03-05 | 2002-09-10 | Monsanto Technology Llc | Multigene expression vectors for the biosynthesis of products via multienzyme biological pathways |
| CA2374482C (en) | 1999-05-21 | 2012-09-18 | Cargill Dow Llc | Methods and materials for the synthesis of organic products |
| US6852517B1 (en) | 1999-08-30 | 2005-02-08 | Wisconsin Alumni Research Foundation | Production of 3-hydroxypropionic acid in recombinant organisms |
| US6660857B2 (en) | 2000-02-03 | 2003-12-09 | Dsm N.V. | Process for the preparation of ε-caprolactam |
| US6878861B2 (en) | 2000-07-21 | 2005-04-12 | Washington State University Research Foundation | Acyl coenzyme A thioesterases |
| NZ523484A (en) | 2000-07-25 | 2005-01-28 | Emmaus Foundation Inc | Methods for increasing the production of ethanol from microbial fermentation |
| 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 |
| CN1358841A (zh) | 2000-12-11 | 2002-07-17 | 云南省微生物研究所 | 云南链霉菌 |
| US7501268B2 (en) | 2000-12-28 | 2009-03-10 | Toyota Jidosha Kabushiki Kaisha | Methods of producing prenyl alcohols |
| CA2434224C (en) | 2001-01-10 | 2013-04-02 | The Penn State Research Foundation | Method and system for modeling cellular metabolism |
| US7127379B2 (en) | 2001-01-31 | 2006-10-24 | The Regents Of The University Of California | Method for the evolutionary design of biochemical reaction networks |
| US20030059792A1 (en) | 2001-03-01 | 2003-03-27 | Palsson Bernhard O. | Models and methods for determining systemic properties of regulated reaction networks |
| US6743610B2 (en) | 2001-03-30 | 2004-06-01 | The University Of Chicago | Method to produce succinic acid from raw hydrolysates |
| JP4630486B2 (ja) | 2001-05-28 | 2011-02-09 | ダイセル化学工業株式会社 | 新規な(r)−2,3−ブタンジオール脱水素酵素、その製造方法、及びこれを利用した光学活性アルコールの製造方法 |
| CA2356540A1 (en) | 2001-08-30 | 2003-02-28 | Emory University | Expressed dna sequences involved in mitochondrial functions |
| CA2466133A1 (en) | 2001-11-02 | 2003-05-15 | Rice University | Recycling system for manipulation of intracellular nadh availability |
| DE60327804D1 (de) | 2002-01-18 | 2009-07-09 | Novozymes As | Alanin-2,3-aminomutase |
| WO2003066863A1 (fr) | 2002-02-06 | 2003-08-14 | Showa Denko K.K. | Gene reductase d'un compose carbonyle alpha-substitue-alpha, beta-insature |
| US20030224363A1 (en) | 2002-03-19 | 2003-12-04 | Park Sung M. | Compositions and methods for modeling bacillus subtilis metabolism |
| CA2480216A1 (en) | 2002-03-29 | 2003-10-09 | Genomatica, Inc. | Human metabolic models and methods |
| US20050287655A1 (en) | 2002-05-10 | 2005-12-29 | Kyowa Hakko Kogyo Co., Ltd. | Process for producing mevalonic acid |
| US7856317B2 (en) | 2002-06-14 | 2010-12-21 | Genomatica, Inc. | Systems and methods for constructing genomic-based phenotypic models |
| US7826975B2 (en) | 2002-07-10 | 2010-11-02 | The Penn State Research Foundation | Method for redesign of microbial production systems |
| EP1532516A4 (en) | 2002-07-10 | 2007-05-23 | Penn State Res Found | Method for determining gene knockout strategies |
| WO2004007688A2 (en) | 2002-07-15 | 2004-01-22 | Kosan Biosciences, Inc. | Metabolic pathways for starter units in polyketide biosynthesis |
| AU2003287028B2 (en) | 2002-10-04 | 2008-09-04 | E.I. Du Pont De Nemours And Company | Process for the biological production of 1,3-propanediol with high yield |
| AU2003222214B2 (en) | 2002-10-15 | 2010-08-12 | The Regents Of The University Of California | Methods and systems to identify operational reaction pathways |
| AU2003287625A1 (en) | 2002-11-06 | 2004-06-03 | University Of Florida | Materials and methods for the efficient production of acetate and other products |
| CN1802341A (zh) | 2003-01-13 | 2006-07-12 | 卡吉尔公司 | 制备工业化学品的方法 |
| US7432091B2 (en) | 2003-02-24 | 2008-10-07 | Research Institute Of Innovative Technology For The Earth | Highly efficient hydrogen production method using microorganism |
| RU2268300C2 (ru) | 2003-04-07 | 2006-01-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИЙ, ОБЛАДАЮЩИХ ПОВЫШЕННОЙ ЭКСПРЕССИЕЙ ГЕНА pckA |
| WO2005010182A1 (ja) | 2003-07-29 | 2005-02-03 | Research Institute Of Innovative Technology For The Earth | コリネ型細菌形質転換体及びそれを用いるジカルボン酸の製造方法 |
| US7927859B2 (en) | 2003-08-22 | 2011-04-19 | Rice University | High molar succinate yield bacteria by increasing the intracellular NADH availability |
| WO2005026349A1 (ja) | 2003-09-17 | 2005-03-24 | Mitsubishi Chemical Corporation | 非アミノ有機酸の製造方法 |
| US7244610B2 (en) | 2003-11-14 | 2007-07-17 | Rice University | Aerobic succinate production in bacteria |
| FR2864967B1 (fr) | 2004-01-12 | 2006-05-19 | Metabolic Explorer Sa | Microorganisme evolue pour la production de 1,2-propanediol |
| CN1926240B (zh) | 2004-01-19 | 2010-06-02 | 帝斯曼知识产权资产管理有限公司 | 6-氨基己酸的生物化学合成 |
| US7608700B2 (en) | 2004-03-08 | 2009-10-27 | North Carolina State University | Lactobacillus acidophilus nucleic acid sequences encoding stress-related proteins and uses therefor |
| DE102004031177A1 (de) | 2004-06-29 | 2006-01-19 | Henkel Kgaa | Neue Geruchsstoffe bildende Genprodukte von Bacillus licheniformis und darauf aufbauende verbesserte biotechnologische Produktionsverfahren |
| US7262046B2 (en) | 2004-08-09 | 2007-08-28 | Rice University | Aerobic succinate production in bacteria |
| JP2008510485A (ja) * | 2004-08-26 | 2008-04-10 | ザ ペン ステイト リサーチ ファウンデーション | 微生物産生系の再設計法 |
| CN101044245B (zh) | 2004-08-27 | 2012-05-02 | 莱斯大学 | 具有增加的琥珀酸产量的突变大肠杆菌菌株 |
| EP2434015B1 (en) | 2004-09-09 | 2013-11-20 | Research Institute Of Innovative Technology For The Earth | DNA fragment having promoter function |
| EP1789569A2 (en) | 2004-09-17 | 2007-05-30 | Rice University | High succinate producing bacteria |
| EP1801227B1 (en) | 2004-10-14 | 2009-04-15 | Sumitomo Chemical Company, Limited | Method for producing 2-hydroxy-4-(methylthio)butanoic acid |
| US7569380B2 (en) | 2004-12-22 | 2009-08-04 | Rice University | Simultaneous anaerobic production of isoamyl acetate and succinic acid |
| JP2006204255A (ja) | 2005-01-31 | 2006-08-10 | Canon Inc | アセチル−CoAアシルトランスフェラーゼ遺伝子破壊ポリヒドロキシアルカノエート生産菌、またこれを利用したポリヒドロキシアルカノエート生産方法 |
| EP1874334A4 (en) | 2005-04-15 | 2011-03-30 | Vascular Biogenics Ltd | COMPOSITIONS WITH BETA 2-GLYCOPROTEIN I-PEPTIDES FOR THE PREVENTION AND / OR TREATMENT OF VASCULAR DISEASES |
| KR100679638B1 (ko) | 2005-08-19 | 2007-02-06 | 한국과학기술원 | 포메이트 디하이드로게나제 d 또는 e를 코딩하는 유전자로 형질전환된 미생물 및 이를 이용한 숙신산의 제조방법 |
| KR100676160B1 (ko) | 2005-08-19 | 2007-02-01 | 한국과학기술원 | 말릭효소를 코딩하는 유전자로 형질전환된 재조합 미생물 및 이를 이용한 숙신산의 제조방법 |
| AU2006287257A1 (en) | 2005-09-09 | 2007-03-15 | Genomatica, Inc. | Methods and organisms for the growth-coupled production of succinate |
| US9297028B2 (en) | 2005-09-29 | 2016-03-29 | Butamax Advanced Biofuels Llc | Fermentive production of four carbon alcohols |
| NZ566406A (en) | 2005-10-26 | 2012-04-27 | Butamax Advanced Biofuels Llc | Fermentive production of four carbon alcohols |
| GB2433260A (en) | 2005-12-16 | 2007-06-20 | Mologic Ltd | A selectable decarboxylase marker |
| US8206970B2 (en) | 2006-05-02 | 2012-06-26 | Butamax(Tm) Advanced Biofuels Llc | Production of 2-butanol and 2-butanone employing aminobutanol phosphate phospholyase |
| DE102006025821A1 (de) | 2006-06-02 | 2007-12-06 | Degussa Gmbh | Ein Enzym zur Herstellung von Mehylmalonatsemialdehyd oder Malonatsemialdehyd |
| US8017364B2 (en) | 2006-12-12 | 2011-09-13 | Butamax(Tm) Advanced Biofuels Llc | Solvent tolerant microorganisms |
| 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 |
| CA2678946C (en) | 2007-03-16 | 2019-02-12 | Genomatica, Inc. | Compositions and methods for the biosynthesis of 1,4-butanediol and its precursors |
| EP2147111A4 (en) | 2007-04-18 | 2010-06-23 | Gevo Inc | MANIPULATED MICROORGANISMS FOR THE MANUFACTURE OF ISOPROPANOL |
| US20080274522A1 (en) | 2007-05-02 | 2008-11-06 | Bramucci Michael G | Method for the production of 2-butanone |
| WO2008144060A2 (en) | 2007-05-17 | 2008-11-27 | Tetravitae Bioscience, Inc. | Methods and compositions for producing solvents |
| EP2017344A1 (en) | 2007-07-20 | 2009-01-21 | Nederlandse Organisatie voor toegepast- natuurwetenschappelijk onderzoek TNO | Production of itaconic acid |
| CN101970673A (zh) | 2007-07-23 | 2011-02-09 | 帝斯曼知识产权资产管理有限公司 | 真核细胞中的丁醇生产 |
| US7947483B2 (en) | 2007-08-10 | 2011-05-24 | Genomatica, Inc. | Methods and organisms for the growth-coupled production of 1,4-butanediol |
| AU2008310573A1 (en) | 2007-10-12 | 2009-04-16 | The Regents Of The University Of California | Microorganism engineered to produce isopropanol |
| BRPI0823506A8 (pt) * | 2007-12-13 | 2018-05-15 | Danisco Us Inc Genencor Div | composições e métodos para a produção de isoprene |
| US8183028B2 (en) | 2007-12-21 | 2012-05-22 | Ls9, Inc. | Methods and compositions for producing olefins |
| CA2712779C (en) | 2008-01-22 | 2021-03-16 | Genomatica, Inc. | Methods and organisms for utilizing synthesis gas or other gaseous carbon sources and methanol |
| CN102015995B (zh) * | 2008-03-03 | 2014-10-22 | 焦耳无限科技公司 | 产生碳基目的产物的二氧化碳固定工程微生物 |
| SI2265709T1 (en) | 2008-03-27 | 2018-03-30 | Genomatica, Inc. | MICROORGANISMS FOR PREPARATION OF ADYPIC ACID AND OTHER COMPOUNDS |
| JP2011519561A (ja) | 2008-05-01 | 2011-07-14 | ジェノマティカ, インコーポレイテッド | メタクリル酸の産生のための微生物 |
| US8129154B2 (en) | 2008-06-17 | 2012-03-06 | Genomatica, Inc. | Microorganisms and methods for the biosynthesis of fumarate, malate, and acrylate |
| SG167485A1 (en) | 2008-06-30 | 2011-01-28 | Danisco Us Inc | Polymers of isoprene from renewable resources |
| EP2313491A4 (en) | 2008-07-08 | 2011-12-07 | Opx Biotechnologies Inc | METHODS, COMPOSITIONS AND SYSTEMS FOR BIOSYNTHETIC BIOPRODUCTION OF 1,4-BUTANEDIOL |
| WO2010022763A1 (en) | 2008-08-25 | 2010-03-04 | Metabolic Explorer | Method for the preparation of 2-hydroxy-isobutyrate |
| CA2737082A1 (en) * | 2008-09-15 | 2010-03-18 | Danisco Us Inc. | Increased isoprene production using mevalonate kinase and isoprene synthase |
| WO2010031079A1 (en) | 2008-09-15 | 2010-03-18 | Danisco Us Inc. | Systems using cell culture for production of isoprene |
| US8357826B2 (en) | 2008-10-16 | 2013-01-22 | Karl Kharas | Methods and apparatus for synthesis of alcohols from syngas |
| EP3260532A1 (en) | 2008-12-12 | 2017-12-27 | CJ Research Center LLC | Green process and compositions for producing poly(5hv) and 5 carbon chemicals |
| KR20110097951A (ko) | 2008-12-16 | 2011-08-31 | 게노마티카 인코포레이티드 | 합성가스와 다른 탄소원을 유용 제품으로 전환시키기 위한 미생물 및 방법 |
| BRPI1013426A2 (pt) * | 2009-04-30 | 2016-11-08 | Genomatica Inc | organismos para produção de 1,3-butanodiol |
| SI3392340T1 (sl) | 2009-06-04 | 2022-05-31 | Genomatica, Inc. | Mikroorganizmi za proizvodnjo 1,4-BUTANDIOLA in pripadajoči postopki |
| US20120276606A1 (en) | 2009-10-30 | 2012-11-01 | Daicel Corporation | Recombinant microorganisms with 1,3-butanediol-producing function and uses thereof |
| CN109136161A (zh) | 2009-12-10 | 2019-01-04 | 基因组股份公司 | 合成气或其他气态碳源和甲醇转化为1,3-丁二醇的方法和有机体 |
| MX336229B (es) | 2010-05-05 | 2016-01-08 | Genomatica Inc | Microorganismos y metodos para la biosintesis de butadieno. |
| MX348334B (es) * | 2011-02-02 | 2017-06-07 | Genomatica Inc | Microorganismo y metodos para la biosintesis de butadieno. |
| US9169486B2 (en) * | 2011-06-22 | 2015-10-27 | Genomatica, Inc. | Microorganisms for producing butadiene and methods related thereto |
| BR112014008061A2 (pt) * | 2011-10-19 | 2017-04-11 | Scientist Of Fortune Sa | método para a produção enzimática de butadieno |
| US20150050708A1 (en) * | 2013-03-15 | 2015-02-19 | Genomatica, Inc. | Microorganisms and methods for producing butadiene and related compounds by formate assimilation |
| EP2971021A4 (en) * | 2013-03-15 | 2016-12-21 | Genomatica Inc | MICROORGANISMS AND METHOD FOR THE PRODUCTION OF BUTADIENE AND RELATED COMPOUNDS BY FORMATASSIMILATION |
-
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- 2017-07-10 US US15/645,880 patent/US10487343B2/en not_active Expired - Fee Related
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TW200630333A (en) * | 2005-01-17 | 2006-09-01 | Basf Ag | Preparation of butadiene from n-butane |
| US20100003716A1 (en) * | 2008-04-23 | 2010-01-07 | Cervin Marguerite A | Isoprene synthase variants for improved microbial production of isoprene |
| TW201016854A (en) * | 2008-09-10 | 2010-05-01 | Genomatica Inc | Microorganisms for the production of 1,4-butanediol |
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