ES2563209T3 - Variantes de beta-glucosidasa y polinucleótidos que codifican las mismas - Google Patents

Variantes de beta-glucosidasa y polinucleótidos que codifican las mismas Download PDF

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ES2563209T3
ES2563209T3 ES11767880.5T ES11767880T ES2563209T3 ES 2563209 T3 ES2563209 T3 ES 2563209T3 ES 11767880 T ES11767880 T ES 11767880T ES 2563209 T3 ES2563209 T3 ES 2563209T3
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seq
beta
glucosidase
variant
bacillus
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Mark Wogulis
Paul Harris
David Osborn
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Novozymes Inc
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Abstract

Variante de beta-glucosidasa, que comprende o consistente en una sustitución en las posiciones correspondientes a las posiciones 89, 91,140 y 186 del polipéptido maduro de SEC ID nº: 2, donde la variante tiene actividad de betaglucosidasa y donde la variante tiene al menos 80%, pero menos del 100%, de identidad de secuencia con el polipéptido maduro de SEC ID nº: 2.

Description

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polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones G91L + F100D + I140V + I186V + S283G + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones G91 L + F100D + I140V + I186V + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones G91 L + F100D + I140V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones G91 L + F100D + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones G91L + I140V + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones F100D + I140V + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2.
[0121] La variante puede comprender las sustituciones L89M + G91L + F100D + I140V + I186V + S283G + N456E del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones L89M + G91L + F100D + I140V + I186V + S283G + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones L89M
+ G91L + F100D + I140V + I186V + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones L89M + G91L + F100D + I140V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones L89M + G91L + F100D + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones L89M + G91L + I140V + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones L89M + F100D + I140V + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2. La variante puede comprender las sustituciones G91 L + F100D + I140V + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2.
[0122] La variante puede comprender las sustituciones L89M + G91L + F100D + I140V + I186V + S283G + N456E + F512Y del polipéptido maduro de SEC ID nº: 2.
[0123] Las variantes de la presente invención pueden comprender además una alteración, por ejemplo, deleción, inserción y/o sustitución en una o más (por ejemplo, varias) otras posiciones.
[0124] Los cambios en los aminoácidos pueden ser de naturaleza menor, es decir, sustituciones o inserciones de aminoácidos conservadoras que no afecten significativamente al plegado y/o la actividad de la proteína; deleciones pequeñas, típicamente de 1-30 aminoácidos; extensiones pequeñas amino-o carboxil-terminales, tales como un residuo de metionina aminoterminal; un péptido enlazador pequeño de hasta 20-25 residuos; o una extensión pequeña que facilite la purificación cambiando la carga neta u otra función, tal como un tracto de polihistidina, un epítopo antigénico o un dominio de unión.
[0125] Ejemplos de sustituciones conservadoras están en los grupos de aminoácidos básicos (arginina, lisina e histidina), aminoácidos ácidos (ácido glutámico y ácido aspártico), aminoácidos polares (glutamina y asparagina), aminoácidos hidrofóbicos (leucina, isoleucina y valina), aminoácidos aromáticos (fenilalanina, triptófano y tirosina) y aminoácidos pequeños (glicina, alanina, serina, treonina y metionina). Sustituciones de aminoácidos que en general no alteran la actividad específica se conocen en la técnica y son descritas, por ejemplo, por H. Neurath and R.L. Hill, 1979, en, The Proteins, Academic Press, Nueva York. Sustituciones comunes son Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu y Asp/Gly.
[0126] Alternativamente, los cambios en los aminoácidos son de tal naturaleza que las propiedades físico químicas de los polipéptidos se ven alteradas. Por ejemplo, cambios en los aminoácidos pueden mejorar la termoestabilidad del polipéptido, alterar la especificidad de sustrato, cambiar el pH óptimo y similares.
[0127] Aminoácidos esenciales en un polipéptido se pueden identificar según procedimientos conocidos en la técnica, tal como mutagénesis dirigida al sitio o mutagénesis de escaneado de alanina (Cunningham and Wells, 1989, Science 244: 1081-1085). En la técnica anterior, mutaciones de alanina individuales se introducen en cada residuo de la molécula y las moléculas mutantes resultantes se evalúan para polipéptido que tiene actividad de beta-glucosidasa para identificar residuos de aminoácidos que son críticos para la actividad de la molécula. Véase también, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. El sitio activo del polipéptido que tiene actividad de beta-glucosidasa u otra interacción biológica se puede determinar también por análisis físico de estructura, como se determina por técnicas tales como resonancia magnética nuclear, cristalografía, difracción electrónica o marcaje por fotoafinidad, junto con mutación de aminoácidos de sitio de contacto putativo. Véase, por ejemplo, de de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. La identidad de aminoácidos esenciales también se puede inferir a partir de un alineamiento con un polipéptido relacionado.
[0128] Las variantes pueden consistir en los aminoácidos 720 a 863, por ejemplo, los aminoácidos 720 a 739, 740 a 759, 760 a 779, 780 a 799, 800 a 819, 820 a 839 y 840 a 863.
[0129] La variante puede tener actividad específica mejorada.
Beta-glucosidasas originales
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[0141] El original puede ser un polipéptido de fusión o polipéptido de fusión divisible donde otro polipéptido se fusiona en el N-término o el C-término del polipéptido de la presente invención. Un polipéptido de fusión se produce por fusión de un polinucleótido que codifica a otro polipéptido a un polinucleótido de la presente invención. Técnicas para producir polipéptidos de fusión se conocen en la técnica, e incluyen ligamiento de las secuencias de codificación que codifican los polipéptidos de modo que éstas estén en marco y que la expresión del polipéptido de fusión esté bajo control del mismo promotor(es) y terminador. Los polipéptidos de fusión también se pueden construir usando tecnología de inteína donde los polipéptidos de fusión se crean postraduccionalmente (Cooper et al., 1993, EMBO J. 12: 2575-2583; Dawson et al., 1994, Science 266: 776-779).
[0142] Un polipéptido de fusión puede además comprender un sitio de escisión entre los dos polipéptidos. En la secreción de la proteína de fusión, el sitio se divide liberando los dos polipéptidos. Ejemplos de sitios de escisión incluyen, pero de forma no limitativa, los sitios descritos en Martin et al., 2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000, J. Biotechnol. 76: 245-251; Rasmussen-Wilson et al., 1997, Appl. Environ. Microbiol. 63: 34883493; Ward et al., 1995, Biotechnology 13: 498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton et al., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1995, Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure, Function, and Genetics 6: 240-248; and Stevens, 2003, Drug Discovery World 4: 35-48.
[0143] El original se puede obtener a partir de microorganismos de cualquier género. Para fines de la presente invención, el término "obtenido a partir de", como se utilizan en este caso, en relación con una fuente dada significará que el original codificado por un polinucleótido es producido por la fuente o por una cepa donde el polinucleótido de la fuente se ha insertado. En un aspecto, el original es secretado extracelularmente.
[0144] El original puede ser una beta-glucosidasa bacteriana. Por ejemplo, el original puede ser un polipéptido bacteriano gram-positivo tal como una beta-glucosidasa de Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus o Streptomyces, o un polipéptido bacteriano gram-negativo tal como una beta-glucosidasa de Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella o Ureaplasma.
[0145] En un aspecto, el original es una beta-glucosidasa de Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus subtilis o Bacillus thuringiensis.
[0146] En otro aspecto, el original es una beta-glucosidasa de Streptococcus equisimilis, Streptococcus pyogenes, Streptococcus uberis o Streptococcus equi subesp. Zooepidemicus.
[0147] En otro aspecto, el original es una beta-glucosidasa de Streptomyces achromogenes, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces griseus o Streptomyces lividans.
[0148] El original puede ser una beta-glucosidasa fúngica. Por ejemplo, el original puede ser un polipéptido de levadura que tiene actividad de beta-glucosidasa tal como una beta-glucosidasa de Candida, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces o Yarrowia. Por ejemplo, el original puede ser una beta-glucosidasa fúngica filamentosa tal como una beta-glucosidasa de Acremonium, Agaricus, Alternaria, Aspergillus, Aureobasidium, Botryospaeria, Ceriporiopsis, Chaetomidium, Chrysosporium, Claviceps, Cochliobolus, Coprinopsis, Coptotermes, Corynascus, Cryphonectria, Cryptococcus, Diplodia, Exidia, Filibasidium, Fusarium, Gibberella, Holomastigotoides, Humicola, Irpex, Lentinula, Leptospaeria, Magnaporthe, Melanocarpus, Meripilus, Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Phanerochaete, Piromyces, Poitrasia, Pseudoplectania, Pseudotrichonympha, Rhizomucor, Schizophyllum, Scytalidium, Talaromyces, Thermoascus, Thielavia, Tolypocladium, Trichoderma, Trichophaea, Verticillium, Volvariella o Xylaria.
[0149] En otro aspecto, el original es una beta-glucosidasa de Saccharomyces carlsbergensis, Saccharomyces cerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii, Saccharomyces kluyveri, Saccharomyces norbensis o Saccharomyces oviformis.
[0150] En otro aspecto, el original es una beta-glucosidasa de Acremonium cellulolyticus, Aspergillus aculeatus, Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus japonicus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Chrysosporium inops, Chrysosporium keratinophilum, Chrysosporium lucknowense, Chrysosporium merdarium, Chrysosporium pannicola, Chrysosporium queenslandicum, Chrysosporium tropicum, Chrysosporium zonatum, Fusarium bactridioides, Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusarium graminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi, Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusarium sambucinum, Fusarium sarcochroum, Fusarium sporotrichioides, Fusarium sulphureum, Fusarium torulosum, Fusarium trichothecioides, Fusarium venenatum, Humicola grisea, Humicola insolens, Humicola lanuginosa, Irpex lacteus, Mucor miehei, Myceliophthora thermophila, Neurospora crassa, Penicillium funiculosum, Penicillium purpurogenum, Phanerochaete chrysosporium, Thielavia achromatica, Thielavia albomyces, Thielavia albopilosa, Thielavia australeinsis, Thielavia fimeti, Thielavia microspora, Thielavia ovispora, Thielavia
20
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[0386] Concentraciones de azúcar de muestras diluidas en 0,005 M H2SO4 fueron medidas después de elución por 0,005 M de H2SO4 con 0,05% p/p de ácido benzoico a una velocidad de flujo de 0,6 ml por minuto a partir de una columna 4,6 x 250 mM AMINEX® HPX-87H (Bio-Rad Laboratories, Inc., Hercules, CA, EE.UU.) a 65°C con
5 cuantificación por integración de glucosa y señales de celobiosa a partir de detección del índice de refracción (CHEMSTATION®, AGILENT® 1100 HPLC, Agilent Technologies, Santa Clara, CA, EE.UU.) calibrado por muestras de azúcar puro. Los equivalentes resultantes fueron usados para calcular el porcentaje de conversión de celulosa para cada reacción.
10 [0387] La glucosa liberada fue calculada substrayendo niveles de glucosa medidos en los PCS solo de los medidos en los PCS con mezcla enzimática.
[0388] Los resultados mostrados en la figura 2 demostraron que la variante de beta-glucosidasa de A. fumigatus F100D
+ S283G + N456E + F512Y tiene una actividad específica más alta que la beta-glucosidasa de tipo salvaje (libera más
15 glucosa en una concentración enzimática dada que la enzima de tipo salvaje en la misma concentración bajo las condiciones especificadas).
Ejemplo 7: construcción de unas variantes del gen de beta-glucosidasa GH3A de la familia de Aspergillus fumigatus
20 [0389] Variantes de la beta-glucosidasa 3A de la familia de Aspergillus fumigatus fueron construidas mediante la realización mutagénesis dirigida al sitio en pEJG97 (para pMaWo87i1) o pDFng128-6 (para pMaWo86i1) o pMaWo87i1 (para pMaWo87i2) o pMaWo86i1 (para pMaWo86i2) o pMaWo86i2 (para pMaWo86) o pMaWo87i2 (para pMaWo87) utilizando un equipo de mutagénesis dirigida al sitio de QUIKCHANGE®.
25 [0390] Un resumen de los oligos usados para la mutagénesis dirigida al sitio y las variantes obtenidas se muestra en la tabla 2.
[0391] Los ADNs de plásmidos mutantes resultantes fueron preparados utilizando un BIOROBOT® 9600. Los 30 constructos de plásmido variante fueron ordenados utilizando un analizador genético Applied Biosystems 3130xl para verificar los cambios.
Tabla 2
Cambios en los aminoácidos
Nombre del cebador Secuencias Nombre del plásmido de clonación
I140V
MaWo220 cgacaagggcgtggacgttttgctggggcctgc (SEC ID Nº: 133) pMaWo87i1
MaWo221
gcaggccccagcaaaacgtccacgcccttgtcg (SEC ID Nº: 134)
I140V + F100D + S283G + N456E + F512Y
MaWo220 cgacaagggcgtggacgttttgctggggcctgc (SEC ID Nº: 135) pMaWo86i1
MaWo221
gcaggccccagcaaaacgtccacgcccttgtcg (SEC ID Nº: 136)
I186V + I140V
MaWo222 ccaagacgcgggtgtggttgctactgccaagc 137) pMaWo87i2
MaWo223
gcttggcagtagcaaccacacccgcgtcttgg (SEC ID Nº: 138)
L89M + G91 L + I140V + F100D + S283G + N456E + F512Y
MaWo218 ggtatcaactggggtatgtgtctccaggattcccctttgggtatccg (SEC ID Nº: 139) pMaWo86i2
MaWo219
cggatacccaaaggggaatcctggagacacataccccagttgatacc (SEC ID Nº: 140)
L89M + G91 L + I186V + I140V
MaWo218 ggtatcaactggggtatgtgtctccaggattcccctttgggtatccg (SEC ID Nº: 141) pMaWo87
MaWo219
cggatacccaaaggggaatcctggagacacataccccagttgatacc (SEC ID Nº: 142)
1186V + L89M + G91 L + 1140V + F100D + S283G + N456E + F512Y
MaWo222 ccaagacgcgggtgtggttgctactgccaagc (SEC ID Nº: 143) pMaWo86
MaWo223
gcttggcagtagcaaccacacccgcgtcttgg (SEC ID Nº: 144)
35
Ejemplo 8: expresión de la variante de beta-glucosidasa GH3A de la familia de Aspergillus fumigatus L89M + G91L + F100D + I140V + I186V + S283G + N456E + F512Y y variante L89M + G91L + I140V + I186V en el Aspergillus oryzae JaL250
40 [0392] Los protoplastos de Aspergillus oryzae JaL250 fueron preparados según el método de Christensen et al., 1988, supra y transformados con 5 µg de vector de expresión pMaWo86 o pMaWo87 o pEJG97 (como un control) o
47

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