DK3077517T3 - Isstrukturerende protein - Google Patents
Isstrukturerende protein Download PDFInfo
- Publication number
- DK3077517T3 DK3077517T3 DK14843223.0T DK14843223T DK3077517T3 DK 3077517 T3 DK3077517 T3 DK 3077517T3 DK 14843223 T DK14843223 T DK 14843223T DK 3077517 T3 DK3077517 T3 DK 3077517T3
- Authority
- DK
- Denmark
- Prior art keywords
- sequence
- host cell
- isp
- nucleic acid
- filamentous fungal
- Prior art date
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- 239000004299 sodium benzoate Substances 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
- C07K14/39—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi from yeasts
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
- A23G9/00—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor
- A23G9/32—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds
- A23G9/38—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds containing peptides or proteins
-
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Mycology (AREA)
- Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Inorganic Chemistry (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Claims (15)
1. Trådformet svampeværtscelle, der omfatter en nukleinsyrekonstruktion eller en ekspressionsvektor, der omfatter en nukleinsyrekonstruktion, hvor den trådformede svampeværtscelle er af slægten Aspergillus, og hvor nukleinsyrekonstruktionen omfatter: en nukleinsyresekvens, der koder for et isstrukturerende protein (ISP), der omfatter sekvensen ifølge SEQ ID NO: 1 eller en sekvens, der er mindst 80 % identisk dermed, eller omfatter sekvensen ifølge aminosyrene 21 til 261 af SEQ ID NO: 1 eller en sekvens, der er mindst 80 % identisk dermed; og koblet operabelt dertil kontrolsekvenser, der åbner mulighed for ekspression af nukleinsyresekvensen i en trådformet svampeværtscelle af slægten Aspergillus.
2. Trådformet svampeværtscelle ifølge krav 1, hvor nukleinsyresekvensen koder for et ISP, der omfatter sekvensen ifølge SEQ ID NO: 1 eller en sekvens, der er mindst 85 %, mindst 90 %, mindst 95 %, mindst 98 % eller mindst 99 % identisk dermed, eller omfatter sekvensen ifølge aminosyrerne 21 til 261 af SEQ ID NO: 1 eller en sekvens, der er mindst 85 %, mindst 90 %, mindst 95 %, mindst 98 % eller mindst 99 % identisk dermed.
3. Trådformet svampeværtscelle ifølge krav 1 eller 2, hvor nukleinsyren koder for et ISP, der har en aminosyresekvens, der kan opnås fra en arktisk gær af slægten Leucosporidium.
4. Trådformet svampeværtscelle ifølge et hvilket som helst af ovennævnte krav, hvor kontrolsekvenserne omfatter en promotor, der ikke nativt er forbundet med nukleinsyren, der koder for et ISP.
5. Trådformet svampeværtscelle ifølge et hvilket som helst af ovennævnte krav, hvor nukleinsyren er kodonparoptimeret til ekspression i den trådformede svampeværtscelle.
6. Trådformet svampeværtscelle ifølge et hvilket som helst af ovennævnte krav, hvor den trådformede svampeværtscelle er en Aspergillus niger eller Aspergillus oryzae.
7. Fremgangsmåde til fremstilling af et isstrukturerende protein (ISP), hvilken fremgangsmåde omfatter: - tilvejebringelse af en trådformet svampeværtscelle af slægten Aspergillus ifølge et hvilket som helst af ovennævnte krav; dyrkning af den trådformede svampeværtscelle under betingelser, der er egnet til fremstilling af det isstrukturerende protein; og eventuelt - indvinding af det isstrukturerende protein.
8. Fremgangsmåde ifølge krav 7, hvor den trådformede svampeværtscelle er en trådformet svampeværtscelle ifølge krav 6.
9. Fremgangsmåde ifølge krav 7 til 8, hvor ISP'et secerneres fra værtscellen.
10. Fremgangsmåde ifølge et hvilket som helst af kravene 7 til 9, hvor ISP'et fremstilles i en mængde på mindst 1 g/1.
11. Isstrukturerende protein, der omfatter sekvensen ifølge SEQ ID NO: 1 eller en sekvens, der er mindst 80 % identisk dermed, eller omfatter sekvensen ifølge aminosyrerne 21 til 261 af SEQ ID NO: 1 eller en sekvens, der er mindst 80 % identisk dermed, hvor: mindst én aminosyre er en modificeret aminosyre, og hvor den modificerede aminosyre er en pyroglutamat, der er til stede i aminoterminalen.
12. Fødevaresammensætning, der omfatter det isstrukturerende protein ifølge krav 11.
13. Fremgangsmåde til fremstilling af et fødevareprodukt, hvilken fremgangsmåde omfatter kombinering af det isstrukturerende protein ifølge krav 11 med en eller flere fødevarebestanddele.
14. Anvendelse af det isstrukturerende protein ifølge krav 11 i en fødevaresammensætning.
15. Fødevaresammensætning ifølge krav 12, fremgangsmåde ifølge krav 13 eller anvendelse ifølge krav 14, hvor fødevaresammensætningen er et frosset konfektureprodukt, såsom en iscreme eller en sorbet.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP13195351 | 2013-12-02 | ||
| PCT/EP2014/076291 WO2015082488A1 (en) | 2013-12-02 | 2014-12-02 | Ice structuring protein |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DK3077517T3 true DK3077517T3 (da) | 2019-02-11 |
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK14843223.0T DK3077517T3 (da) | 2013-12-02 | 2014-12-02 | Isstrukturerende protein |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US10487125B2 (da) |
| EP (1) | EP3077517B1 (da) |
| CN (1) | CN105992822A (da) |
| DK (1) | DK3077517T3 (da) |
| ES (1) | ES2706742T3 (da) |
| MX (1) | MX370305B (da) |
| WO (1) | WO2015082488A1 (da) |
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| US10487252B2 (en) * | 2018-01-24 | 2019-11-26 | Microtek Laboratories, Inc. | Water based thermal cooling gels comprising a viscosity modifier and ice nucleating protein |
| CN110428865B (zh) * | 2019-08-14 | 2021-08-20 | 信阳师范学院 | 一种高通量预测抗冻蛋白质的方法 |
| CN113388009B (zh) * | 2021-05-18 | 2022-07-19 | 中国科学院福建物质结构研究所 | 一种标签蛋白及其编码基因、重组载体与应用 |
| CN113444159A (zh) * | 2021-06-18 | 2021-09-28 | 南京纽田科技有限公司 | 能表达冰冻蛋白的黑曲霉发酵菌种 |
| WO2024041839A1 (en) | 2022-08-23 | 2024-02-29 | Unilever Ip Holdings B.V. | Improvements in or relating to digestion of proteins |
Family Cites Families (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| CA1341226C (en) | 1988-08-16 | 2001-05-01 | Wim Van Hartingsveldt | Gene replacement as a tool for the construction of aspergillus strains |
| US5118792A (en) | 1989-05-10 | 1992-06-02 | Dna Plant Technology Corporation | Ice crystal growth suppression polypeptides and method of making |
| CA2056434A1 (en) | 1989-05-10 | 1990-11-11 | Gareth J. Warren | Antifreeze polypeptides |
| EP0635574B1 (en) | 1993-07-23 | 2003-04-23 | Dsm N.V. | Selection marker gene free recombinant strains, a method for obtaining them and the use of these strains |
| AU2705895A (en) | 1994-06-30 | 1996-01-25 | Novo Nordisk Biotech, Inc. | Non-toxic, non-toxigenic, non-pathogenic fusarium expression system and promoters and terminators for use therein |
| DK0836646T3 (da) | 1995-07-05 | 2005-12-19 | Unilever Nv | Anti-frysepeptider fra havfisk som additiver til födevareprodukter |
| ATE418614T1 (de) | 1995-08-03 | 2009-01-15 | Dsm Ip Assets Bv | Amds-gen aus aspergillus niger für eine acetamidase kodierend |
| DK0979294T3 (da) | 1997-04-11 | 2015-08-31 | Dsm Ip Assets Bv | Genkonversion som et redskab til konstruktion af rekombinante industrielle filamentøse svampe |
| PL341760A1 (en) | 1997-12-22 | 2001-05-07 | Dsm Nv | Expression cloning in mildew fungi |
| EP2278016B1 (en) | 1999-03-22 | 2012-09-26 | Novozymes Inc. | Promoter sequences derived from Fusarium Venenatum and uses thereof |
| AU7288100A (en) | 1999-09-17 | 2001-04-24 | Dsm N.V. | Regulation of secondary metabolite production |
| CA2513833A1 (en) | 2003-02-05 | 2004-08-19 | Dsm Ip Assets B.V. | Use of oxalate deficient aspergillus niger strains for producing a polypeptide |
| BRPI0400822A (pt) * | 2003-12-10 | 2005-08-23 | Unilever Nv | Produto de confeitaria e unidade de varejo |
| DE602005023427D1 (de) | 2004-04-02 | 2010-10-21 | Dsm Ip Assets Bv | Filamentöse pilzmutanten mit verbesserter homologer rekombinationseffizienz |
| WO2005100573A2 (en) | 2004-04-16 | 2005-10-27 | Dsm Ip Assets B.V. | Fungal promoters for expressing a gene in a fungal cell |
| WO2005123763A1 (en) | 2004-06-16 | 2005-12-29 | Dsm Ip Assets B.V. | Production of polypeptides by improved secretion |
| WO2006040312A2 (en) | 2004-10-12 | 2006-04-20 | Dsm Ip Assets B.V. | Fungal transcriptional activators useful in methods for producing a polypeptide |
| AU2005293516B2 (en) | 2004-10-15 | 2011-01-06 | Dsm Ip Assets B.V. | Homologous amdS genes as selectable marker |
| US7888489B2 (en) | 2005-01-24 | 2011-02-15 | Dsm Ip Assets B.V. | Method for producing a compound of interest in a filamentous fungal cell |
| US20080227148A1 (en) | 2005-03-01 | 2008-09-18 | Thibaut Jose Wenzel | Aspergillus Promotors for Expressing a Gene in a Fungal Cell |
| JP2009509970A (ja) * | 2005-09-22 | 2009-03-12 | プロサイ インコーポレイテッド | 酵母突然変異体において産生されるグリコシル化ポリペプチドおよびその使用方法 |
| EP1954812B1 (en) | 2005-11-29 | 2012-11-21 | DSM IP Assets B.V. | Dna binding site of a transcriptional activator useful in gene expression |
| JP5250850B2 (ja) | 2006-06-29 | 2013-07-31 | ディーエスエム アイピー アセッツ ビー．ブイ． | 改善されたポリペプチド発現を達成する方法 |
| CN101784666A (zh) | 2007-02-15 | 2010-07-21 | 帝斯曼知识产权资产管理有限公司 | 用于生产感兴趣的化合物的重组宿主细胞 |
| KR101700711B1 (ko) | 2007-11-21 | 2017-01-31 | 로스킬드 유니베르시테트 | 얼음-결합 활성을 포함하는 폴리펩티드 |
| EP2406386B1 (en) | 2009-03-10 | 2019-01-23 | DSM IP Assets B.V. | Method for improving the yield of a polypeptide |
| US20120041171A1 (en) | 2009-04-22 | 2012-02-16 | Dsm Ip Assets B.V. | Process for the production of a recombinant polypeptide of interest |
| KR101048721B1 (ko) | 2009-06-22 | 2011-07-14 | 한국해양연구원 | 루코스포리디움 속 미생물의 결빙방지 단백질 유전자, 그를 포함하는 재조합 벡터 및 그 유전자로 암호화된 단백질 |
| CA2768608A1 (en) | 2009-07-22 | 2011-01-27 | Dsm Ip Assets B.V. | Improved host cell for the production of a compound of interest |
| US9273320B2 (en) * | 2009-08-07 | 2016-03-01 | Novozymes A/S | Method of producing a sweet protein |
| US8945898B2 (en) | 2010-07-01 | 2015-02-03 | Dsm Ip Assets B.V. | Recombinant host cell with deficiency in non-ribosomal peptide synthase production |
| KR101300177B1 (ko) | 2011-05-13 | 2013-08-26 | 한국해양과학기술원 | 극지 효모 유래 결빙방지단백질의 대량 생산방법 |
| EP2731452B1 (en) * | 2011-07-11 | 2015-08-12 | Unilever PLC | Frozen confection with gel coating |
| WO2013135729A1 (en) | 2012-03-12 | 2013-09-19 | Dsm Ip Assets B.V. | Recombination system |
| US9745563B2 (en) | 2012-07-19 | 2017-08-29 | Dsm Ip Assets B.V. | Amylase-deficient strain |
| EP2875119B1 (en) | 2012-07-19 | 2017-12-20 | DSM IP Assets B.V. | Agse-deficient strain |
-
2014
- 2014-12-02 EP EP14843223.0A patent/EP3077517B1/en not_active Not-in-force
- 2014-12-02 CN CN201480065622.0A patent/CN105992822A/zh not_active Withdrawn
- 2014-12-02 DK DK14843223.0T patent/DK3077517T3/da active
- 2014-12-02 MX MX2016007109A patent/MX370305B/es active IP Right Grant
- 2014-12-02 US US15/039,110 patent/US10487125B2/en not_active Expired - Fee Related
- 2014-12-02 WO PCT/EP2014/076291 patent/WO2015082488A1/en active Application Filing
- 2014-12-02 ES ES14843223T patent/ES2706742T3/es active Active
Also Published As
| Publication number | Publication date |
|---|---|
| EP3077517B1 (en) | 2018-10-17 |
| EP3077517A1 (en) | 2016-10-12 |
| MX2016007109A (es) | 2016-09-08 |
| CN105992822A (zh) | 2016-10-05 |
| MX370305B (es) | 2019-12-09 |
| ES2706742T3 (es) | 2019-04-01 |
| WO2015082488A1 (en) | 2015-06-11 |
| US10487125B2 (en) | 2019-11-26 |
| US20170029476A1 (en) | 2017-02-02 |
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