ES2569033T3 - Procesos para producir productos de fermentación - Google Patents

Procesos para producir productos de fermentación Download PDF

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ES2569033T3
ES2569033T3 ES11768432.4T ES11768432T ES2569033T3 ES 2569033 T3 ES2569033 T3 ES 2569033T3 ES 11768432 T ES11768432 T ES 11768432T ES 2569033 T3 ES2569033 T3 ES 2569033T3
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amylase
substitutions
reference alpha
alpha
processes
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Randall Deinhammer
Guillermo Coward-Kelly
Ming Li
Junxin Duan
Zheng Liu
Shiro Fukuyama
Keiichi Ayabe
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Novozymes AS
Novozymes North America Inc
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Novozymes North America Inc
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
    • 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
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/02—Monosaccharides
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/20—Preparation of compounds containing saccharide radicals produced by the action of an exo-1,4 alpha-glucosidase, e.g. dextrose
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
    • C12P7/04—Preparation of oxygen-containing organic compounds containing a hydroxy group acyclic
    • C12P7/06—Ethanol, i.e. non-beverage
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
    • Y02E50/00—Technologies for the production of fuel of non-fossil origin
    • Y02E50/10—Biofuels, e.g. bio-diesel

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
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  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
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  • Biotechnology (AREA)
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  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Biomedical Technology (AREA)
  • Molecular Biology (AREA)
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  • Enzymes And Modification Thereof (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

Proceso para producir productos de fermentación a partir de material que contiene almidón que incluye las etapas de: i) licuefacción del material que contiene almidón utilizando una alfa-amilasa; ii) sacarificación utilizando una glucoamilasa que tiene al menos 80% de identidad con el polipéptido maduro mostrado en SEC ID n.º: 9; iii) fermentación utilizando un organismo fermentador.

Description

imagen1
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Alfa-amilasa de referencia A con las sustituciones V59A+Q89R+E129V+ K177L+R179E+K220P+N224L+ Q254S+1270L
168 21 ND
Alfa-amilasa de referencia A con las sustituciones V59A+Q89R+E129V+ K177L+R179E+K220P+N224L+ Q254S+H274K
>180 24 ND
Alfa-amilasa de referencia A con las sustituciones V59A+Q89R+E129V+ K177L+R179E+K220P+N224L+ Q254S+Y276F
91 15 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ R157Y+K177L+R179E+K220P+ N224L+S242Q+Q254S
141 41 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+H208Y+K220P+ N224L+S242Q+Q254S
>180 62 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S
>180 49 >480
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S+H274K
>180 53 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S+Y276F
>180 57 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S+D281N
>180 37 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S+M284T
>180 51 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S+G416V
>180 45 ND
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ Q254S
143 21 >480
Alfa-amilasa de referencia A con las sustituciones V59A+E129V+ K177L+R179E+K220P+N224L+ Q254S+M284T
>180 22 ND
Alfa-amilasa de referencia A con las sustituciones A91L+M961+E129V+ K177L+R179E+K220P+N224L+ S242Q+Q254S
>180 38 ND
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E
57 11 402
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E+K220P+N224L+S242Q+ Q254S
174 44 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+R179E+K220P+N224L+S242Q+ Q254S+Y276F+L427M
>180 49 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E+K220P+N224L+S242Q+ Q254S+M284T
>180 49 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E+K220P+N224L+S242Q+ Q254S+N376*+I377*
177 36 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E+K220P+N224L+Q254S
94 13 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E+K220P+N224L+Q254S+ M284T
129 24 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179E+S242Q
148 30 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+ R179V
78 9 >480
Alfa-amilasa de referencia A con las sustituciones E129V+K177L+R179V+K220P+N224L+S242Q+ Q254S
178 31 >480
Alfa-amilasa de referencia A con las sustituciones K220P+N224L+ S242Q+Q254S
66 17 >480
Alfa-amilasa de referencia A con las sustituciones K220P+N224L+ Q254S
30 6 159
Alfa-amilasa de referencia A con la sustitución M284T
35 7 278
Alfa-amilasa de referencia A con las sustituciones M284V
59 13 ND
ND no determinado
[0118] Los resultados demuestran que las variantes de alfa-amilasa tienen significativamente superior a las de la alfa-amilasa de referencia.
una vida media y una estabilidad
5
Ejemplo 2
Preparación de variantes de proteasa y prueba de termoestabilidad
10
[0119] Los productos químicos usados fueron productos comerciales de al menos calidad reactiva.
15
imagen14
imagen15
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JTP095
N26R/T46R/D79L/S87P/A112P/D142L 62%
JTP096
T46R/D79L/S87P/T116V/D142L 67%
JTP099
D79L/P81R/S87P/A112P/D142L 80%
JTP101
A27K/D79L/S87P/A112P/T124V/D142L 81%
JTP116
D79L/Y82F/S87P/A112P/T124V/D142L 59%
JTP117
D79L/Y82F/S87P/A112P/T124V/D142L 94%
JTP127
D79L/S87P/A112P/T124V/A126V/D142L 53%
JTP050
D79L S87P A112P D142L 23% 9%
JTP134
D79L Y82F S87P A112P D142L 40%
JTP135
S38T D79L S87P A112P A126V D142L 62%
JTP136
D79L Y82F S87P A112P A126V D142L 59%
JTP137
A27K D79L S87P A112P A126V D142L 54%
JTP145
S49P D79L S87P A112P D142L 59%
JTP146
S50P D79L S87P A112P D142L 63%
JTP148
D79L S87P D104P A112P D142L 64%
JTP161
D79L Y82F S87G A112P D142L 30% 12%
JTP180
S70V D79L Y82F S87G Y97W A112P D142L 52%
JTP181
D79L Y82F S87G Y97W D104P A112P D142L 45%
JTP187
S70V D79L Y82F S87G A112P D142L 45%
JTP188
D79L Y82F S87G D104P A112P D142L 43%
JTP189
D79L Y82F S87G A112P A126V D142L 46%
JTP193
Y82F S87G S70V D79L D104P A112P D142L 15%
JTP194
Y82F S87G D79L D104P A112P A126V D142L 22%
JTP196
A27K D79L Y82F S87G D104P A112P A126V D142L 18%
Tabla 4. Actividad relativa de variantes sustitución(es) comienza desde N-terminal aminoácidos 1 a 177 de SEC ID n.º: 3.
de proteasa. Numeración de del péptido maduro en los
Variante
Sustituciones Actividad relativa
80°C/70°C
JTP196
A27K D79L Y82F S87G A112P A126V D142L D104P 55%
JTP210
A27K Y82F S87G D104P A126V D142L A112P 36%
JTP211
A27K D79L Y82F D104P A126V D142L A112P 44%
JTP213
A27K Y82F D104P A112P D142L A126V 37%
Ejemplo 3
5 Perfil de temperatura de variantes de proteasa seleccionadas utilizando enzimas purificadas
[0138] Las variantes de proteasa seleccionadas que mostraron buena termoestabilidad fueron purificadas y las enzimas purificadas fueron usadas en un ensayo de ceína-BCA se describe más adelante. La actividad de la
10 proteasa restante fue determinada a 60°C tras la incubación de la enzima a temperaturas elevadas como se indica durante 60 min.
Ensayo de ceína-BCA:
19
imagen17
imagen18
De los resultados se puede observar que la temperatura óptima para la glucoamilasa de Penicillium oxalicum en las condiciones dadas es entre 50°C y 70°C y la glucoamilasa mantiene más del 80% de la actividad a 95°C.
5 [0147] Termoestabilidad. Para valorar la termoestabilidad de la glucoamilasa de Penicillium oxalicum el ensayo de condición de reacción fue modificado en que la solución enzimática y el tampón de acetato fue preincubado durante 15 min a 20, 30, 40, 50, 60, 70, 75, 80, 85, 90 y 95°C. Después de la incubación, 20 microL de almidón se añadió a la solución y el ensayo fue realizado como se ha descrito anteriormente.
10 [0148] Los resultados se muestran en la tabla 7.
Tabla 7 Termoestabilidad
Temperatura (°C)
20 30 40 50 60 70 80 85 90 95
Actividad relativa (%)
91,0 92,9 88,1 100,0 96,9 86,0 34,8 36,0 34,2 34,8
15 De los resultados se puede observar que la glucoamilasa de Penicillium oxalicum es estable hasta 70 °C después de la preincubación durante 15 min en que mantiene más del 80% de la actividad.
[0149] PH óptimo. Para valorar el pH óptimo de la glucoamilasa de Penicillium oxalicum, el ensayo de condición de reacción anteriormente descrito fue realizado a pH 2,0, 3,0, 3,5, 4,0, 4,5, 5,0, 6,0, 7,0, 8,0, 9,0, 10,0 y 11,0. En vez
20 de usar el tampón de acetato descrito en el ensayo de condición de reacción, se usó el siguiente tampón 100mM de ácido succínico, HEPES, CHES, CAPSO, 1mM CaCl2,150mM KCI, 0,01% Tritón X-100, pH ajustado a 2,0, 3,0, 3,5, 4,0, 4,5, 5,0, 6,0 7,0, 8,0, 9,0,10,0 o 11,0 con HCl o NaOH.
[0150] Los resultados se muestran en la tabla 8. 25 Tabla 8 pH óptimo
pH
2,0 3,0 3,5 4,0 4,5 5,0 6,0 7,0 8,0 9,0 10,0 11,0
Actividad relativa (%)
71,4 78,6 77,0 91,2 84,2 100,0 55,5 66,7 30,9 17,8 15,9 16,1
De los resultados se puede observar que la glucoamilasa de Penicillium oxalicum en las condiciones dadas tiene la 30 actividad máxima en pH 5,0. La glucoamilasa de Penicillium oxalicum es activa en un margen de pH amplio en el que mantiene más del 50% de la actividad de pH 2 a 7.
[0151] Estabilidad de pH. Para valorar la termoestabilidad de la glucoamilasa de Penicillium oxalicum, el ensayo de condición de reacción fue modificado en que la solución enzimática (50 micro g/mL) fue preincubada durante 20
35 horas en tampones con pH 2,0, 3,0, 3,5, 4,0, 4,5, 5,0, 6,0 7,0, 8,0, 9,0,10,0 y 11,0 utilizando los tampones descritos bajo pH óptimo. Después de la preincubación, 20 microL de almidón soluble a un volumen final de 100 microL se añadió a la solución y el ensayo fue realizado como se ha descrito anteriormente.
[0152] Los resultados se muestran en la tabla 9. 40 Tabla 9 estabilidad de pH
pH
2,0 3,0 3,5 4,0 4,5 5,0 6,0 7,0 8,0 9,0 10,0 11,0
Actividad relativa (%)
17,4 98,0 98,0 103,2 100,0 93,4 71,2 90,7 58,7 17,4 17,0 17,2
De los resultados se puede observar que la glucoamilasa de Penicillium oxalicum es estable de pH 3 a pH 7 45 después de la preincubación durante 20 horas y reduce su actividad a pH 8.
Ejemplo 5: evaluación de la glucoamilasa de Penicillium oxalicum en la pre-sacarificación a pH 5,0 y 70°C
[0153] Este ejemplo describe un proceso de producción de etanol donde la glucoamilasa de Penicillium oxalicum
50 termoestable se usa en un proceso de pre-sacarificación seguido de un proceso de fermentación sin usar glucoamilasa adicional. Este proceso se compara con un proceso de producción de etanol tradicional donde el proceso de licuefacción es seguido de un proceso de SSF utilizando una glucoamilasa no termoestable.
21
imagen19
imagen20

Claims (1)

  1. imagen1
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ES11768432.4T 2010-04-14 2011-04-13 Procesos para producir productos de fermentación Active ES2569033T3 (es)

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