Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase

Abstract: Aspergillus niger HPD-2 has interesting growth characteristics, it grows at a temperature of 38 ºC and pH of 3, it is also known that it produces various enzymes of commercial interest such as glucoamylase, which is present in the medium even under non-inducible conditions and has importan...

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Autores: Pérez Rodríguez, Fernando, Pliego-Arreaga, Raquel, Silva-Martínez, Guillermo Antonio, Cervantes-Montelongo, Juan Antonio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:México
Institución:UNIVERSIDAD DE SONORA
Repositorio:Biotecnia
Idioma:inglés
OAI Identifier:oai:oai.biotecnia.unison.mx:article/2024
Acceso en línea:https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024
Access Level:acceso abierto
Palabra clave:Glucoamylase
A. niger
Biochemical characterization
Molecular characterization
Enzyme kinetic
Glucoamilasa
caracterización molecular
caracterización bioquímica
cinética enzimática
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spelling Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylaseCaracterización bioquímica y molecular de la glucoamilasa producida por la cepa de Aspergillus niger HPD-2: Caracterización bioquímica y molecular de la glucoamilasa Pérez Rodríguez, FernandoPliego-Arreaga, RaquelSilva-Martínez, Guillermo AntonioCervantes-Montelongo, Juan AntonioGlucoamylaseA. nigerBiochemical characterizationMolecular characterizationEnzyme kineticGlucoamilasaA. nigercaracterización molecularcaracterización bioquímicacinética enzimáticaAbstract: Aspergillus niger HPD-2 has interesting growth characteristics, it grows at a temperature of 38 ºC and pH of 3, it is also known that it produces various enzymes of commercial interest such as glucoamylase, which is present in the medium even under non-inducible conditions and has important activity characteristics such as an optimum temperature of 70 ºC and an optimum pH of 3-4. These features are very important because they will help to minimize microbial contamination risk in industrial hydrolysis processes. For the characterization of A. niger HPD-2 glucoamylase, the presence and activity of the enzyme were verified in a non-inducing medium. The apparent kinetic parameters Km, Ki and Vmax were determined, 6.66 mM, 0.601 M and 66.5 mM/min respectively. As well as its optimum pH and temperature activity (pH 3 and 70 °C). Comparatively speaking, these data are competitive against those reported for similar purified enzymes. On the other hand, DNA sequence analysis of A. niger HPD-2 glucoamylase gene showed no changes in the promoter region or starch-binding domains. Therefore, the presence of the enzyme in a non-inducing medium could be related to changes in a repressor protein CreA.    Resumen: Aspergillus niger HPD-2 presenta características particulares de cultivo, crece a una temperatura de 38 ºC y a un pH de 3, además se sabe que produce diversas enzimas de interés comercial como la glucoamilasa, que se encuentra presente en el medio aún bajo condiciones no inducibles y tiene características de actividad interesantes como son, una temperatura óptima de 70 ºC y un pH óptimo de 3-4. Estas características son muy importantes porque ayudarán a minimizar el riesgo de contaminación microbiana en procesos de hidrólisis industrial. Para la caracterización de la glucoamilasa de A. niger HPD-2 se comprobó la presencia y actividad de la enzima en un medio no inductor. Se determinaron los parámetros cinéticos aparentes Km, Ki, y Vmax, 6.66 mM, 0.601 M y 66.5 mM/min respectivamente, así como su temperatura y pH óptimos de actividad (pH 3 y 70 °C). Comparativamente hablando, estos datos son bastante competitivos que aquellos reportados para enzimas similares purificadas. Por otro lado, el análisis de la secuencia de ADN del gen de la glucoamilasa de A. niger HPD-2 mostró que no existen cambios en la región promotora ni en los dominios de unión al almidón. Por lo que la presencia de la enzima en un medio no inductor podría estar relacionada con cambios en una proteína represora CreA.Universidad de Sonora2023-12-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionOriginal peer-reviewed articlesArtículos originales evaluados por paresapplication/pdftext/htmltext/xmlhttps://biotecnia.unison.mx/index.php/biotecnia/article/view/202410.18633/biotecnia.v26i1.2024Biotecnia; Vol. 26 (2024): January - December; 5-15Biotecnia; Vol. 26 (2024): Enero - Diciembre; 5-151665-14561665-1456reponame:Biotecniainstname:UNIVERSIDAD DE SONORAinstacron:UNISONenghttps://biotecnia.unison.mx/index.php/biotecnia/article/view/2024/982https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024/983https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024/1131Derechos de autor 2023 https://creativecommons.org/licenses/by-nc-sa/4.0info:eu-repo/semantics/openAccessoai:oai.biotecnia.unison.mx:article/20242024-08-19T18:52:22Z
dc.title.none.fl_str_mv Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
Caracterización bioquímica y molecular de la glucoamilasa producida por la cepa de Aspergillus niger HPD-2: Caracterización bioquímica y molecular de la glucoamilasa
title Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
spellingShingle Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
Pérez Rodríguez, Fernando
Glucoamylase
A. niger
Biochemical characterization
Molecular characterization
Enzyme kinetic
Glucoamilasa
A. niger
caracterización molecular
caracterización bioquímica
cinética enzimática
title_short Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
title_full Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
title_fullStr Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
title_full_unstemmed Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
title_sort Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2: Biochemical and molecular characterization of glucoamylase
dc.creator.none.fl_str_mv Pérez Rodríguez, Fernando
Pliego-Arreaga, Raquel
Silva-Martínez, Guillermo Antonio
Cervantes-Montelongo, Juan Antonio
author Pérez Rodríguez, Fernando
author_facet Pérez Rodríguez, Fernando
Pliego-Arreaga, Raquel
Silva-Martínez, Guillermo Antonio
Cervantes-Montelongo, Juan Antonio
author_role author
author2 Pliego-Arreaga, Raquel
Silva-Martínez, Guillermo Antonio
Cervantes-Montelongo, Juan Antonio
author2_role author
author
author
dc.subject.none.fl_str_mv Glucoamylase
A. niger
Biochemical characterization
Molecular characterization
Enzyme kinetic
Glucoamilasa
A. niger
caracterización molecular
caracterización bioquímica
cinética enzimática
topic Glucoamylase
A. niger
Biochemical characterization
Molecular characterization
Enzyme kinetic
Glucoamilasa
A. niger
caracterización molecular
caracterización bioquímica
cinética enzimática
description Abstract: Aspergillus niger HPD-2 has interesting growth characteristics, it grows at a temperature of 38 ºC and pH of 3, it is also known that it produces various enzymes of commercial interest such as glucoamylase, which is present in the medium even under non-inducible conditions and has important activity characteristics such as an optimum temperature of 70 ºC and an optimum pH of 3-4. These features are very important because they will help to minimize microbial contamination risk in industrial hydrolysis processes. For the characterization of A. niger HPD-2 glucoamylase, the presence and activity of the enzyme were verified in a non-inducing medium. The apparent kinetic parameters Km, Ki and Vmax were determined, 6.66 mM, 0.601 M and 66.5 mM/min respectively. As well as its optimum pH and temperature activity (pH 3 and 70 °C). Comparatively speaking, these data are competitive against those reported for similar purified enzymes. On the other hand, DNA sequence analysis of A. niger HPD-2 glucoamylase gene showed no changes in the promoter region or starch-binding domains. Therefore, the presence of the enzyme in a non-inducing medium could be related to changes in a repressor protein CreA.    
publishDate 2023
dc.date.none.fl_str_mv 2023-12-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Original peer-reviewed articles
Artículos originales evaluados por pares
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024
10.18633/biotecnia.v26i1.2024
url https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024
identifier_str_mv 10.18633/biotecnia.v26i1.2024
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024/982
https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024/983
https://biotecnia.unison.mx/index.php/biotecnia/article/view/2024/1131
dc.rights.none.fl_str_mv Derechos de autor 2023
https://creativecommons.org/licenses/by-nc-sa/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Derechos de autor 2023
https://creativecommons.org/licenses/by-nc-sa/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
text/html
text/xml
dc.publisher.none.fl_str_mv Universidad de Sonora
publisher.none.fl_str_mv Universidad de Sonora
dc.source.none.fl_str_mv Biotecnia; Vol. 26 (2024): January - December; 5-15
Biotecnia; Vol. 26 (2024): Enero - Diciembre; 5-15
1665-1456
1665-1456
reponame:Biotecnia
instname:UNIVERSIDAD DE SONORA
instacron:UNISON
instname_str UNIVERSIDAD DE SONORA
instacron_str UNISON
institution UNISON
reponame_str Biotecnia
collection Biotecnia
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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