HU204097B - Process for producing cloning system relating to kluyveromyces species - Google Patents
Process for producing cloning system relating to kluyveromyces species Download PDFInfo
- Publication number
- HU204097B HU204097B HU832272A HU227283A HU204097B HU 204097 B HU204097 B HU 204097B HU 832272 A HU832272 A HU 832272A HU 227283 A HU227283 A HU 227283A HU 204097 B HU204097 B HU 204097B
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- Hungary
- Prior art keywords
- plasmid
- kluyveromyces
- transformed
- dna
- lac4
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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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
- C07K14/43—Sweetening agents, e.g. thaumatin, monellin
-
- 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
- C12N15/67—General methods for enhancing the expression
- C12N15/68—Stabilisation of the vector
-
- 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
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
- C12N15/815—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts for yeasts other than Saccharomyces
-
- 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
- C12N15/87—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation
- C12N15/90—Stable introduction of foreign DNA into chromosome
-
- 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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/036—Fusion polypeptide containing a localisation/targetting motif targeting to the medium outside of the cell, e.g. type III secretion
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Mycology (AREA)
- Physics & Mathematics (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Botany (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pyrane Compounds (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8202091 | 1982-05-19 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| HU204097B true HU204097B (en) | 1991-11-28 |
Family
ID=19839766
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| HU832272A HU204097B (en) | 1982-05-19 | 1983-05-19 | Process for producing cloning system relating to kluyveromyces species |
Country Status (20)
Families Citing this family (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS58146281A (ja) * | 1981-10-19 | 1983-08-31 | Suntory Ltd | 酵母細胞の形質転換法 |
| US4943529A (en) | 1982-05-19 | 1990-07-24 | Gist-Brocades Nv | Kluyveromyces as a host strain |
| ATE49421T1 (de) * | 1982-05-19 | 1990-01-15 | Gist Brocades Nv | Klonierungssystem fuer kluyveromyce spezies. |
| JPH0716432B2 (ja) * | 1982-10-20 | 1995-03-01 | サントリー株式会社 | 酵母の高発現ベクタープラスミドを用いたペプチドの生産方法 |
| US4876197A (en) * | 1983-02-22 | 1989-10-24 | Chiron Corporation | Eukaryotic regulatable transcription |
| CA1341302C (en) * | 1983-02-22 | 2001-10-09 | Rae Lyn Burke | Yeast expression systems with vectors having gapdh or pyk promoters and synthesis of foreign protein |
| JPS60501290A (ja) * | 1983-05-19 | 1985-08-15 | ユニリ−バ− ナ−ムロ−ゼ ベンノ−トシヤ−プ | 酵母細胞に新しく導入した遺伝子の発現改良 |
| JPS61501186A (ja) * | 1983-10-11 | 1986-06-19 | インターナシヨナル ジネテイツク エンジニアリング インコーポレイテツド | タウマチン（Ｔｈａｕｍａｔｉｎ）遺伝子の作製と発現 |
| US5422267A (en) * | 1984-05-22 | 1995-06-06 | Robert R. Yocum | Industrial yeast comprising an integrated glucoamylase gene |
| US6214577B1 (en) | 1984-05-22 | 2001-04-10 | Robert Rogers Yocum | Yeast vectors conferring antibiotic resistance |
| IL75210A0 (en) * | 1984-05-22 | 1985-09-29 | Bioteknika International | Yeast vector |
| US5240838A (en) * | 1984-07-27 | 1993-08-31 | Internationale Otrool Maatschappij "Octropa" B.V. | Regulatory sequences of alcohol oxidase (MOX) and dihydroxyacetonesynthase (DAS) of Hansenula polymorpha |
| US5741672A (en) * | 1984-07-27 | 1998-04-21 | Unilever Patent Holdings B.V. | Expression and production of polypeptides using the promoters of the hansenula polymorpha MOX and DAS genes |
| US4879231A (en) * | 1984-10-30 | 1989-11-07 | Phillips Petroleum Company | Transformation of yeasts of the genus pichia |
| US4855231A (en) * | 1984-10-30 | 1989-08-08 | Phillips Petroleum Company | Regulatory region for heterologous gene expression in yeast |
| US4837148A (en) * | 1984-10-30 | 1989-06-06 | Phillips Petroleum Company | Autonomous replication sequences for yeast strains of the genus pichia |
| US5047340A (en) * | 1985-06-05 | 1991-09-10 | The University Of Kentucky Research Foundation | LAC+ saccharomyces cerevisiae |
| CA1310923C (en) * | 1985-11-13 | 1992-12-01 | Joachim Ludwig Weickmann | Dna encoding [asp --] and [lys -, asp --] thaumatin i |
| IT1203758B (it) * | 1986-03-27 | 1989-02-23 | Univ Roma | Vettori di clonazione e di espressione di geni eterologhi in lieviti e lieviti trasformati con tali vettori |
| CA1339101C (en) * | 1986-06-03 | 1997-07-29 | Nicolaas Overbeeke | Production of guar alpha-galactosidase and immunologically related alpha-galactosidases by host organisms transformed with recombinant dna methods |
| EP0260404B1 (en) * | 1986-08-21 | 1995-05-31 | VAN DEN BERG, Robert | Amylolytic enzymes producing microorganisms constructed by recombinant DNA technology and their use for fermentation processes |
| EP0257115A1 (en) * | 1986-08-21 | 1988-03-02 | Heineken Technisch Beheer B.V. | Amylolytic enzyme producing microorganisms, constructed by recombinant DNA technology, and their use in fermentation processes |
| US5151354A (en) * | 1986-08-21 | 1992-09-29 | Cornelius Hollenberg | Fermentation processes using amylolytic enzyme producing microorganisms |
| US5882884A (en) * | 1987-06-19 | 1999-03-16 | Lucky Biotech Corporation | Expression of proteinaceous sweeteners in yeast |
| AR247761A1 (es) * | 1987-07-28 | 1995-03-31 | Gist Brocades Nv | Metodo para producir un polipeptido en una celula hospedante de kluyveromyces, dicha celula hospedante transformada y secuencia a adn empleada |
| FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
| US5221624A (en) * | 1988-11-08 | 1993-06-22 | International Genetic Engineering, Inc. | DNA encoding (Lys46, Asp97, Asp113) and (Lys46, Asp.sup.137) thaumatin I polypeptides |
| US5204252A (en) * | 1989-02-08 | 1993-04-20 | Henkel Research Corporation | Candida tropicalis transformation system |
| AU638438B2 (en) | 1989-02-24 | 1993-07-01 | Monsanto Technology Llc | Synthetic plant genes and method for preparation |
| US20010003849A1 (en) | 1989-08-07 | 2001-06-14 | Kenneth A. Barton | Expression of genes in plants |
| US5264554A (en) * | 1990-01-19 | 1993-11-23 | The Blood Center Of Southeastern Wisconsin, Inc. | Platelet cell adhesion molecule and variants thereof |
| FR2678636A1 (fr) * | 1991-07-02 | 1993-01-08 | Rhone Poulenc Rorer Sa | Procede de production de proteines recombinantes et cellules hote utilisees. |
| FR2680518A1 (fr) * | 1991-08-21 | 1993-02-26 | Rhone Poulenc Rorer Sa | Promoteur de levure et son utilisation. |
| ES2080689B1 (es) * | 1994-04-21 | 1996-09-01 | Urquima Sa | Procedimiento de obtencion de un edulcorante natural proteico. |
| US6682924B1 (en) * | 1995-05-05 | 2004-01-27 | Novozymes A/S | Protease variants and compositions |
| US5837517A (en) * | 1995-05-05 | 1998-11-17 | Novo Nordisk A/S | Protease variants and compositions |
| GB9907461D0 (en) | 1999-03-31 | 1999-05-26 | King S College London | Neurite regeneration |
| JP4531868B2 (ja) * | 1997-04-11 | 2010-08-25 | コニンクリーケ デーエスエム ナムローゼ フェンノートシャップ | １を超える非リボソームｒｎａをコードしているドメインの染色体ゲノムに組込まれた少なくとも２コピーの所望遺伝子を含む、特にクルイベロミセスによる酵母細胞 |
| US6265186B1 (en) | 1997-04-11 | 2001-07-24 | Dsm N.V. | Yeast cells comprising at least two copies of a desired gene integrated into the chromosomal genome at more than one non-ribosomal RNA encoding domain, particularly with Kluyveromyces |
| ES2154995B1 (es) * | 1998-11-20 | 2001-11-16 | Consejo Superior Investigacion | Levadura panadera recombinante capaz de asimilar lactosa. |
| US8372620B2 (en) | 1998-12-23 | 2013-02-12 | Dupont Nutrition Biosciences Aps | Bacterial xylanases |
| CN100347308C (zh) | 1999-05-21 | 2007-11-07 | 卡吉尔道有限责任公司 | 合成有机产物的方法和材料 |
| DE19943383B4 (de) | 1999-09-10 | 2006-03-16 | Tad Pharma Gmbh | Regulatorische Sequenzen und Expressionskassetten für Hefen |
| KR20030027947A (ko) * | 2000-08-10 | 2003-04-07 | 오노 야꾸힝 고교 가부시키가이샤 | 세포사를 유도하는 글리세릴알데히드-3-인산 탈수소효소프로모터 |
| GB0020498D0 (en) | 2000-08-18 | 2000-10-11 | Sterix Ltd | Compound |
| US7141410B2 (en) * | 2000-11-22 | 2006-11-28 | Natureworks Llc | Methods and materials for the production of organic products in cells of Candida species |
| CA2430270A1 (en) | 2000-11-22 | 2002-05-30 | Cargill Dow Polymers, Llc | Methods and materials for the synthesis of organic products |
| EP2175013A1 (en) | 2000-12-07 | 2010-04-14 | DSM IP Assets B.V. | Protein hydrolysates enriched in peptides having a carboxy terminal proline residue |
| EP1464234A1 (en) | 2000-12-07 | 2004-10-06 | DSM IP Assets B.V. | Method for the prevention or reduction of haze in beverages |
| GB0116453D0 (en) | 2001-07-05 | 2001-08-29 | Imp College Innovations Ltd | Method |
| EP2042196B1 (en) | 2001-10-10 | 2016-07-13 | ratiopharm GmbH | Remodelling and glycoconjugation of Granulocyte Colony Stimulating Factor (G-CSF) |
| US7517671B2 (en) | 2002-02-28 | 2009-04-14 | New England Biolabs, Inc. | Methods and compositions for concentrating secreted recombinant protein |
| WO2003104382A1 (en) | 2002-06-07 | 2003-12-18 | Dsm Ip Assets B.V. | Improved method for the prevention or reduction of haze in beverages |
| TWI328612B (en) | 2002-07-25 | 2010-08-11 | Dsm Ip Assets Bv | Genes and their encoded polypeptides involved in the biosynthetic pathway of vitamin b12, vectors and host cells comprising the genes, and process for producing vitamin b12 |
| EP1615945B1 (en) | 2003-04-09 | 2011-09-28 | BioGeneriX AG | Glycopegylation methods and proteins/peptides produced by the methods |
| GB0403864D0 (en) | 2004-02-20 | 2004-03-24 | Ucl Ventures | Modulator |
| EP3563688A1 (en) | 2005-11-28 | 2019-11-06 | DSM IP Assets B.V. | Enzyme preparations yielding a clean taste |
| GB0600406D0 (en) | 2006-01-10 | 2006-02-15 | Univ Bath | Crystal |
| AU2008219305B2 (en) | 2007-02-20 | 2013-08-22 | Dsm Ip Assets B.V. | Novel sialidase |
| WO2008113799A1 (en) | 2007-03-22 | 2008-09-25 | Dsm Ip Assets B.V. | Novel lysyl oxidases |
| WO2011101339A2 (en) | 2010-02-18 | 2011-08-25 | Dsm Ip Assets B.V. | Fermentation broth and filtration filter cake and uses thereof |
| WO2011105841A2 (ko) * | 2010-02-24 | 2011-09-01 | 중앙대학교 산학협력단 | 브라제인 발현용 재조합 발현벡터 및 높은 단맛을 가지는 신규한 브라제인 다중 변이체 |
| WO2012007445A1 (en) | 2010-07-13 | 2012-01-19 | Dsm Ip Assets B.V. | Mutarotase in crystallization |
| WO2012007446A1 (en) | 2010-07-13 | 2012-01-19 | Dsm Ip Assets B.V. | Use of a mutarotase in the production of dried powders |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4237224A (en) | 1974-11-04 | 1980-12-02 | Board Of Trustees Of The Leland Stanford Jr. University | Process for producing biologically functional molecular chimeras |
| FR2441659A1 (fr) * | 1978-11-14 | 1980-06-13 | Anvar | Nouveaux plasmides hybrides et microorganismes les contenant |
| IL63270A0 (en) * | 1980-08-05 | 1981-10-30 | Univ Leland Stanford Junior | Eukaryotic autonomously replicating segment |
| IL63035A (en) * | 1980-09-09 | 1985-05-31 | Univ California | Dnas capable of replication and stable mitotic maintenance in a host eukaryote,their preparation and eukaryotic cells comprising them |
| WO1982002091A1 (en) * | 1980-12-10 | 1982-06-24 | Instruments Inc Beckman | Entraining vaporized sample in metastable gas |
| ATE76901T1 (de) * | 1980-12-12 | 1992-06-15 | Unilever Nv | Strukturgene, die fuer die verschiedenen allelischen und reifungsformen von praeprothaumatin und deren mutanten kodieren, diese strukturgene enthaltende klonierungsvektoren und deren expression in mikrobiellen wirtzellen. |
| CA1192151A (en) * | 1980-12-12 | 1985-08-20 | Cornelis T. Verrips | Dna sequences encoding the various allelic forms of mature thaumatin, and cloning vehicles comprising said dna's and their use in transformed microorganisms |
| US4666847A (en) * | 1981-01-16 | 1987-05-19 | Collaborative Research, Inc. | Recombinant DNA means and method |
| NZ199722A (en) * | 1981-02-25 | 1985-12-13 | Genentech Inc | Dna transfer vector for expression of exogenous polypeptide in yeast;transformed yeast strain |
| JPS57146571A (en) * | 1981-03-09 | 1982-09-10 | Mitsubishi Chem Ind Ltd | Killer yeast |
| DK368882A (da) * | 1981-08-25 | 1983-02-26 | Alan John Kingsman | Expessions vektorer |
| BR8205954A (pt) | 1981-10-14 | 1983-09-13 | Unilever Nv | Sequencia de dna,plasmidio recombinante,cultura bacteriana e microorganismos |
| ATE49421T1 (de) * | 1982-05-19 | 1990-01-15 | Gist Brocades Nv | Klonierungssystem fuer kluyveromyce spezies. |
-
1983
- 1983-05-19 AT AT83200714T patent/ATE49421T1/de not_active IP Right Cessation
- 1983-05-19 HU HU832272A patent/HU204097B/hu not_active IP Right Cessation
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- 1983-05-19 ES ES522556A patent/ES8402874A1/es not_active Expired
- 1983-05-19 AU AU15539/83A patent/AU571181B2/en not_active Expired
- 1983-05-19 JP JP58501746A patent/JPS59501572A/ja active Granted
- 1983-05-19 GR GR71403A patent/GR78852B/el unknown
- 1983-05-19 PT PT76727A patent/PT76727B/pt unknown
- 1983-05-19 DE DE8383200714T patent/DE3381090D1/de not_active Expired - Lifetime
- 1983-05-19 EP EP83200714A patent/EP0096430B2/en not_active Expired - Lifetime
- 1983-05-19 CA CA000428497A patent/CA1224735A/en not_active Expired
- 1983-05-19 DE DE8383200712T patent/DE3379665D1/de not_active Expired
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- 1983-05-19 BR BR8307525A patent/BR8307525A/pt unknown
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1984
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- 1984-01-19 US US06/572,414 patent/US4859596A/en not_active Expired - Lifetime
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1986
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