Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>

Autores
Martos, María Alicia; Baumann, Alicia; Cruz, Mónica Nancy; Hours, Roque Alberto; Garro, Oscar Alfredo
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aspergillus niger, isolated from decay citrus peels in the province of Misiones, was able to produce pectinases by submerged fermentation. The enzymatic extract exhibited polygalacturonase, pectinesterase and lyase activities. Others enzymes capable of degrading cell wall polymers were also detected in the enzymatic extract such as cellulases and xylanases. Polygalacturonase was an endo-polygalacturonase. The enzyme exhibited a maximal activity at pH range between 4.5 to 5.0, was stable in the pH range from 2.5 to 5.5 and remained unchanged when was incubated at temperatures lower than 50 ºC. The fungi produced three PG isoenzymes. The enzymatic extract was able to clarify apple juice. The results observed make the pectinolytic enzymes produced by A. niger appropriate for future application in fruit juice processing industries.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Ciencias Exactas
Aspergillus niger
Pectinolytic enzymes
Polygalacturonase
Biotecnología
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/96852
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/96852
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>Martos, María AliciaBaumann, AliciaCruz, Mónica NancyHours, Roque AlbertoGarro, Oscar AlfredoCiencias ExactasAspergillus nigerPectinolytic enzymesPolygalacturonaseBiotecnologíaAspergillus niger, isolated from decay citrus peels in the province of Misiones, was able to produce pectinases by submerged fermentation. The enzymatic extract exhibited polygalacturonase, pectinesterase and lyase activities. Others enzymes capable of degrading cell wall polymers were also detected in the enzymatic extract such as cellulases and xylanases. Polygalacturonase was an endo-polygalacturonase. The enzyme exhibited a maximal activity at pH range between 4.5 to 5.0, was stable in the pH range from 2.5 to 5.5 and remained unchanged when was incubated at temperatures lower than 50 ºC. The fungi produced three PG isoenzymes. The enzymatic extract was able to clarify apple juice. The results observed make the pectinolytic enzymes produced by A. niger appropriate for future application in fruit juice processing industries.Centro de Investigación y Desarrollo en Fermentaciones Industriales2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf917-932http://sedici.unlp.edu.ar/handle/10915/96852enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/82969info:eu-repo/semantics/altIdentifier/url/https://www.jmbfs.org/jmbfs_0146_martos/?issue_id=1574&article_id=6info:eu-repo/semantics/altIdentifier/issn/1338-5178info:eu-repo/semantics/altIdentifier/hdl/11336/82969info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-11-05T12:59:48Zoai:sedici.unlp.edu.ar:10915/96852Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-11-05 12:59:48.559SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
title Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
spellingShingle Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
Martos, María Alicia
Ciencias Exactas
Aspergillus niger
Pectinolytic enzymes
Polygalacturonase
Biotecnología
title_short Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
title_full Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
title_fullStr Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
title_full_unstemmed Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
title_sort Partial characterization of enzymatic activities produced by a wild strain of <i>A. niger</i>
dc.creator.none.fl_str_mv Martos, María Alicia
Baumann, Alicia
Cruz, Mónica Nancy
Hours, Roque Alberto
Garro, Oscar Alfredo
author Martos, María Alicia
author_facet Martos, María Alicia
Baumann, Alicia
Cruz, Mónica Nancy
Hours, Roque Alberto
Garro, Oscar Alfredo
author_role author
author2 Baumann, Alicia
Cruz, Mónica Nancy
Hours, Roque Alberto
Garro, Oscar Alfredo
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Aspergillus niger
Pectinolytic enzymes
Polygalacturonase
Biotecnología
topic Ciencias Exactas
Aspergillus niger
Pectinolytic enzymes
Polygalacturonase
Biotecnología
dc.description.none.fl_txt_mv Aspergillus niger, isolated from decay citrus peels in the province of Misiones, was able to produce pectinases by submerged fermentation. The enzymatic extract exhibited polygalacturonase, pectinesterase and lyase activities. Others enzymes capable of degrading cell wall polymers were also detected in the enzymatic extract such as cellulases and xylanases. Polygalacturonase was an endo-polygalacturonase. The enzyme exhibited a maximal activity at pH range between 4.5 to 5.0, was stable in the pH range from 2.5 to 5.5 and remained unchanged when was incubated at temperatures lower than 50 ºC. The fungi produced three PG isoenzymes. The enzymatic extract was able to clarify apple juice. The results observed make the pectinolytic enzymes produced by A. niger appropriate for future application in fruit juice processing industries.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description Aspergillus niger, isolated from decay citrus peels in the province of Misiones, was able to produce pectinases by submerged fermentation. The enzymatic extract exhibited polygalacturonase, pectinesterase and lyase activities. Others enzymes capable of degrading cell wall polymers were also detected in the enzymatic extract such as cellulases and xylanases. Polygalacturonase was an endo-polygalacturonase. The enzyme exhibited a maximal activity at pH range between 4.5 to 5.0, was stable in the pH range from 2.5 to 5.5 and remained unchanged when was incubated at temperatures lower than 50 ºC. The fungi produced three PG isoenzymes. The enzymatic extract was able to clarify apple juice. The results observed make the pectinolytic enzymes produced by A. niger appropriate for future application in fruit juice processing industries.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/96852
url http://sedici.unlp.edu.ar/handle/10915/96852
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/82969
info:eu-repo/semantics/altIdentifier/url/https://www.jmbfs.org/jmbfs_0146_martos/?issue_id=1574&article_id=6
info:eu-repo/semantics/altIdentifier/issn/1338-5178
info:eu-repo/semantics/altIdentifier/hdl/11336/82969
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
917-932
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 12.61048

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