Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii

Autores
Contreras Esquivel, J.C.; Voget, Claudio Enrique
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An endo-polygalacturonase, named PGI, was purified to homogeneity from the culture filtrate of Aspergillus kawachii IFO 4033 grown in a glucose-tryptone medium. The molecular mass of PGI was estimated to be 60kDa by SDS-PAGE and 40kDa by gel filtration on Sephacryl S-100. The isoelectric point was 3.55 as determined by isoelectic focusing. PGI exhibited binding properties to ConA-Sepharose suggesting that the protein is glycosylated. The N-terminal amino acid sequence was also determined as S-T-C-T-F-T-D-A-A-T-A-S-E-S-K. The remarkable property of PGI was its high activity in the pH range 2.0-3.0 towards soluble and insoluble substrates, while being inactive at pH 5.0. Enzyme stability at low pHs was markedly enhanced by different compounds, such as proteins, polysaccharides, simple sugars and the substrate pectin. PGI was very efficient to extract pectin from lemmon protopectin and to macerate carrot tissues at pH 2.0. These properties make PGI an interesting biocatalyst for industrial applications under highly acidic conditions.
Fil: Contreras Esquivel, J.C.. Universidad Autonoma de Coahuila; México
Fil: Voget, Claudio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
Materia
ACIDIC ENZYMES
ASPERGILLUS KAWACHII
ENDO-POLYGALACTURONASE
PECTIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/100677
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachiiContreras Esquivel, J.C.Voget, Claudio EnriqueACIDIC ENZYMESASPERGILLUS KAWACHIIENDO-POLYGALACTURONASEPECTINhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2An endo-polygalacturonase, named PGI, was purified to homogeneity from the culture filtrate of Aspergillus kawachii IFO 4033 grown in a glucose-tryptone medium. The molecular mass of PGI was estimated to be 60kDa by SDS-PAGE and 40kDa by gel filtration on Sephacryl S-100. The isoelectric point was 3.55 as determined by isoelectic focusing. PGI exhibited binding properties to ConA-Sepharose suggesting that the protein is glycosylated. The N-terminal amino acid sequence was also determined as S-T-C-T-F-T-D-A-A-T-A-S-E-S-K. The remarkable property of PGI was its high activity in the pH range 2.0-3.0 towards soluble and insoluble substrates, while being inactive at pH 5.0. Enzyme stability at low pHs was markedly enhanced by different compounds, such as proteins, polysaccharides, simple sugars and the substrate pectin. PGI was very efficient to extract pectin from lemmon protopectin and to macerate carrot tissues at pH 2.0. These properties make PGI an interesting biocatalyst for industrial applications under highly acidic conditions.Fil: Contreras Esquivel, J.C.. Universidad Autonoma de Coahuila; MéxicoFil: Voget, Claudio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaElsevier Science2004-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/100677Contreras Esquivel, J.C.; Voget, Claudio Enrique; Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii; Elsevier Science; Journal of Biotechnology; 110; 1; 5-2004; 21-280168-1656CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0168165604000616info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2004.01.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:27:51Zoai:ri.conicet.gov.ar:11336/100677instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:27:52.122CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
title Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
spellingShingle Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
Contreras Esquivel, J.C.
ACIDIC ENZYMES
ASPERGILLUS KAWACHII
ENDO-POLYGALACTURONASE
PECTIN
title_short Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
title_full Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
title_fullStr Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
title_full_unstemmed Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
title_sort Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
dc.creator.none.fl_str_mv Contreras Esquivel, J.C.
Voget, Claudio Enrique
author Contreras Esquivel, J.C.
author_facet Contreras Esquivel, J.C.
Voget, Claudio Enrique
author_role author
author2 Voget, Claudio Enrique
author2_role author
dc.subject.none.fl_str_mv ACIDIC ENZYMES
ASPERGILLUS KAWACHII
ENDO-POLYGALACTURONASE
PECTIN
topic ACIDIC ENZYMES
ASPERGILLUS KAWACHII
ENDO-POLYGALACTURONASE
PECTIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv An endo-polygalacturonase, named PGI, was purified to homogeneity from the culture filtrate of Aspergillus kawachii IFO 4033 grown in a glucose-tryptone medium. The molecular mass of PGI was estimated to be 60kDa by SDS-PAGE and 40kDa by gel filtration on Sephacryl S-100. The isoelectric point was 3.55 as determined by isoelectic focusing. PGI exhibited binding properties to ConA-Sepharose suggesting that the protein is glycosylated. The N-terminal amino acid sequence was also determined as S-T-C-T-F-T-D-A-A-T-A-S-E-S-K. The remarkable property of PGI was its high activity in the pH range 2.0-3.0 towards soluble and insoluble substrates, while being inactive at pH 5.0. Enzyme stability at low pHs was markedly enhanced by different compounds, such as proteins, polysaccharides, simple sugars and the substrate pectin. PGI was very efficient to extract pectin from lemmon protopectin and to macerate carrot tissues at pH 2.0. These properties make PGI an interesting biocatalyst for industrial applications under highly acidic conditions.
Fil: Contreras Esquivel, J.C.. Universidad Autonoma de Coahuila; México
Fil: Voget, Claudio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
description An endo-polygalacturonase, named PGI, was purified to homogeneity from the culture filtrate of Aspergillus kawachii IFO 4033 grown in a glucose-tryptone medium. The molecular mass of PGI was estimated to be 60kDa by SDS-PAGE and 40kDa by gel filtration on Sephacryl S-100. The isoelectric point was 3.55 as determined by isoelectic focusing. PGI exhibited binding properties to ConA-Sepharose suggesting that the protein is glycosylated. The N-terminal amino acid sequence was also determined as S-T-C-T-F-T-D-A-A-T-A-S-E-S-K. The remarkable property of PGI was its high activity in the pH range 2.0-3.0 towards soluble and insoluble substrates, while being inactive at pH 5.0. Enzyme stability at low pHs was markedly enhanced by different compounds, such as proteins, polysaccharides, simple sugars and the substrate pectin. PGI was very efficient to extract pectin from lemmon protopectin and to macerate carrot tissues at pH 2.0. These properties make PGI an interesting biocatalyst for industrial applications under highly acidic conditions.
publishDate 2004
dc.date.none.fl_str_mv 2004-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/100677
Contreras Esquivel, J.C.; Voget, Claudio Enrique; Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii; Elsevier Science; Journal of Biotechnology; 110; 1; 5-2004; 21-28
0168-1656
CONICET Digital
CONICET
url http://hdl.handle.net/11336/100677
identifier_str_mv Contreras Esquivel, J.C.; Voget, Claudio Enrique; Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii; Elsevier Science; Journal of Biotechnology; 110; 1; 5-2004; 21-28
0168-1656
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0168165604000616
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2004.01.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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