ES2536878T3 - Mutantes de alfa-amilasa - Google Patents
Mutantes de alfa-amilasa Download PDFInfo
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- ES2536878T3 ES2536878T3 ES09152241.7T ES09152241T ES2536878T3 ES 2536878 T3 ES2536878 T3 ES 2536878T3 ES 09152241 T ES09152241 T ES 09152241T ES 2536878 T3 ES2536878 T3 ES 2536878T3
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- Prior art keywords
- amylase
- seq
- variant
- bacillus
- vector
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- Expired - Lifetime
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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
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
Abstract
Variante de una α-amilasa original tipo Termamyl, donde la α-amilasa original tipo Termamyl es seleccionada entre: (i) SEC ID Nº: 1, SEC ID Nº: 2, SEC ID Nº: 3, SEC ID Nº: 4, SEC ID NO: 5, SEC ID 5 Nº: 6, SEC ID Nº: 7 o SEC ID Nº: 8; o (ii) una α-amilasa original tipo Termamyl que tiene al menos el 80% de homología con una de las secuencias de (i); y donde la variante tiene actividad α-amilasa y comprende las mutaciones H183* y G184* y una sustitución seleccionada de N195A, R, D, C, E, Q, G, H, I, L, K, M, P, S, T, W, Y, V (con respecto a SEC ID Nº: 6) o en posiciones correspondientes en otra α-amilasa original tipo Termamyl, y donde la variante muestra termoestabilidad aumentada a pH ácido y/o a concentración de Ca2+ por debajo de 40 ppm, en comparación con una variante correspondiente que comprende las mutaciones H183* y G184* sin la sustitución en N195.
Description
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stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, Streptomyces lividans o Streptomyces murinus; y bacterias gramnegativas tales como E. coli.
[0076] La secuencia de ADN mutada puede además comprender una secuencia de ADN que codifica funciones que permiten la expresión de la secuencia de ADN mutada.
Mutagénesis localizada aleatoria [0077] La mutagénesis aleatoria puede estar ventajosamente localizada en una parte de la α-amilasa original en cuestión. Esto puede, p. ej., ser ventajoso cuando ciertas regiones de la enzima han sido identificadas para ser de importancia particular para una propiedad dada de la enzima, y cuando se modifican se prevé que resultarán en una variante con propiedades mejoradas. Tales regiones pueden normalmente ser identificadas cuando la estructura terciaria de la enzima madre ha sido dilucidada y relacionada con la función de la enzima.
[0078] La mutagénesis aleatoria localizada, o específica es convenientemente realizada usando técnicas de mutagénesis generada por PCR como se ha descrito anteriormente o cualquier otra técnica adecuada conocida en la técnica. De forma alternativa, la secuencia de ADN que codifica la parte de la secuencia de ADN para ser modificada puede ser aislada, p. ej., por inserción en un vector adecuado, y dicha parte puede ser posteriormente sometida a mutagénesis usando cualquiera de los métodos de mutagénesis mencionados anteriormente.
Métodos alternativos de suministro de variantes de α-amilasa
[0079] Métodos alternativos para suministrar variantes de la invención incluyen el método de transposición de genes conocido en la técnica incluyendo los métodos p. ej. descritos en WO 95/22625 (de Affymax Technologies N.V.) y WO 96/00343 (de Novo Nordisk A/S).
Expresión de variantes de α-amilasa
[0080] Según la invención, una secuencia de ADN que codifica la variante producida por métodos anteriormente descritos, o por cualesquiera métodos alternativos conocidos en la técnica, pueden ser expresados, en forma enzimática, usando un vector de expresión que normalmente incluye las secuencias de control que codifican un promotor, operador, sitio de unión al ribosoma, señal de iniciación de la traducción, y, opcionalmente, un gen represor o varios genes activadores.
[0081] El vector de expresión recombinante que lleva la secuencia de ADN que codifica una variante de α-amilasa de la invención puede ser cualquier vector que puede ser sometido convenientemente a procedimientos de ADN recombinante, y la elección del vector frecuentemente dependerá de la célula huésped en la que debe ser introducido. Así, el vector puede ser un vector de replicación autónoma, es decir, un vector que existe como una entidad extracromosómica, cuya replicación es independiente de la replicación cromosómica, p. ej. un plásmido, un bacteriófago
o un elemento extracromosómico, minicromosoma o un cromosoma artificial. De forma alternativa, el vector puede ser uno que, cuando se introduce en una célula huésped, se integra en el genoma de la célula huésped y se replica con el(los) cromosoma(s) en el(los) que ha sido integrado.
[0082] En el vector, la secuencia de ADN debería ser operativamente conectada a una secuencia del promotor adecuada. El promotor puede ser cualquier secuencia de ADN que muestra actividad transcripcional en la célula huésped de elección y puede ser derivada de genes que codifican proteínas bien homólogas o heterólogas a la célula huésped. Ejemplos de promotores adecuados para dirigir la transcripción de la secuencia de ADN que codifica una variante de α-amilasa de la invención, especialmente en un huésped bacteriano, son el promotor del operón lac de E. coli, los promotores del gen dagA de agarasa de Streptomyces coelicolor, los promotores del gen de α-amilasa (amyL) de Bacillus licheniformis, los promotores del gen de amilasa maltogénica (amyM) de Bacillus stearothermophilus, los promotores de la α-amilasa (amyQ) de Bacillus amyloliquefaciens, los promotores de los genes xylA y xylB de Bacillus subtilis etc. Para la transcripción en un huésped fúngico, ejemplos de promotores útiles son estos derivados del gen que codifica la TAKA amilasa de A. oryzae, la proteinasa aspártica de Rhizomucor miehei, la α-amilasa neutra de A. niger, la α-amilasa estable en ácido de A. niger, la glucoamilasa de A. niger, la lipasa de Rhizomucor miehei, la proteasa alcalina de A. oryzae, la triosa fosfato isomerasa de A. oryzae o la acetamidasa de A. nidulans.
[0083] El vector de expresión de la invención puede también comprender un terminador de la transcripción adecuado y, en eucariotas, las secuencias de poliadenilación conectadas operativamente a la secuencia de ADN que codifica la variante de α-amilasa de la invención. Las secuencias de terminación y de poliadenilación pueden derivar de manera adecuada de las mismas fuentes que el promotor.
[0084] El vector puede además comprender una secuencia de ADN que permite que el vector se replique en la célula huésped en cuestión. Ejemplos de tales secuencias son los orígenes de replicación de los plásmidos pUC19, pACYC177, pUB110, pE194, pAMB1 y pIJ702.
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[0085] El vector puede también comprender un marcador seleccionable, p. ej. un gen cuyo producto implementa una falta en la célula huésped, tal como los genes dal de B. subtilis o B. licheniformis, o uno que confiere resistencia antibiótica tal como resistencia a la ampicilina, la canamicina, el cloranfenicol o la tetraciclina. Además, el vector puede comprender marcadores de selección de Aspergillus tales como amdS, argB, niaD y sC, un marcador que da lugar a la resistencia a la higromicina, o la selección puede ser realizada por cotransformación, p. ej. como se describe en WO 91/17243.
[0086] Mientras que la expresión intracelular puede ser ventajosa en algunos aspectos, p. ej. cuando se usan bacterias determinadas como las células huéspedes, es generalmente preferido que la expresión sea extracelular. En general, las α-amilasas de Bacillus mencionadas aquí comprenden una prerregión que permite la secreción de la proteasa expresada en el medio de cultivo. Si se desea, esta prerregión puede ser sustituida por una prerregión diferente o secuencia señal, convenientemente realizada por sustitución de las secuencias de ADN que codifican las prerregiones respectivas.
[0087] Los procedimientos usados para enlazar el constructo de ADN de la invención que codifica una variante de αamilasa, el promotor, terminador y otros elementos, respectivamente, y para insertarlos en vectores adecuados conteniendo la información necesaria para la replicación, son conocidos por los expertos en la técnica (véase, por ejemplo, Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor, 1989 ).
[0088] La célula de la invención, bien comprendiendo un constructo de ADN o un vector de expresión de la invención tal como se ha definido anteriormente, es usado ventajosamente como una célula huésped en la producción recombinante de una variante de α -amilasa de la invención. La célula puede ser transformada con el constructo de ADN de la invención que codifica la variante, integrando convenientemente el constructo de ADN (en una o más copias) en el cromosoma huésped. Esta integración está generalmente considerada como una ventaja puesto que la secuencia de ADN es más propensa a ser mantenida de forma estable en la célula. La integración de los constructos de ADN en el cromosoma huésped puede ser realizada según métodos convencionales, p. ej. por recombinación homóloga o heteróloga. De forma alternativa, la célula puede ser transformada con un vector de expresión como se ha descrito anteriormente en relación con los diferentes tipos de células huéspedes.
[0089] La célula de la invención puede ser una célula de un organismo mayor tal como un mamífero o un insecto, pero es preferiblemente una célula microbiana, p. ej. una célula bacteriana o una fúngica (incluyendo la levadura).
[0090] Ejemplos de bacterias adecuadas son bacterias gram positivas tales como Bacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis o Streptomyces lividans o Streptomyces murinus, o bacterias gram-negativas tales como E. Coli. La transformación de las bacterias puede, por ejemplo, ser efectuada por transformación de protoplastos o usando células competentes de una manera conocida per se.
[0091] El organismo de levadura puede ser seleccionado favorablemente de una especie de Saccharomyces o Schizosaccharomyces, p. ej. Saccharomyces cerevisiae. El hongo filamentoso puede ventajosamente pertenecer a una especie de Aspergillus, p. ej. Aspergillus oryzae o Aspergillus niger. Células micóticas pueden ser transformadas por un proceso que implica la formación de protoplastos y la transformación de los protoplastos seguida por la regeneración de la pared celular de una manera conocida per se. Un procedimiento adecuado para la transformación de células huéspedes de Aspergillus está descrito en EP 238 023.
[0092] En otro aspecto adicional, la presente invención se refiere a un método para producir una variante de α-amilasa de la invención, dicho método comprende el cultivo de una célula huésped como se ha descrito anteriormente bajo condiciones propicias para la producción de la variante y la recuperación de la variante de las células y/o del medio de cultivo.
[0093] El medio usado para cultivar las células pueden ser cualquier medio convencional adecuado para el crecimiento de la célula huésped en cuestión y la obtención de la expresión de la variante de α-amilasa de la invención. Medios adecuados están disponibles de proveedores comerciales o pueden ser preparados según recetas publicadas (p. ej. como se describe en los catálogos de la American Type Culture Collection).
[0094] La variante de α-amilasa segregada de las células huéspedes pueden ser recuperadas convenientemente del medio de cultivo por procedimientos bien conocidos, incluyendo la separación de las células del medio por centrifugado
o por filtración, y la precipitación de los componentes proteináceos del medio mediante una sal tal como sulfato de amonio, seguido del uso de procedimientos cromatográficos tales como la cromatografía de intercambio iónico, cromatografía de afinidad, o similares.
Aplicaciones industriales
[0095] Las variantes de α -amilasa de esta invención poseen propiedades valiosas que permiten una variedad de aplicaciones industriales. En particular, las variantes de la enzima de la invención son aplicables como un componente
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obstante, las designaciones "tampón", "cristal 1", cristal 1a" y cristal 2" son aquellas a las que se hace referencia en estas pautas.
6.1. Sustrato
5 [0126] 4, 6-etilideno(G7)-p-nitrofenil(G1)-α,D-maltoheptaósido (escrito como etilideno-G7-PNP) p. ej. Boehringer Mannheim 1442 309
6.2 Reactivo auxiliar de α-glucosidasa
10 [0127] α-glucosidasa, p. ej. Boehringer Mannheim 1442 309
6.3 Solución BRIJ 35 15 [0128]
BRIJ 35 (30% p/v de Sigma 430 AG-6) 1000 ml Agua desmineralizada hasta 2.000 ml
6.4 Estabilizador
Solución BRIJ 35 33 ml CaCl2*2H2O (Merck 2382) 882 g Agua desmineralizada hasta 2.000 ml
7. Muestras y estándares
25 7.1 Curva estándar
Ejemplo: preparación de curva estándar de BS-amilasa
[0130] El estándar pertinente es diluido a 0.60 KNU(s)/ml como sigue. Una cantidad calculada de estándar es pesada y
30 añadida a un matraz aforado de 200 ml, que es rellenado hasta alrededor de la marca de 2/3 con agua desmineralizada. Se añade estabilizador correspondiente al 1% del volumen del matraz y el matraz es rellenado hasta la marca con agua desmineralizada.
[0131] Se utiliza un Hamilton Microlab 1000 para producir las diluciones mostradas abajo. Agua desmineralizada con 1% 35 de estabilizador se usa como el diluyente.
- Número de dilución
- Solución de reserva enzimática 1% estabilizador KNU(s)/ml
- 1
- 20µL 580µL 0,02
- 2
- 30µL 570µL 0,03
- 3
- 40µL 560µL 0,04
- 4
- 50µL 550µL 0,05
- 5
- 60µL 540µL 0,06
7.2 Control de nivel
40 [0132] Un control del nivel de BS amilasa de Novo Nordisk A/S está incluido en todas las series usando el Cobas Fara. El control es diluido con 1% estabilizador de modo que la dilución final está en la gama de la curva estándar. Todos los pesos y diluciones están anotados en la lista de trabajo
7.3 Soluciones de muestra
45 Determinación única
[0133] Muestras de fermentación (no muestras finales) a partir de la producción, todas las muestras de fermentación de instalaciones experimentales y muestras de estabilidad de almacenamiento son pesadas y analizadas una vez sólo. 50 [0134] Determinación doble en 1 serie:
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TVB146: SEC ID Nº:3 con la deleción en posiciones I181-G182 + 36600 NU/mg N193F: (mutación doble) TVB163: SEC ID Nº:3 con la deleción en posiciones I181-36300 NU/mg G182+N193F+E214Q: (mutación triple)
Ejemplo 3
Cocción a presión y licuefacción en instalación experimental con variante de alfa-amilasa TVB146
5 [0175] Experimentos de licuefacción en instalación experimental fueron realizados en el sistema mini-jet usando una dosificación de 50 NU (S)/g DS a pH 5.5 con 5 ppm de Ca++ añadido, para comparar el rendimiento de la variante de BSG alfa-amilasa TVB146 formulada (SEC ID Nº: 3 con deleción en posiciones
[0177] Mezclas de almidón de maíz fueron preparadas suspendiendo 11,8 kg de Cerestar C*Pharm GL 03406 (89 % almidón) en agua desionizada y compensando hasta 30 kg. El pH fue ajustado a 5.5 a temperatura ambiente, después 15 de la adición de 0,55 g de CaCl2.2H2O.
[0178] Las enzimas siguientes fueron usadas:
TVB146 108 KNU(S)/g, 146 KNU(SM9)/g BSG amilasa 101 KNU(S)/g, 98 KNU(SM9)/g
20 [0179] Una cantidad de enzima correspondiente a 50 NU (SM9)/g DS fue añadida, y la conductividad ajustada a 300mS usando NaCl. Las condiciones estándares fueron las siguientes:
Concentración de sustrato 35 % p/p (inicial) 31,6-31,9 % p/p (final) Temperatura 105°C, 5 min (licuefacción primaria) 95°C, 90 min (licuefacción secundaria) pH (inicial) 5.5
[0180] Después del sometimiento a presión, el almidón licuado fue recogido y transportado en termo-matraces sellados 25 de la instalación experimental al laboratorio, donde se continuó la licuefacción secundaria a 95 °C.
[0181] 10 ml de muestras fueron tomadas a intervalos de 15 minutos de 15-90 minutos. 2 gotas de 1 N HCl fueron añadidas para inactivar la enzima. A partir de estas muestras, 0,3-0,1 g (según el DE previsto) fueron pesadas y diluidas a 100 ml. Azúcares de reducción fueron luego determinados según el método Neocuproina (Determinación de azúcar de
30 reducción con precisión mejorada. Dygert, Li, Florida and Thomas (1965). Anal. Biochem 13: 368) y los valores de DE determinados. El desarrollo de DE como función del tiempo está provisto en la siguiente tabla:
- TVB146 BSG
- Tiempo (min,)
- DE (Neocuproina)
- 15
- 2,80 2,32
- 30
- 4,88 3,56
- 45
- 6,58 4,98
- 60
- 8,17 6,00
- 75
- 9,91 7,40
- 90
- 11,23 8,03
[0182] Como se puede observar la variante de alfa-amilasa TVB146 dio mejor rendimiento significativamente bajo 35 condiciones de aplicación industrialmente relevantes a niveles bajos de calcio que la BSG alfa-amilasa original.
Ejemplo 4
Cocción a presión y Licuefacción con una combinación de variantes de alfa-amilasa (TVB146 y LE174)
40 [0183] La cocción a presión y licuefacción usando una combinación de las variantes de alfa-amilasa, TVB146 y LE174 (proporción 1:1) fueron realizadas en las condiciones siguientes:
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Claims (1)
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imagen1
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DK117297 | 1997-10-13 | ||
DK117297 | 1997-10-13 |
Publications (1)
Publication Number | Publication Date |
---|---|
ES2536878T3 true ES2536878T3 (es) | 2015-05-29 |
Family
ID=8101815
Family Applications (3)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ES09152241.7T Expired - Lifetime ES2536878T3 (es) | 1997-10-13 | 1998-10-13 | Mutantes de alfa-amilasa |
ES98947417T Expired - Lifetime ES2322825T3 (es) | 1997-10-13 | 1998-10-13 | Mutantes de alfa-amilasa. |
ES10182050T Expired - Lifetime ES2436066T3 (es) | 1997-10-13 | 1998-10-13 | Mutantes de alfa-amilasa |
Family Applications After (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ES98947417T Expired - Lifetime ES2322825T3 (es) | 1997-10-13 | 1998-10-13 | Mutantes de alfa-amilasa. |
ES10182050T Expired - Lifetime ES2436066T3 (es) | 1997-10-13 | 1998-10-13 | Mutantes de alfa-amilasa |
Country Status (12)
Country | Link |
---|---|
US (1) | US6187576B1 (es) |
EP (3) | EP1023439B1 (es) |
JP (1) | JP4358431B2 (es) |
KR (1) | KR20010015754A (es) |
AR (1) | AR017331A1 (es) |
AT (1) | ATE423192T1 (es) |
AU (1) | AU9434398A (es) |
CA (2) | CA2305191C (es) |
DE (1) | DE69840577D1 (es) |
DK (2) | DK2206768T3 (es) |
ES (3) | ES2536878T3 (es) |
WO (1) | WO1999019467A1 (es) |
Families Citing this family (521)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CA2845178A1 (en) * | 1997-10-30 | 1999-05-14 | Novozymes A/S | .alpha.-amylase mutants |
US6197565B1 (en) * | 1998-11-16 | 2001-03-06 | Novo-Nordisk A/S | α-Amylase variants |
US6887986B1 (en) | 1998-11-16 | 2005-05-03 | Novozymes A/S | α-amylase variants |
JP4745503B2 (ja) * | 1999-03-31 | 2011-08-10 | ノボザイムス アクティーゼルスカブ | アルカリα−アミラーゼ活性を有するポリペプチド及びそれらをコードする核酸 |
US6623948B1 (en) * | 1999-03-31 | 2003-09-23 | Novozymes A/S | Nucleic acid sequences encoding alkaline alpha-amylases |
EP2221365A1 (en) | 2000-03-08 | 2010-08-25 | Novozymes A/S | Variants with altered properties |
JP2004504837A (ja) * | 2000-07-28 | 2004-02-19 | ヘンケル・コマンディットゲゼルシャフト・アウフ・アクチエン | バシラス種a7−7(dsm12368)から抽出した新規デンプン分解酵素ならびに該新規デンプン分解酵素を含有する洗浄および清浄剤 |
DE10036752C2 (de) * | 2000-07-28 | 2003-02-20 | Henkel Kgaa | Wasch- und Reinigungsmittel mit einem neuen amylolytischen Enzym aus Bacillus sp. A 7-7(DSM 12368) |
US20020155574A1 (en) * | 2000-08-01 | 2002-10-24 | Novozymes A/S | Alpha-amylase mutants with altered properties |
JP4855632B2 (ja) * | 2000-08-01 | 2012-01-18 | ノボザイムス アクティーゼルスカブ | 変更された性質を有するα−アミラーゼ突然変異体 |
US7244597B2 (en) | 2000-11-10 | 2007-07-17 | Novozymes A/S | Secondary liquefaction in ethanol production |
EP2159279A3 (en) | 2001-05-15 | 2010-05-12 | Novozymes A/S | Alpha-amylase variant with altered properties |
CN1288450C (zh) * | 2001-07-11 | 2006-12-06 | 佛姆法克特股份有限公司 | 探头和探测卡制造方法 |
US6729019B2 (en) * | 2001-07-11 | 2004-05-04 | Formfactor, Inc. | Method of manufacturing a probe card |
DE10138753B4 (de) * | 2001-08-07 | 2017-07-20 | Henkel Ag & Co. Kgaa | Wasch- und Reinigungsmittel mit Hybrid-Alpha-Amylasen |
US20040063184A1 (en) | 2002-09-26 | 2004-04-01 | Novozymes North America, Inc. | Fermentation processes and compositions |
EP2500423B1 (en) | 2003-02-26 | 2015-06-17 | Danisco US Inc. | Amylases producing an altered immunogenic response and methods of making and using the same |
DE10362172B4 (de) * | 2003-03-05 | 2009-04-02 | Henkel Ag & Co. Kgaa | Wasch-und Reinigungsmittel mit Alpha-Amylase-Varianten mit verbesserter Alkaliaktivität |
DE04718914T1 (de) | 2003-03-10 | 2006-02-23 | Novozymes A/S | Verfahren zur herstellung von alkohol |
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DE69032360T2 (de) | 1989-06-29 | 1998-12-03 | Genencor Int | Mutierte mikrobielle alpha-Amylasen mit erhöhter thermischer, saurer und/oder alkylischer Stabilität |
AU639570B2 (en) | 1990-05-09 | 1993-07-29 | Novozymes A/S | A cellulase preparation comprising an endoglucanase enzyme |
KR100237967B1 (ko) | 1990-12-21 | 2000-01-15 | 한센 핀 베네드 | pH의 범위에 걸쳐 낮은 분자전하의 변이도를 갖는 효소 돌연변이체 |
DK0689589T4 (da) | 1993-02-11 | 2010-01-04 | Genencor Int | Oxidativ stabil alfa-amylase |
JPH09503916A (ja) * | 1993-10-08 | 1997-04-22 | ノボ ノルディスク アクティーゼルスカブ | アミラーゼ変異体 |
US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
WO1995026397A1 (en) | 1994-03-29 | 1995-10-05 | Novo Nordisk A/S | Alkaline bacillus amylase |
DE69534369T2 (de) * | 1994-06-17 | 2006-03-09 | Genencor International, Inc., Palo Alto | Von der alpha-amylase aus b. licheniformis abgeleitete amylolytische enzyme mit verbesserten eigenschaften |
DE4422198C2 (de) | 1994-06-24 | 1997-08-28 | Audi Ag | Verfahren zum Steuern der elektrischen Beheizung eines Katalysators |
AR000862A1 (es) * | 1995-02-03 | 1997-08-06 | Novozymes As | Variantes de una ó-amilasa madre, un metodo para producir la misma, una estructura de adn y un vector de expresion, una celula transformada por dichaestructura de adn y vector, un aditivo para detergente, composicion detergente, una composicion para lavado de ropa y una composicion para la eliminacion del |
EP2199378B1 (en) | 1995-02-03 | 2012-08-15 | Novozymes A/S | A method of designing alpha-amylase mutants with predetermined properties |
WO1997007202A1 (en) | 1995-08-11 | 1997-02-27 | Novo Nordisk A/S | Novel lipolytic enzymes |
ES2432519T3 (es) * | 1996-04-30 | 2013-12-04 | Novozymes A/S | Mutantes de alfa-amilasa |
CA2845178A1 (en) * | 1997-10-30 | 1999-05-14 | Novozymes A/S | .alpha.-amylase mutants |
-
1998
- 1998-10-13 EP EP98947417A patent/EP1023439B1/en not_active Expired - Lifetime
- 1998-10-13 US US09/170,670 patent/US6187576B1/en not_active Expired - Lifetime
- 1998-10-13 EP EP09152241.7A patent/EP2206768B1/en not_active Expired - Lifetime
- 1998-10-13 DE DE69840577T patent/DE69840577D1/de not_active Expired - Lifetime
- 1998-10-13 JP JP2000516020A patent/JP4358431B2/ja not_active Expired - Lifetime
- 1998-10-13 KR KR1020007003941A patent/KR20010015754A/ko not_active Application Discontinuation
- 1998-10-13 EP EP10182050.4A patent/EP2302027B1/en not_active Expired - Lifetime
- 1998-10-13 AR ARP980105089A patent/AR017331A1/es active IP Right Grant
- 1998-10-13 AT AT98947417T patent/ATE423192T1/de not_active IP Right Cessation
- 1998-10-13 ES ES09152241.7T patent/ES2536878T3/es not_active Expired - Lifetime
- 1998-10-13 CA CA2305191A patent/CA2305191C/en not_active Expired - Lifetime
- 1998-10-13 ES ES98947417T patent/ES2322825T3/es not_active Expired - Lifetime
- 1998-10-13 ES ES10182050T patent/ES2436066T3/es not_active Expired - Lifetime
- 1998-10-13 AU AU94343/98A patent/AU9434398A/en not_active Abandoned
- 1998-10-13 CA CA2745783A patent/CA2745783C/en not_active Expired - Lifetime
- 1998-10-13 DK DK09152241.7T patent/DK2206768T3/en active
- 1998-10-13 WO PCT/DK1998/000444 patent/WO1999019467A1/en not_active Application Discontinuation
- 1998-10-13 DK DK10182050.4T patent/DK2302027T3/da active
Also Published As
Publication number | Publication date |
---|---|
KR20010015754A (ko) | 2001-02-26 |
ATE423192T1 (de) | 2009-03-15 |
WO1999019467A1 (en) | 1999-04-22 |
JP2001520006A (ja) | 2001-10-30 |
EP2206768B1 (en) | 2015-04-01 |
EP2302027A2 (en) | 2011-03-30 |
EP2302027A3 (en) | 2011-06-29 |
AU9434398A (en) | 1999-05-03 |
EP2206768A3 (en) | 2010-10-06 |
EP1023439A1 (en) | 2000-08-02 |
ES2322825T3 (es) | 2009-06-29 |
AR017331A1 (es) | 2001-09-05 |
US6187576B1 (en) | 2001-02-13 |
DK2302027T3 (da) | 2013-12-02 |
CA2745783C (en) | 2016-05-24 |
DK2206768T3 (en) | 2015-06-29 |
ES2436066T3 (es) | 2013-12-26 |
CA2305191A1 (en) | 1999-04-22 |
DE69840577D1 (de) | 2009-04-02 |
CA2745783A1 (en) | 1999-04-22 |
CA2305191C (en) | 2011-09-27 |
EP2206768A2 (en) | 2010-07-14 |
EP1023439B1 (en) | 2009-02-18 |
EP2302027B1 (en) | 2013-08-28 |
JP4358431B2 (ja) | 2009-11-04 |
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