BRPI0720801A2 - Produção de um lipídio aciltranfersase a partir de células transformadas de bacillus licheniformis. - Google Patents
Produção de um lipídio aciltranfersase a partir de células transformadas de bacillus licheniformis. Download PDFInfo
- Publication number
- BRPI0720801A2 BRPI0720801A2 BRPI0720801-4A BRPI0720801A BRPI0720801A2 BR PI0720801 A2 BRPI0720801 A2 BR PI0720801A2 BR PI0720801 A BRPI0720801 A BR PI0720801A BR PI0720801 A2 BRPI0720801 A2 BR PI0720801A2
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- Prior art keywords
- seq
- nucleotide sequence
- lipid acyltransferase
- acyltransferase
- amino acid
- Prior art date
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/75—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Bacillus
-
- 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
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/1029—Acyltransferases (2.3) transferring groups other than amino-acyl groups (2.3.1)
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
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- Engineering & Computer Science (AREA)
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- Molecular Biology (AREA)
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- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (1)
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|---|---|---|---|
| PCT/IB2007/000558 WO2008090395A1 (en) | 2007-01-25 | 2007-01-25 | Production of a lipid acyltransferase from transformed bacillus licheniformis cells |
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| BRPI0720801A2 true BRPI0720801A2 (pt) | 2014-09-16 |
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| BRPI0720801-4A BRPI0720801A2 (pt) | 2007-01-25 | 2007-01-25 | Produção de um lipídio aciltranfersase a partir de células transformadas de bacillus licheniformis. |
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| EP (2) | EP2109670A1 (enExample) |
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| WO (1) | WO2008090395A1 (enExample) |
Families Citing this family (15)
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| ATE362315T1 (de) | 2001-05-18 | 2007-06-15 | Danisco | Verfahren zur herstellung von teig mit einem enzym |
| GB0716126D0 (en) * | 2007-08-17 | 2007-09-26 | Danisco | Process |
| WO2006008508A1 (en) | 2004-07-16 | 2006-01-26 | Danisco A/S | Enzymatic oil-degumming method |
| EA020035B1 (ru) | 2007-12-21 | 2014-08-29 | ДюПон НЬЮТРИШН БАЙОСАЙЕНСИЗ АпС | Способы |
| CN101418276B (zh) * | 2008-12-08 | 2010-12-22 | 江南大学 | 一种宿主细胞及其用于重组蛋白高效分泌表达的方法 |
| GB0905367D0 (en) * | 2009-03-27 | 2009-05-13 | Danisco | Method |
| CN102656264A (zh) * | 2009-10-15 | 2012-09-05 | 丹尼斯科公司 | 脂质酰基转移酶蛋白及其制备方法 |
| GB0920089D0 (en) | 2009-11-17 | 2009-12-30 | Danisco | Method |
| GB201007668D0 (en) | 2010-05-07 | 2010-06-23 | Danisco | Method |
| PH12021552871A1 (en) * | 2011-12-27 | 2022-09-28 | Commw Scient Ind Res Org | Processes for producing lipids |
| JP5926801B2 (ja) * | 2012-07-17 | 2016-05-25 | 国立大学法人福島大学 | プラスマローゲンの加水分解方法、プラスマローゲンの測定方法 |
| US20170121741A1 (en) | 2014-04-01 | 2017-05-04 | Dupont Nutrition Biosciences Aps | Method for increasing crude palm oil yields |
| KR101994252B1 (ko) * | 2016-06-30 | 2019-06-28 | 명지대학교 산학협력단 | 베타 아가레이즈의 생산능을 갖는 재조합 바실러스 서브틸리스 균주 및 이의 용도 |
| CN110592100B (zh) * | 2019-10-08 | 2022-08-02 | 海南大学 | 一种木薯camta基因及其抑制表达载体的构建和抗病应用 |
| CN119899821B (zh) * | 2024-07-01 | 2025-10-17 | 华南理工大学 | 一种紫红链霉菌磷脂酶a2突变体及其应用 |
Family Cites Families (251)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AT110768B (de) | 1927-09-29 | 1928-10-10 | Patiag Patentverwertungs Und I | Windkraftmaschine. |
| US2888385A (en) * | 1952-11-28 | 1959-05-26 | Grandel Felix | Process of making a preparation containing lipases and oxidases |
| US3260606A (en) * | 1964-04-29 | 1966-07-12 | Taiyo Food Co Ltd | Enzymatic treatment of egg |
| GB1092775A (en) * | 1965-07-07 | 1967-11-29 | Knud Aunstrup | Preparation of amyloglucosidase |
| US3368903A (en) | 1966-02-18 | 1968-02-13 | Vanderbilt Co R T | Baked goods dough and method |
| CH461935A (fr) * | 1966-05-03 | 1968-08-31 | Menzi Robert | Procédé de fabrication de pâtes alimentaires séchées |
| DE1900959A1 (de) * | 1969-01-09 | 1970-08-27 | Unilever Nv | Verfahren zur Herstellung von Pflanzenphosphatiden mit universeller Emulgierkraft |
| US3634195A (en) * | 1969-09-08 | 1972-01-11 | Miles Lab | Production of lipase |
| NL154598B (nl) | 1970-11-10 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van laagmoleculire verbindingen en van eiwitten die deze verbindingen specifiek kunnen binden, alsmede testverpakking. |
| US3817837A (en) | 1971-05-14 | 1974-06-18 | Syva Corp | Enzyme amplification assay |
| GB1375783A (enExample) | 1972-02-04 | 1974-11-27 | ||
| GB1442418A (en) | 1972-12-14 | 1976-07-14 | Procter & Gamble | Method of cleansing polyester-containing fabrics |
| IL46862A (en) | 1974-04-08 | 1977-12-30 | Baxter Travenol Lab | Lipolytic enzyme flavoring system for fat-containing food |
| US3939350A (en) | 1974-04-29 | 1976-02-17 | Board Of Trustees Of The Leland Stanford Junior University | Fluorescent immunoassay employing total reflection for activation |
| US3973042A (en) | 1974-05-10 | 1976-08-03 | Cornell Research Foundation, Inc. | Flavor development by microbial lipases in pasteurized milk blue cheese |
| US3996345A (en) | 1974-08-12 | 1976-12-07 | Syva Company | Fluorescence quenching with immunological pairs in immunoassays |
| GB1525929A (en) * | 1974-11-25 | 1978-09-27 | Unilever Ltd | Stabilised emulsions comprising phospholipoprotein |
| GB1577933A (en) | 1976-02-11 | 1980-10-29 | Unilever Ltd | Fat process and composition |
| US4160848A (en) * | 1977-04-18 | 1979-07-10 | Pennwalt Corporation | Antistaling agent for bakery products |
| JPS6049477B2 (ja) | 1977-04-19 | 1985-11-01 | 協和醗酵工業株式会社 | グリセロ−ル酸化酵素およびその製造法ならびにグリセロ−ル酸化酵素を用いるグリセロ−ルの定量法 |
| US4275149A (en) | 1978-11-24 | 1981-06-23 | Syva Company | Macromolecular environment control in specific receptor assays |
| US4277437A (en) | 1978-04-05 | 1981-07-07 | Syva Company | Kit for carrying out chemically induced fluorescence immunoassay |
| JPS5850719B2 (ja) | 1978-10-18 | 1983-11-11 | 協和醗酵工業株式会社 | トリグリセライドの定量方法 |
| US4399218A (en) | 1980-02-05 | 1983-08-16 | Boehringer Mannheim Gmbh | Method and reagent for the determination of glycerin |
| US4366241A (en) | 1980-08-07 | 1982-12-28 | Syva Company | Concentrating zone method in heterogeneous immunoassays |
| JPS58500638A (ja) | 1981-05-07 | 1983-04-28 | ユニリ−バ− ナ−ムロ−ゼ ベンノ−トシヤ−プ | エステルの合成法 |
| JPS6030488B2 (ja) * | 1982-11-10 | 1985-07-17 | 協和醗酵工業株式会社 | 生地の改良剤およびそれを含有してなる生地 |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| DK289083A (da) | 1983-06-23 | 1984-12-24 | Novo Industri As | Lipase, fremgangsmaade til fremstilling deraf og anvendelse deraf |
| DK402583D0 (da) * | 1983-09-05 | 1983-09-05 | Novo Industri As | Fremgangsmade til fremstilling af et immobiliseret lipasepraeparat og anvendelse deraf |
| DK152763C (da) | 1983-09-05 | 1988-10-24 | Novo Industri As | Fremgangsmaade til fremstilling af et immobiliseret lipasepraeparat |
| US4707364A (en) | 1984-01-27 | 1987-11-17 | Miles Laboratories, Inc. | Composition for accelerating cheese aging |
| US4636468A (en) | 1984-06-25 | 1987-01-13 | Genencor, Inc. | Lipolytic enzyme derived from a aspergillus microorganism having an accelerating effect on cheese flavor development |
| CA1262654A (en) | 1984-08-10 | 1989-11-07 | Takaoki Torigoe | Food quality improving agent |
| NL8402979A (nl) * | 1984-09-28 | 1986-04-16 | Tno | Werkwijze voor het bestrijden van vaatverwelkingsziekten bij gewassen, in het bijzonder de iepeziekte. |
| JPS61181390A (ja) | 1985-02-06 | 1986-08-14 | Amano Pharmaceut Co Ltd | 酵素によるグリセライドの製造法 |
| US4689297A (en) | 1985-03-05 | 1987-08-25 | Miles Laboratories, Inc. | Dust free particulate enzyme formulation |
| EP0195311B2 (en) | 1985-03-06 | 1996-01-17 | Yoshikawa Oil & Fat Co., Ltd. | Process for preparing fatty acid esters |
| US5219733A (en) * | 1985-03-06 | 1993-06-15 | Yoshikawa Oil & Fat Co., Ltd. | Process for preparing fatty acid esters |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| JPS61242542A (ja) | 1985-04-22 | 1986-10-28 | Fuji Oil Co Ltd | チ−ズ風味材の製造法 |
| US5310679A (en) * | 1985-05-13 | 1994-05-10 | Artiss Joseph D | Composition for reducing turbidity in samples of biological fluids |
| GB8514708D0 (en) | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
| GB8514707D0 (en) | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
| DK154572C (da) | 1985-08-07 | 1989-04-24 | Novo Industri As | Enzymatisk detergentadditiv, detergent og fremgangsmaade til vask af tekstiler |
| GB8525012D0 (en) * | 1985-10-10 | 1985-11-13 | Cpc International Inc | Carbohydrate refining process |
| GB2185990B (en) | 1986-02-05 | 1990-01-24 | Unilever Plc | Margarine fat |
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| US5536661A (en) * | 1987-03-10 | 1996-07-16 | Novo Nordisk A/S | Process for the production of protein products in aspergillus |
| US5766912A (en) | 1986-03-17 | 1998-06-16 | Novo Nordisk A/S | Humicola lipase produced in aspergillus |
| US5874558A (en) * | 1986-03-17 | 1999-02-23 | Novo Nordisk | Nucleic acid encoding a recombinant humicola sp. lipase |
| JPS62262997A (ja) * | 1986-05-02 | 1987-11-16 | ノボ ノルディスク アクティーゼルスカブ | ワツクスの製造方法 |
| JPS6344892A (ja) | 1986-08-13 | 1988-02-25 | Kao Corp | 油脂類のエステル交換反応方法 |
| DK157560C (da) | 1986-08-29 | 1990-06-11 | Novo Nordisk As | Enzymatisk detergentadditiv, detergent indeholdende det enzymatiske detergentadditiv og fremgangsmaade til vask af tekstiler. |
| ES2058119T3 (es) * | 1986-08-29 | 1994-11-01 | Novo Nordisk As | Aditivo detergente enzimatico. |
| EP0260573A3 (de) | 1986-09-18 | 1989-03-22 | Lucas Meyer GmbH & Co | Verfahren zur Herstellung eines hydrolysierten Lecithins, sowie Anwendung des hydrolysierten Lecithins |
| US5273898A (en) | 1986-10-17 | 1993-12-28 | Noro Nordisk A/S | Thermally stable and positionally non-specific lipase isolated from Candida |
| US5108457A (en) | 1986-11-19 | 1992-04-28 | The Clorox Company | Enzymatic peracid bleaching system with modified enzyme |
| KR900003014B1 (ko) * | 1986-12-27 | 1990-05-04 | 도오아 야꾸힌 고오교오 가부시끼가이샤 | 양식어(養殖魚)용 사료 첨가제 |
| US5219744A (en) * | 1987-08-26 | 1993-06-15 | Ajinomoto Co., Inc. | Process for modifying fats and oils |
| ES2076939T3 (es) | 1987-08-28 | 1995-11-16 | Novo Nordisk As | Lipasa recombinante de humicola y procedimiento para la produccion de lipasas recombinantes de humicola. |
| EP0321811B2 (en) | 1987-12-21 | 1999-12-22 | Dsm N.V. | Method for improving flour dough |
| DK6488D0 (da) | 1988-01-07 | 1988-01-07 | Novo Industri As | Enzymer |
| DK77788A (da) * | 1988-02-16 | 1989-08-17 | Novo Industri As | Fremgangsmaade til fremstilling af kokosnoedolie |
| JP3079276B2 (ja) * | 1988-02-28 | 2000-08-21 | 天野製薬株式会社 | 組換え体dna、それを含むシュードモナス属菌及びそれを用いたリパーゼの製造法 |
| EP0334462B2 (en) | 1988-03-25 | 2002-04-24 | Genencor International, Inc. | Molecular cloning and expression of genes encoding lipolytic enzymes |
| US5232846A (en) | 1988-08-09 | 1993-08-03 | Unitika Ltd. | Method for producing a thermostable lipoprotein lipase from streptomyces |
| GB8906837D0 (en) | 1989-03-23 | 1989-05-10 | Unilever Plc | Bread improvers |
| DE3920561A1 (de) * | 1989-06-23 | 1991-01-10 | Knoll Ag | Verfahren zur vermeidung von verdauungsstoerungen bei pflanzenfressenden tieren |
| US5213968A (en) * | 1989-08-21 | 1993-05-25 | Nestec S.A. | Process for preparing emulsifying agents |
| DE69004782T2 (de) | 1989-09-29 | 1994-03-17 | Unilever Nv | Getrocknetes Lyso-Phospholipoprotein enthaltendes Nahrungsmittel. |
| US5677160A (en) | 1989-10-30 | 1997-10-14 | Henkel Corporation | Fat splitting process |
| US5288619A (en) * | 1989-12-18 | 1994-02-22 | Kraft General Foods, Inc. | Enzymatic method for preparing transesterified oils |
| JPH03262492A (ja) | 1990-03-06 | 1991-11-22 | P Macneil Gerald | モノグリセリドの製造方法 |
| DK19991D0 (da) * | 1991-02-06 | 1991-02-06 | Novo Nordisk As | Proteinpraeparationer |
| KR100225087B1 (ko) | 1990-03-23 | 1999-10-15 | 한스 발터라벤 | 피타아제의 식물내 발현 |
| JP3110452B2 (ja) | 1990-05-09 | 2000-11-20 | ノボ ノルディスク アクティーゼルスカブ | エンドグルカナーゼ酵素を含んでなるセルラーゼ調製物 |
| US5814501A (en) | 1990-06-04 | 1998-09-29 | Genencor International, Inc. | Process for making dust-free enzyme-containing particles from an enzyme-containing fermentation broth |
| EP0468731A1 (en) | 1990-07-26 | 1992-01-29 | Oriental Yeast Co., Ltd. | Bread improver and method of producing bread |
| US5869438A (en) * | 1990-09-13 | 1999-02-09 | Novo Nordisk A/S | Lipase variants |
| CA2092615A1 (en) | 1990-09-13 | 1992-03-14 | Allan Svendsen | Lipase variants |
| US5892013A (en) * | 1990-09-13 | 1999-04-06 | Novo Nordisk A/S | Lipase variants |
| CA2058056C (en) | 1990-12-21 | 1996-11-05 | Chiaki Saito | Method of decreasing cholesterol concentration in food |
| PH31068A (en) | 1991-03-07 | 1998-02-05 | Ici Plc | Process for the production of terephthalic acid. |
| DE4112440C1 (enExample) | 1991-04-16 | 1992-10-22 | Diagen Institut Fuer Molekularbiologische Diagnostik Gmbh, 4000 Duesseldorf, De | |
| EP0585285B1 (en) * | 1991-05-01 | 1998-08-12 | Novo Nordisk A/S | Stabilized enzymes |
| DE4115938A1 (de) | 1991-05-16 | 1992-11-19 | Metallgesellschaft Ag | Enzymatisches verfahren zur verminderung des gehaltes an phosphorhaltigen bestandteilen in pflanzlichen und tierischen oelen |
| CA2077020A1 (en) | 1991-09-03 | 1993-03-04 | Yoshikazu Isono | Process for producing lipoprotein-containing substance having reduced lipid content and food containing substance thus produced |
| US5879920A (en) * | 1991-10-07 | 1999-03-09 | Genencor International, Inc. | Coated enzyme-containing granule |
| ATE133196T1 (de) | 1991-11-11 | 1996-02-15 | Akzo Nobel Nv | Verfahren zur herstellung von salzgranulaten |
| EP0558112A1 (en) | 1992-02-25 | 1993-09-01 | Unilever N.V. | Enzymic diglyceride removal |
| CA2079839A1 (en) | 1992-02-28 | 1993-08-29 | Vincent Destefanis | Calcium peroxide and ascorbic acid containing compositions as replacements for bromate in breadmaking |
| GB2267033B (en) | 1992-03-07 | 1996-01-24 | David Garnett | Lysophospholipid Animal Feed Supplement |
| DK42092D0 (enExample) | 1992-03-27 | 1992-03-27 | Novo Nordisk As | |
| DK73592D0 (da) * | 1992-06-03 | 1992-06-03 | Novo Nordisk As | Nyt enzym |
| ATE222599T1 (de) * | 1992-06-16 | 2002-09-15 | Sankyo Co | Phospholipase a1, verfahren zu seiner herstellung und anwendung |
| DK88892D0 (da) * | 1992-07-06 | 1992-07-06 | Novo Nordisk As | Forbindelse |
| EP0580252A2 (en) | 1992-07-20 | 1994-01-26 | Quest International B.V. | Improvements in or relating to pectin methyl esterase |
| ATE135163T1 (de) | 1992-07-27 | 1996-03-15 | Gist Brocades Nv | Enzymprodukt und verfahren zur verbesserung der qualität von brot |
| DK104592D0 (da) | 1992-08-21 | 1992-08-21 | Novo Nordisk As | Fremgangsmaade |
| JPH08504327A (ja) | 1992-12-10 | 1996-05-14 | ギスト ブロカデス ナムローゼ フェンノートシャップ | 糸状菌における異種タンパクの生産 |
| JP3507076B2 (ja) * | 1992-12-22 | 2004-03-15 | ノボザイムス アクティーゼルスカブ | アルカリリパーゼ |
| DK154292D0 (da) | 1992-12-23 | 1992-12-23 | Novo Nordisk As | Nyt enzym |
| JP2937746B2 (ja) | 1993-04-25 | 1999-08-23 | 昭和産業株式会社 | 油脂の精製方法 |
| ZA943640B (en) | 1993-06-07 | 1995-01-26 | Buckman Labor Inc | Synergistically stabilized liquid enzymatic compositions |
| JP2859520B2 (ja) | 1993-08-30 | 1999-02-17 | ノボ ノルディスク アクティーゼルスカブ | リパーゼ及びそれを生産する微生物及びリパーゼ製造方法及びリパーゼ含有洗剤組成物 |
| JP2678341B2 (ja) | 1993-09-27 | 1997-11-17 | 富士紡績株式会社 | 固定化リパーゼ |
| EP0650669B1 (en) | 1993-10-29 | 2002-01-09 | Dsm N.V. | Baking improver compositions |
| EP0652289A1 (en) | 1993-11-05 | 1995-05-10 | Unilever Plc | Random interesterification of triglyceride fats |
| DE4339556C1 (de) | 1993-11-19 | 1995-02-02 | Metallgesellschaft Ag | Verfahren zum Entschleimen von Pflanzenöl mittels Enzymen |
| EP1090553A3 (en) * | 1993-12-24 | 2001-04-18 | Dsm N.V. | Dry yeast compositions |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| US6117679A (en) | 1994-02-17 | 2000-09-12 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
| WO1995022606A1 (en) | 1994-02-21 | 1995-08-24 | Novo Nordisk A/S | Method for production of an immobilized enzyme preparation and use of the immobilized enzyme preparation |
| ATE222604T1 (de) | 1994-02-22 | 2002-09-15 | Novozymes As | Methode zur herstellung einer variante eines lipolytischen enzymes |
| US5834280A (en) | 1994-05-03 | 1998-11-10 | Novo Nordisk A/S | Glucose oxidases obtained from a cladosporium |
| US5741665A (en) * | 1994-05-10 | 1998-04-21 | University Of Hawaii | Light-regulated promoters for production of heterologous proteins in filamentous fungi |
| DE69501228T2 (de) | 1994-05-11 | 1998-05-07 | Amano Pharma Co Ltd | Ascorbatoxidase, dafür kodierendes Gen, Verfahren zu ihrer Herstellung und dieselbe verwendende Reagens-Zusammensetzung |
| WO1995034222A1 (fr) | 1994-06-16 | 1995-12-21 | Firmenich S.A. | Procede d'aromatisation et composition aromatisante |
| DE69519331D1 (de) | 1994-06-17 | 2000-12-14 | Dsm Nv | Zusammensetzung zur Brotverbesserung |
| CN1167503A (zh) | 1994-10-26 | 1997-12-10 | 诺沃挪第克公司 | 一种具有脂解活性的酶 |
| EP0784675A1 (en) * | 1994-10-26 | 1997-07-23 | Novo Nordisk A/S | Enzymatic detergent composition |
| ES2181792T3 (es) | 1994-10-26 | 2003-03-01 | Novozymes As | Nueva enzima lipolitica. |
| GB2296011B (en) | 1994-12-13 | 1999-06-16 | Solvay | Novel fusarium isolate and lipases, cutinases and enzyme compositions derived therefrom |
| US6093562A (en) * | 1996-02-05 | 2000-07-25 | Novo Nordisk A/S | Amylase variants |
| JP3394975B2 (ja) | 1995-02-22 | 2003-04-07 | セレスター ユーエスエー インク | 動物性脂肪からステロールおよび遊離脂肪酸を削減する方法 |
| JPH08228778A (ja) | 1995-02-27 | 1996-09-10 | Showa Denko Kk | 新規なリパーゼ遺伝子及びそれを用いたリパーゼの製造方法 |
| JP3359777B2 (ja) * | 1995-03-06 | 2002-12-24 | 日清製粉株式会社 | 油揚げ即席麺およびその製造方法 |
| AU5002096A (en) | 1995-03-30 | 1996-10-16 | Novo Nordisk A/S | Alkaline lipolytic enzyme |
| US5919746A (en) * | 1995-03-30 | 1999-07-06 | Novo Nordisk A/S | Alkaline lipolytic enzyme |
| US5989599A (en) | 1995-04-24 | 1999-11-23 | Nestec S.A. | Process for the interesterification of phospholipids |
| EP0743017B1 (en) | 1995-05-15 | 2004-09-29 | DSM IP Assets B.V. | Application of phospholipases in animal feed |
| GB2301103B (en) | 1995-05-23 | 1999-12-22 | Danisco | An enzyme system comprising ferulic acid esterase |
| PL184045B1 (pl) * | 1995-06-07 | 2002-08-30 | Danisco | Sposób polepszania reologicznych właściwości ciasta z mąki oraz jakości wytworzonego z ciasta wyrobu gotowego |
| US6936289B2 (en) | 1995-06-07 | 2005-08-30 | Danisco A/S | Method of improving the properties of a flour dough, a flour dough improving composition and improved food products |
| GB0112226D0 (en) | 2001-05-18 | 2001-07-11 | Danisco | Method of improving dough and bread quality |
| US6495357B1 (en) | 1995-07-14 | 2002-12-17 | Novozyme A/S | Lipolytic enzymes |
| CN1193346A (zh) | 1995-07-14 | 1998-09-16 | 诺沃挪第克公司 | 一种具有脂解活性的修饰酶 |
| DE19527274A1 (de) | 1995-07-26 | 1997-01-30 | Metallgesellschaft Ag | Enzymatisches Verfahren zur Entschleimung von pflanzlichen Ölen mit Aspergillus-Phospholipase |
| CN1192780B (zh) | 1995-08-11 | 2010-08-04 | 诺沃奇梅兹有限公司 | 新的脂解酶 |
| JP4053595B2 (ja) | 1995-09-22 | 2008-02-27 | メディカル・リサーチ・カウンシル | 核酸の突然変異誘発におけるまたはそれに関する改良 |
| EP0776604B1 (en) | 1995-12-01 | 2002-01-23 | Unilever N.V. | Microwavable crispy bread-rolls |
| US6344328B1 (en) | 1995-12-07 | 2002-02-05 | Diversa Corporation | Method for screening for enzyme activity |
| US6361974B1 (en) | 1995-12-07 | 2002-03-26 | Diversa Corporation | Exonuclease-mediated nucleic acid reassembly in directed evolution |
| US5756328A (en) * | 1995-12-20 | 1998-05-26 | Cornell Research Foundation, Inc. | Acyltransferase and cDNA encoding acyltransferase |
| US5942430A (en) | 1996-02-16 | 1999-08-24 | Diversa Corporation | Esterases |
| US6001586A (en) | 1996-03-29 | 1999-12-14 | Genencor International, Inc. | Compartmentalization method for screening microorganisms |
| ATE279512T1 (de) | 1996-04-25 | 2004-10-15 | Novozymes As | Alkalisches, lipolytisches enzym |
| DE19620649A1 (de) | 1996-05-22 | 1997-11-27 | Roehm Gmbh | Rekombinant hergestellte Lysophospholipase aus Aspergillus |
| JPH10155493A (ja) | 1996-10-04 | 1998-06-16 | Sankyo Co Ltd | アスペルギルス属由来のホスホリパーゼa1をコードする遺伝子 |
| JP3182381B2 (ja) | 1996-10-25 | 2001-07-03 | 日清製粉株式会社 | 麺類の機械製麺法 |
| DE19648343C1 (de) * | 1996-11-22 | 1998-02-12 | Roehm Gmbh | Verfahren zur Herstellung von Backwaren mit verbesserter Frischhaltung |
| JP3582265B2 (ja) | 1996-11-28 | 2004-10-27 | 味の素株式会社 | 改質穀粉及びこれを使用した穀粉加工食品 |
| CN1148442C (zh) | 1996-12-09 | 2004-05-05 | 诺维信公司 | 利用来自具有磷脂酶a和/或b活性的丝状真菌的磷脂酶降低含有大量非水合磷的食用油中的含磷成分 |
| US6103505A (en) | 1996-12-09 | 2000-08-15 | Novo Nordisk A/S | Method for reducing phosphorus content of edible oils |
| DE19701348A1 (de) | 1997-01-16 | 1998-07-23 | Roehm Gmbh | Protein mit Phospholipaseaktivität |
| US5821102A (en) | 1997-01-21 | 1998-10-13 | Novo Nordisk Biotech Inc. | Nucleic acids encoding polyeptides having absidia lipase activity |
| DK0977869T4 (da) | 1997-04-09 | 2009-01-19 | Danisco | Lipase og brug af samme til forbedring af dej og bageriprodukter |
| EP0882797B1 (en) | 1997-06-04 | 2003-07-16 | Loders Croklaan B.V. | Preparation of symmetrical triglycerides aba |
| RU2140751C1 (ru) | 1997-06-11 | 1999-11-10 | Ассоциация "Ассоя" | Пищевая добавка для производства хлеба и хлебобулочных изделий |
| JP4121186B2 (ja) | 1997-06-16 | 2008-07-23 | 株式会社日立製作所 | セラミックス管の検査方法及びその装置 |
| EP0913468A3 (en) | 1997-07-22 | 2001-06-13 | Dsm N.V. | Bread improving comüposition |
| EP0897667B2 (en) | 1997-07-31 | 2008-11-12 | DSM IP Assets B.V. | Bread improving composition |
| US6355282B1 (en) | 1997-10-31 | 2002-03-12 | Amano Pharmaceutical Co., Ltd. | Dough composition and preparation thereof |
| AU1556699A (en) | 1997-12-23 | 1999-07-19 | Novo Nordisk A/S | A process for immobilisation of enzymes |
| US6156548A (en) * | 1997-12-23 | 2000-12-05 | Novo Nordisk A/S | Immobilization of enzymes with a fluidized bed for use in an organic medium |
| AU3247699A (en) | 1998-02-17 | 1999-09-06 | Novo Nordisk A/S | Lipase variant |
| US5955310A (en) | 1998-02-26 | 1999-09-21 | Novo Nordisk Biotech, Inc. | Methods for producing a polypeptide in a bacillus cell |
| US6815190B1 (en) | 1998-04-12 | 2004-11-09 | Novozymes A/S | Cutinase variants |
| WO1999053769A1 (en) | 1998-04-20 | 1999-10-28 | Novo Nordisk A/S | Preparation of dough and baked products |
| US6365204B1 (en) * | 1998-04-20 | 2002-04-02 | Novozymes | Preparation of dough and baked products |
| US6866837B2 (en) * | 1998-06-05 | 2005-03-15 | Mallinckrodt Inc. | Radiolabeled peptides for the diagnosis and treatment of breast and prostate tumors and metastases of such tumors |
| US20030074695A1 (en) * | 1998-06-24 | 2003-04-17 | Farese Robert V. | Plant diacylglycerol O-acyltransferase and uses thereof |
| WO2000001713A2 (en) * | 1998-07-02 | 2000-01-13 | Calgene Llc | Diacylglycerol acyl transferase proteins |
| SE510497C2 (sv) | 1998-07-15 | 1999-05-31 | Biofeed Thailand Co Ltd | Funktionellt födoämne innehållande mikroorganismer |
| ES2188190T5 (es) | 1998-07-21 | 2007-11-16 | Danisco A/S | Producto alimentario. |
| JP3414652B2 (ja) | 1998-10-12 | 2003-06-09 | 敷島製パン株式会社 | 小麦粉焼成品、その製造方法および品質改良剤 |
| DK1131444T3 (da) * | 1998-11-10 | 2006-08-07 | Novozymes Inc | Polypeptider med lysophospholipase aktivitet og nucleinsyre som koder for disse |
| US7312062B2 (en) * | 1998-11-27 | 2007-12-25 | Novozymes A/S | Lipolytic enzyme variants |
| RU2235775C2 (ru) | 1998-11-27 | 2004-09-10 | Новозимс А/С | Способ получения варианта липолитического фермента и липолитический фермент (варианты) |
| NZ511340A (en) | 1998-11-27 | 2003-07-25 | Novozymes As | Lipolytic enzyme variants |
| JP2000226335A (ja) | 1998-12-04 | 2000-08-15 | Amano Pharmaceut Co Ltd | 経口用酵素製剤、酵素含有食材及び酵素製剤の服用方法 |
| BRPI9915832B1 (pt) | 1998-12-04 | 2016-09-13 | Novozymes As | "variante de uma cutinase de cepa dsm 1800 de humicola insolens precursora, sequência de dna, vetor, célula hospedeira microbiana transformada, processos para produzir uma variante, para hidrólise enzimática de um oligômero cíclico de poli(etileno tereftalato), para tingir pano ou fio de poliéster, para melhorar o acabamento funcional de um fio ou pano contendo pet, e, composilão detergente". |
| US6399121B1 (en) | 1999-03-16 | 2002-06-04 | Novozymes A/S | Process for producing cheese |
| JP4271872B2 (ja) | 1999-03-16 | 2009-06-03 | ノボザイムス アクティーゼルスカブ | チーズの製造方法 |
| AU4039400A (en) | 1999-03-26 | 2000-10-16 | Diversa Corporation | Exonuclease-mediated nucleic acid reassembly in directed evolution |
| ATE416252T1 (de) | 1999-06-02 | 2008-12-15 | Novozymes As | Chemisch veränderte, lipolytische enzyme |
| EP1057415A1 (en) | 1999-06-04 | 2000-12-06 | Societe Des Produits Nestle S.A. | Lipase-treated pasta and manufacturing process |
| US6254645B1 (en) * | 1999-08-20 | 2001-07-03 | Genencor International, Inc. | Enzymatic modification of the surface of a polyester fiber or article |
| US6337187B1 (en) | 1999-11-05 | 2002-01-08 | Millennium Pharmaceuticals, Inc. | 18891, a novel human lipase |
| AU783277B2 (en) * | 1999-10-14 | 2005-10-06 | Novozymes A/S | Lysophospholipase from aspergillus |
| US6146869A (en) | 1999-10-21 | 2000-11-14 | Novo Nordisk Biotech, Inc. | Polypeptides having phospholipase B activity and nucleic acids encoding same |
| DE19953854C2 (de) | 1999-11-09 | 2002-01-17 | Max Planck Gesellschaft | Verfahren zur Herstellung von Biopolymeren mit veränderten Eigenschaften |
| GB2358784B (en) | 1999-12-03 | 2004-06-30 | Danisco | Method of improving dough and bread quality |
| EP1233676A1 (en) | 1999-12-03 | 2002-08-28 | Danisco A/S | Method of improving dough and bread quality |
| US7078205B2 (en) * | 2000-02-17 | 2006-07-18 | Millennium Pharmaceuticals, Inc. | Nucleic acid sequences encoding melanoma associated antigen molecules, aminotransferase molecules, atpase molecules, acyltransferase molecules, pyridoxal-phosphate dependent enzyme molecules and uses therefor |
| DE10119972A1 (de) | 2000-04-15 | 2002-05-23 | Nikolaus Weber | Enzymatisches Verfahren zur Herstellung von Fettsäuresterylestern aus Dämpferdestillaten der Fettraffination und Tallöl |
| US20020192792A1 (en) | 2000-04-28 | 2002-12-19 | Palle Schneider | Laccase mutants |
| US6509182B2 (en) * | 2000-06-26 | 2003-01-21 | Novozymes A/S | Lipolytic enzymes |
| US6432898B1 (en) * | 2000-10-31 | 2002-08-13 | Novozymes Biotech, Inc. | Polypeptides having lipase activity and nucleic acids encoding same |
| US6511837B2 (en) * | 2000-06-26 | 2003-01-28 | Novozymes A/S | Lipolytic enzymes |
| US6558715B1 (en) * | 2000-10-31 | 2003-05-06 | Novozymes Biotech, Inc. | Methods for using lipases in baking |
| US6506588B2 (en) * | 2000-06-26 | 2003-01-14 | Novozymes, A/S | Lipolytic enzymes |
| WO2002002762A1 (en) | 2000-07-03 | 2002-01-10 | Mochida Pharmaceutical Co., Ltd. | Novel lipase |
| EP1301080B1 (en) * | 2000-07-06 | 2011-09-14 | Novozymes A/S | Method of preparing a dough, or a baked product made from a dough, with addition of lipolytic enzymes |
| EP1307548A2 (en) | 2000-07-13 | 2003-05-07 | Maxygen, Inc. | Novel lipase genes |
| EP1309677B2 (en) | 2000-08-11 | 2012-04-11 | Genencor International, Inc. | Bacillus transformation, transformants and mutant libraries |
| US7241463B2 (en) | 2000-09-25 | 2007-07-10 | Novozymes A/S | Methods for processing crustacean material |
| US6660491B2 (en) * | 2000-11-24 | 2003-12-09 | Ikeda Food Research Co., Ltd. | Process for producing dietary sterol fatty acid esters |
| MXPA03007393A (es) | 2001-02-21 | 2004-03-16 | Novozymes As | Produccion de productos alimenticios almidonosos. |
| US6645749B2 (en) * | 2001-05-25 | 2003-11-11 | Novozymes A/S | Lipolytic enzyme |
| US7630836B2 (en) | 2001-05-30 | 2009-12-08 | The Kitasato Institute | Polynucleotides |
| DE50115482D1 (de) | 2001-07-11 | 2010-06-24 | Cognis Ip Man Gmbh | Lipase/Acyltransferase aus Candida parapsilosis |
| ATE342374T1 (de) | 2001-08-22 | 2006-11-15 | Haerting Thomas Francis | Verfahren zur herstellung von sterol- und stanolestern mittels enzymatischer transesterifikation in lösungsmittel- und wasserfreien medien |
| AU2003215527A1 (en) * | 2002-04-10 | 2003-10-27 | Novozymes A/S | Bacillus licheniformis mutant host cell |
| US7226771B2 (en) * | 2002-04-19 | 2007-06-05 | Diversa Corporation | Phospholipases, nucleic acids encoding them and methods for making and using them |
| SE0201581D0 (sv) * | 2002-05-29 | 2002-05-29 | Scandinavian Biotechnology Res | New improved acyltransferase |
| WO2003102118A2 (en) * | 2002-05-30 | 2003-12-11 | Council Of Scientific And Industrial Research | Process for the pre-treatment of vegetable oils for physical refining |
| CA2490944C (en) | 2002-07-03 | 2012-05-15 | Novozymes A/S | Treatment of dough with a lipoxygenase and a lipolytic enzyme |
| DK2338986T3 (en) | 2002-08-19 | 2015-01-19 | Dsm Ip Assets Bv | Novel lipases and uses thereof |
| CA2403025A1 (en) | 2002-10-08 | 2004-04-08 | Cognis Deutschland Gmbh & Co. Kg | Enzymes with lipase/acyltransferase activity |
| GB2379165A (en) | 2002-10-22 | 2003-03-05 | Dsm Nv | Animal feed |
| JP4300839B2 (ja) | 2002-11-14 | 2009-07-22 | セイコーエプソン株式会社 | 画像処理装置、画像処理方法および画像処理プログラム |
| US20060035800A1 (en) | 2002-12-11 | 2006-02-16 | Novozymes A/S | Detergent composition |
| WO2004053152A1 (en) | 2002-12-12 | 2004-06-24 | Novozymes A/S | Method of selecting a lipolytic enzyme |
| JP2006511725A (ja) | 2002-12-23 | 2006-04-06 | ノボザイムス ノース アメリカ,インコーポレイティド | ポリエステル布の処理方法 |
| BR122016015076B1 (pt) | 2003-01-17 | 2017-05-16 | Dupont Nutrition Biosci Aps | método de produção de um éster de carboidrato e uso de uma enzima lipídio aciltransferase para produzir um éster de carboidrato |
| MXPA05007654A (es) * | 2003-01-17 | 2005-09-30 | Danisco | Metodo. |
| US7955814B2 (en) * | 2003-01-17 | 2011-06-07 | Danisco A/S | Method |
| BRPI0409599B1 (pt) | 2003-04-28 | 2014-09-16 | Novozymes As | Sequência de ácido nucléico, construto de ácido nucléico, vetor de expressão recombinante, micro-organismo recombinante, composição de massa, métodos de produzir uma fosfolipase, de preparar uma massa ou um produto assado feito da massa, processos para reduzir o conteúdo de fósforo em um óleo vegetal e para produzir queijo |
| US20060251763A1 (en) | 2003-06-19 | 2006-11-09 | Patkar Shamkant A | Phospholipase variants |
| WO2005005977A2 (en) | 2003-06-30 | 2005-01-20 | Applera Corporation | Fluorescent phospholipase assays and compositions |
| BRPI0412401A (pt) | 2003-07-07 | 2006-09-05 | Genencor Int | polipeptìdeos da amilase exoespecìficos, ácidos nucléicos que codificam tais polipeptìdeos e usos dos mesmos |
| JP4327536B2 (ja) | 2003-09-01 | 2009-09-09 | レシップ株式会社 | 券硬貨投入口及びそれを備えた券硬貨分離装置 |
| WO2005056782A2 (en) | 2003-12-03 | 2005-06-23 | Genencor International, Inc. | Perhydrolase |
| KR101169265B1 (ko) | 2003-12-24 | 2012-08-02 | 대니스코 에이/에스 | 단백질 |
| US7718408B2 (en) * | 2003-12-24 | 2010-05-18 | Danisco A/S | Method |
| US7906307B2 (en) | 2003-12-24 | 2011-03-15 | Danisco A/S | Variant lipid acyltransferases and methods of making |
| NZ547082A (en) * | 2003-12-24 | 2009-07-31 | Danisco | Enzymatic treatment of oils |
| EP2284184A3 (en) | 2004-01-09 | 2011-05-18 | Novozymes, Inc. | Bacillus YvmA inactivation |
| JP2007524744A (ja) | 2004-02-24 | 2007-08-30 | ノボザイムス アクティーゼルスカブ | 液状洗剤中の酵素の安定化 |
| GB0405637D0 (en) | 2004-03-12 | 2004-04-21 | Danisco | Protein |
| AU2005223969B2 (en) | 2004-03-24 | 2010-08-05 | Novozymes A/S | Process for producing cheese |
| CA2562171A1 (en) | 2004-04-08 | 2005-11-24 | Genencor International, Inc. | Mutant .alpha.-amylases |
| WO2006008508A1 (en) * | 2004-07-16 | 2006-01-26 | Danisco A/S | Enzymatic oil-degumming method |
| DE102004040134A1 (de) | 2004-08-19 | 2006-02-23 | Henkel Kgaa | Neue essentielle Gene von Bacillus licheniformis und darauf aufbauende verbesserte biotechnologische Produktionsverfahren |
| US7811979B2 (en) | 2004-09-21 | 2010-10-12 | Novozymes A/S | Subtilases |
| CN101084307B (zh) * | 2004-09-30 | 2011-06-01 | 诺维信股份有限公司 | 具有脂肪酶活性的多肽和编码其的多核苷酸 |
| DE102005039836A1 (de) | 2005-08-23 | 2007-03-01 | Cognis Ip Management Gmbh | Sterolesterpulver |
| EP1788080A1 (en) | 2005-11-22 | 2007-05-23 | Süd-Chemie Ag | Use of a thermostable phospholipase in the degumming of an oil or fat, and a method for obtaining a thermostable phopholipase |
| CN101200754B (zh) | 2007-12-07 | 2010-06-02 | 中国农业科学院油料作物研究所 | 无溶剂系统中固定化全细胞酶催化生产植物甾醇酯的方法 |
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2007
- 2007-01-25 PL PL11184428T patent/PL2405007T3/pl unknown
- 2007-01-25 CN CN200780050429XA patent/CN101652474B/zh not_active Expired - Fee Related
- 2007-01-25 MX MX2009008021A patent/MX2009008021A/es active IP Right Grant
- 2007-01-25 JP JP2009546822A patent/JP5124593B2/ja not_active Expired - Fee Related
- 2007-01-25 AU AU2007344910A patent/AU2007344910B2/en not_active Ceased
- 2007-01-25 DK DK11184428.8T patent/DK2405007T5/da active
- 2007-01-25 WO PCT/IB2007/000558 patent/WO2008090395A1/en not_active Ceased
- 2007-01-25 BR BRPI0720801-4A patent/BRPI0720801A2/pt not_active IP Right Cessation
- 2007-01-25 EP EP07705681A patent/EP2109670A1/en not_active Withdrawn
- 2007-01-25 EP EP11184428.8A patent/EP2405007B1/en active Active
- 2007-01-25 CA CA2673954A patent/CA2673954C/en not_active Expired - Fee Related
-
2009
- 2009-07-20 US US12/505,935 patent/US7960150B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| EP2109670A1 (en) | 2009-10-21 |
| PL2405007T3 (pl) | 2014-04-30 |
| US7960150B2 (en) | 2011-06-14 |
| EP2405007A1 (en) | 2012-01-11 |
| CN101652474A (zh) | 2010-02-17 |
| AU2007344910A1 (en) | 2008-07-31 |
| DK2405007T5 (da) | 2014-06-23 |
| WO2008090395A1 (en) | 2008-07-31 |
| CN101652474B (zh) | 2012-06-27 |
| EP2405007B1 (en) | 2013-12-04 |
| AU2007344910B2 (en) | 2013-03-28 |
| CA2673954A1 (en) | 2008-07-31 |
| CA2673954C (en) | 2015-09-15 |
| JP5124593B2 (ja) | 2013-01-23 |
| DK2405007T3 (en) | 2014-02-24 |
| JP2010516271A (ja) | 2010-05-20 |
| MX2009008021A (es) | 2009-08-07 |
| US20100081169A1 (en) | 2010-04-01 |
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