ES2585280T3 - Asparaginasa de basidiomicetos - Google Patents
Asparaginasa de basidiomicetos Download PDFInfo
- Publication number
- ES2585280T3 ES2585280T3 ES11712561.7T ES11712561T ES2585280T3 ES 2585280 T3 ES2585280 T3 ES 2585280T3 ES 11712561 T ES11712561 T ES 11712561T ES 2585280 T3 ES2585280 T3 ES 2585280T3
- Authority
- ES
- Spain
- Prior art keywords
- asparaginase
- basidiomycete
- enzyme
- temperature
- kh2po4
- Prior art date
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- 108010024976 Asparaginase Proteins 0.000 title abstract description 6
- 102000015790 Asparaginase Human genes 0.000 title abstract 2
- 229960003272 asparaginase Drugs 0.000 title description 4
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 title description 4
- 241000221198 Basidiomycota Species 0.000 title 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 1
- 108090000790 Enzymes Proteins 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 7
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
- 238000000034 method Methods 0.000 description 6
- 239000007836 KH2PO4 Substances 0.000 description 5
- 229960001230 asparagine Drugs 0.000 description 5
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 5
- 235000019796 monopotassium phosphate Nutrition 0.000 description 5
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 102100025573 1-alkyl-2-acetylglycerophosphocholine esterase Human genes 0.000 description 4
- 240000006499 Flammulina velutipes Species 0.000 description 4
- 235000016640 Flammulina velutipes Nutrition 0.000 description 4
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 4
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 229920001817 Agar Polymers 0.000 description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 235000009582 asparagine Nutrition 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 3
- 229910000396 dipotassium phosphate Inorganic materials 0.000 description 3
- 235000019797 dipotassium phosphate Nutrition 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 235000013619 trace mineral Nutrition 0.000 description 3
- 239000011573 trace mineral Substances 0.000 description 3
- 229930182816 L-glutamine Natural products 0.000 description 2
- 235000010419 agar Nutrition 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 238000001212 derivatisation Methods 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 2
- 235000019341 magnesium sulphate Nutrition 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 241000206672 Gelidium Species 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010068370 Glutens Proteins 0.000 description 1
- 229910021578 Iron(III) chloride Inorganic materials 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- ARUVKPQLZAKDPS-UHFFFAOYSA-L copper(II) sulfate Chemical compound [Cu+2].[O-][S+2]([O-])([O-])[O-] ARUVKPQLZAKDPS-UHFFFAOYSA-L 0.000 description 1
- 229910000366 copper(II) sulfate Inorganic materials 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 229960001031 glucose Drugs 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 235000021312 gluten Nutrition 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- RBTARNINKXHZNM-UHFFFAOYSA-K iron trichloride Chemical compound Cl[Fe](Cl)Cl RBTARNINKXHZNM-UHFFFAOYSA-K 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229910000357 manganese(II) sulfate Inorganic materials 0.000 description 1
- SQQMAOCOWKFBNP-UHFFFAOYSA-L manganese(II) sulfate Chemical compound [Mn+2].[O-]S([O-])(=O)=O SQQMAOCOWKFBNP-UHFFFAOYSA-L 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 229910021654 trace metal Inorganic materials 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 229910000368 zinc sulfate Inorganic materials 0.000 description 1
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
- 239000011686 zinc sulphate Substances 0.000 description 1
- 235000009529 zinc sulphate Nutrition 0.000 description 1
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)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
- C12N9/82—Asparaginase (3.5.1.1)
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K10/00—Animal feeding-stuffs
- A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
- A23L5/25—Removal of unwanted matter, e.g. deodorisation or detoxification using enzymes
-
- 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
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Microbiology (AREA)
- Polymers & Plastics (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Food Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Physiology (AREA)
- Nutrition Science (AREA)
- Animal Husbandry (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- General Preparation And Processing Of Foods (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Fodder In General (AREA)
- Feed For Specific Animals (AREA)
- Seeds, Soups, And Other Foods (AREA)
Abstract
Una enzima asparaginasa, con la secuencia de aminoácidos: MKSFALFVPL IVAAVVNSAV VTFSTGLGCN SVSQTYRGNG NFCADPPGDW SSVGFSEIGG DNRVTVHNQN SCTPASQVGQ GFGPACWNQG ATKLRSAWVA CPGQRLAENG TIVDDDGAFI DFA.
Description
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como diana, a una aparato secretor del huésped (véase, a dicho efecto, Mountain, A., 1989, Bacillus, C. Harwood, ed., Plenum Press, New York, 73 -114). Los protocolos estándar, mediante la utilización de las técnicas las cuales se han descrito anteriormente, arriba, son técnicas conocidas en el arte de la técnica especializada, y éstas se utilizaron para las sobreexpresión de asparaginasa recombinante, mediante Bacillus subtilis.
Ejemplo 1 – Cultivo de Flammulina velutipes
La totalidad de los medios y del equipamiento, se sometieron a tratamiento de autoclave, previamente a su uso, y se aplicaron durante la totalidad del procedimiento. Se procedió a mantener el Flammulina velutipes, en placas de agar estándar (30,0 g L-1 de glucosa monohidratada; 4,5 g L-1 de asparagina monihidratada; 1,5 g de L-1 KH2PO4; 0,5 g de L-1 MgSO4; 3,0 g L-1 de extracto de levadura; 15,0 g L-1 de agar agar; 1,0 ml L-1 de una solución de trazas de metales (oligoelmentos), la cual contenía 0,005 g L-1 de CuSO4 -5H2O, 0,08 g L-1 de FeCl3 · 6H2O, 0,09 g L-1 de ZnSO4 · 7H2O, 0,03 g L-1 de MnSO4 · H2O y 0,4 g L-1 de EDTA. El pH del medio, se ajustó a un valor de 1, con 1 M NaOH, previamente a la esterilización.
Se procedió a preparar los precultivos, mediante la homogeneización de un tampón de agar de 10 x 10 mm, más micelio de Flammulina velutipes, en 100 ml de una solución de una de nutrición, estándar, mediante la utilización de un instrumento del tipo Ultra Turrax (Miccra D-9, Art, Mullheim, Alemania). Los cultivos sumergidos, se mantuvieron a una temperatura de 24 °C, y a 150 r. p. m. (revoluciones por minutos). Después de un cultivo, durante un transcurso de tiempo de 5 días, se procedió a transferir 50 ml de precultivo, al interior de 250 del medio de cultivo principal, consistente en medio mínimo (1,5 g L-1 de KH2PO4; 0,5 g L-1 de MgSO4; 1,0 ml L-1 de solución de elementos de trazas – oligoelementos) y 40 g L-1 de gluten ó 10 mM de glutamina, respectivamente.
Ejemplo 2 – Preparación de las enzimas, a partir de Flammulina velutipes
Después de 18 días de cultivo, se procedió a filtrar el cultivo, y el sobrenadante que contenía la enzima extracelular (200 ml), se sometió a espumado inverso [1], siendo, la asparaginasa y otra proteína, las únicas proteínas restantes en el sobrenadante. Se procedió, a continuación, a concentrar el líquido restante, mediante la utilización de un proceso de autofiltración (MWCO – corte de peso molecular -10.000)(MWCO, de sus iniciales en idioma inglés, correspondientes a Molecular wigth cut – off), y ambas proteínas, se separaron, vía cromatografía de exclusión de tamaño, en una Superosa 6.
La mayor parte de la actividad hidrolítica originalmente presente, se recuperó, indicando ello el hecho consistente en que, este protocolo, proporcionaba un concentrado de enzimas de utilidad, únicamente mediante dos etapas.
Ejemplo 3 – Hidrólisis de la L-asparaginasa, mediante la utilización de una enzima nativa
Se procedió precalentar 100 µl de 10 mM asparagina, en un tampón 0,1 M de K2HPO4 / KH2PO4 (pH 7,0), a una temperatura de 37 °C, durante un transcurso de tiempo 5 minutos. La reacción, se inició mediante la adición de 50 µl de solución enzimática. Después de un tiempo de incubación de 20 minutos, a una temperatura de 37 °C, y de una velocidad angular correspondiente a 400 r. p. m. (revoluciones por minuto), en el agitador térmico, se procedió a parar el ensayo, mediante la adición de 20 µl de TCA (ácido trifluoroacético). A continuación, se procedió a llevar a cabo un experimento de control, sin substrato. Se procedió a medir, de una forma cuantitativa, los contenidos de ácido aspártico, mediante procedimiento de HPLC, después de una derivatización con OPA, y se utilizó la diferencia entre la muestra y el control, para calcular entonces la actividad de la enzima.
La evidencia analítica, indicaba una hidrólisis enzimática del substrato L-asparagina.
Ejemplo 4 – Hidrólisis de la L-glutamina, mediante la utilización de una enzima nativa
Se procedió precalentar 100 µl de 10 mM glutamina, en un tampón 0,1 M de K2HPO4 / KH2PO4 (pH 7,0), a una temperatura de 37 °C, durante un transcurso de tiempo 5 minutos. La reacción, se inició mediante la adición de 50 µl de solución enzimática. Después de un tiempo de incubación de 20 minutos, a una temperatura de 37 °C, y de una velocidad angular correspondiente a 400 r. p. m. (revoluciones por minuto), en el agitador térmico, se procedió a parar el ensayo, mediante la adición de 20 µl de TCA. A continuación, se procedió a llevar a cabo un experimento de control, sin substrato. Se procedió a medir, de una forma cuantitativa, los contenidos de ácido glutámico, mediante procedimiento de HPLC, después de una derivatización con OPA, y se utilizó la diferencia entre la muestra y el control, para calcular entonces la actividad de la enzima.
Esta evidencia analítica, indicaba una actividad secundaria de la asparaginasa, hacia el substrato L-glutamina.
Ejemplo 5 – Hidrólisis de la L-asparagina, mediante la utilización de una enzima recombinante
Se procedió precalentar 140 µl de 10 mM asparagina, en un tampón 0,1 M de K2HPO4 / KH2PO4 (pH 7,0), a una temperatura de 37 °C, durante un transcurso de tiempo 5 minutos. La reacción, se inició mediante la adición de 50 µl de solución de enzima recombinante, diluida, a un valor de 200 veces, con agua. Después de un tiempo de
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Claims (1)
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imagen1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP10169405 | 2010-07-14 | ||
| EP10169405 | 2010-07-14 | ||
| PCT/EP2011/055375 WO2012007192A1 (en) | 2010-07-14 | 2011-04-06 | Asparaginase from basidiomycetes |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2585280T3 true ES2585280T3 (es) | 2016-10-04 |
Family
ID=44275917
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES11712561.7T Active ES2585280T3 (es) | 2010-07-14 | 2011-04-06 | Asparaginasa de basidiomicetos |
Country Status (18)
| Country | Link |
|---|---|
| US (2) | US20130209608A1 (es) |
| EP (1) | EP2593473B1 (es) |
| JP (1) | JP2013539358A (es) |
| CN (1) | CN103003297B (es) |
| AU (1) | AU2011278657B2 (es) |
| BR (1) | BR112013000768A2 (es) |
| CA (1) | CA2802126A1 (es) |
| CL (1) | CL2012003490A1 (es) |
| DK (1) | DK2593473T3 (es) |
| ES (1) | ES2585280T3 (es) |
| IL (1) | IL223085A (es) |
| MX (1) | MX340937B (es) |
| NZ (1) | NZ603773A (es) |
| PL (1) | PL2593473T3 (es) |
| RU (1) | RU2560597C2 (es) |
| UA (1) | UA113391C2 (es) |
| WO (1) | WO2012007192A1 (es) |
| ZA (1) | ZA201301160B (es) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9427008B2 (en) | 2012-09-06 | 2016-08-30 | Mycotechnology, Inc. | Method of myceliation of agricultural substates for producing functional foods and nutraceuticals |
| US9068171B2 (en) | 2012-09-06 | 2015-06-30 | Mycotechnology, Inc. | Method for myceliating coffee |
| WO2015033344A1 (en) | 2013-09-05 | 2015-03-12 | Yissum Research Development Company Of The Hebrew University Of Jerusalem Ltd. | Methods and kits for inhibiting pathogenicity of group a streptococcus (gas) or group g streptococcus (ggs) |
| US10231469B2 (en) | 2014-03-15 | 2019-03-19 | Mycotechnology, Inc. | Myceliated products and methods for making myceliated products from cacao and other agricultural substrates |
| US10709157B2 (en) | 2014-08-26 | 2020-07-14 | Mycotechnology, Inc. | Methods for the production and use of mycelial liquid tissue culture |
| CN113519814B (zh) | 2014-08-26 | 2024-04-02 | 麦可科技有限公司 | 含菌丝液体组织培养物上清与食品的组合物及其用途 |
| US9572364B2 (en) | 2014-08-26 | 2017-02-21 | Mycotechnology, Inc. | Methods for the production and use of mycelial liquid tissue culture |
| US10980257B2 (en) | 2015-02-26 | 2021-04-20 | Myco Technology, Inc. | Methods for lowering gluten content using fungal cultures |
| BR112018070148A2 (pt) | 2016-04-14 | 2019-05-07 | Mycotechnology Inc | métodos para a produção e uso de composições alimentícias de alto teor proteico miceliadas |
| US11166477B2 (en) | 2016-04-14 | 2021-11-09 | Mycotechnology, Inc. | Myceliated vegetable protein and food compositions comprising same |
| US10806101B2 (en) | 2016-04-14 | 2020-10-20 | Mycotechnology, Inc. | Methods for the production and use of myceliated high protein food compositions |
| CN109750069A (zh) * | 2017-11-01 | 2019-05-14 | 北京中科伊品生物科技有限公司 | 生产l-赖氨酸的重组菌、其构建方法以及l-赖氨酸的生产方法 |
| WO2020061502A1 (en) | 2018-09-20 | 2020-03-26 | The Better Meat Company | Enhanced aerobic fermentation methods for producing edible fungal mycelium blended meats and meat analogue compositions |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5638192B2 (es) * | 1973-01-26 | 1981-09-04 | ||
| JPS6212720A (ja) * | 1985-07-10 | 1987-01-21 | Yasahiro Morita | アロエ霊芝の製造法 |
| JPS6360915A (ja) * | 1986-09-01 | 1988-03-17 | Masao Nashiro | 脱毛防止兼育毛剤 |
| JP3819540B2 (ja) * | 1996-06-07 | 2006-09-13 | 株式会社林原生物化学研究所 | Ｌ−アスパラギナーゼ活性を有する哺乳類由来のポリペプチド |
| RU2221868C2 (ru) * | 2001-08-22 | 2004-01-20 | Эльдаров Михаил Анатольевич | Ген l-аспарагиназы erwinia carotovora и штамм escherichia coli вкпм № в-8174 - продуцент l-аспарагиназы erwinia carotovora |
| US7037540B2 (en) | 2002-09-19 | 2006-05-02 | Frito-Lay North America, Inc. | Method for reducing acrylamide formation in thermally processed foods |
| JP2004283062A (ja) * | 2003-03-20 | 2004-10-14 | Riken Vitamin Co Ltd | 加熱調理された加工食品 |
| EP1910526A2 (en) * | 2005-07-13 | 2008-04-16 | Botanica Bioscience Corporation | Methods for the administration of fv and related compositions |
| ES2519466T3 (es) * | 2007-03-09 | 2014-11-07 | Novozymes A/S | Asparaginasas termoestables |
| EA018424B1 (ru) * | 2007-04-20 | 2013-07-30 | ДСМ АйПи АССЕТС Б.В. | Варианты фермента аспарагиназы и их применение |
| WO2008128975A1 (en) * | 2007-04-20 | 2008-10-30 | Dsm Ip Assets B.V. | Novel asparaginases and uses thereof |
-
2011
- 2011-04-06 MX MX2012014701A patent/MX340937B/es active IP Right Grant
- 2011-04-06 WO PCT/EP2011/055375 patent/WO2012007192A1/en active Application Filing
- 2011-04-06 PL PL11712561.7T patent/PL2593473T3/pl unknown
- 2011-04-06 DK DK11712561.7T patent/DK2593473T3/en active
- 2011-04-06 BR BR112013000768A patent/BR112013000768A2/pt not_active IP Right Cessation
- 2011-04-06 RU RU2013106310/10A patent/RU2560597C2/ru not_active IP Right Cessation
- 2011-04-06 US US13/810,134 patent/US20130209608A1/en not_active Abandoned
- 2011-04-06 AU AU2011278657A patent/AU2011278657B2/en not_active Ceased
- 2011-04-06 ES ES11712561.7T patent/ES2585280T3/es active Active
- 2011-04-06 EP EP11712561.7A patent/EP2593473B1/en not_active Not-in-force
- 2011-04-06 JP JP2013518993A patent/JP2013539358A/ja active Pending
- 2011-04-06 CA CA2802126A patent/CA2802126A1/en not_active Abandoned
- 2011-04-06 NZ NZ603773A patent/NZ603773A/en not_active IP Right Cessation
- 2011-04-06 CN CN201180034717.2A patent/CN103003297B/zh not_active Expired - Fee Related
- 2011-06-04 UA UAA201301816A patent/UA113391C2/uk unknown
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2012
- 2012-11-15 IL IL223085A patent/IL223085A/en not_active IP Right Cessation
- 2012-12-10 CL CL2012003490A patent/CL2012003490A1/es unknown
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2013
- 2013-02-13 ZA ZA2013/01160A patent/ZA201301160B/en unknown
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2014
- 2014-09-04 US US14/477,448 patent/US9410138B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| RU2013106310A (ru) | 2014-08-20 |
| AU2011278657A1 (en) | 2012-12-06 |
| CN103003297A (zh) | 2013-03-27 |
| IL223085A (en) | 2016-09-29 |
| IL223085A0 (en) | 2013-02-03 |
| CN103003297B (zh) | 2016-06-01 |
| EP2593473A1 (en) | 2013-05-22 |
| UA113391C2 (uk) | 2017-01-25 |
| ZA201301160B (en) | 2014-07-30 |
| CL2012003490A1 (es) | 2014-02-14 |
| US20150093472A1 (en) | 2015-04-02 |
| MX340937B (es) | 2016-08-01 |
| US9410138B2 (en) | 2016-08-09 |
| MX2012014701A (es) | 2013-01-28 |
| BR112013000768A2 (pt) | 2016-05-24 |
| CA2802126A1 (en) | 2012-01-19 |
| DK2593473T3 (en) | 2016-08-01 |
| JP2013539358A (ja) | 2013-10-24 |
| WO2012007192A1 (en) | 2012-01-19 |
| NZ603773A (en) | 2014-05-30 |
| US20130209608A1 (en) | 2013-08-15 |
| PL2593473T3 (pl) | 2016-11-30 |
| RU2560597C2 (ru) | 2015-08-20 |
| AU2011278657B2 (en) | 2015-05-14 |
| EP2593473B1 (en) | 2016-05-25 |
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