Purification and characterization of an exo-polygalacturonase

Autores
Quiroga, Emma Nelly; Sgariglia, Melina Araceli; Molina, César F.; Sampietro, Diego Alejandro; Soberon, Jose Rodolfo; Vattuone, Marta Amelia
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The present work describes the purification and characterization of a novel extracellular polygalacturonase, PGase I, produced by Pycnoporus sanguineus when grown on citrus fruit pectin. This substrate gave enhanced enzyme production as compared to sucrose and lactose. PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product as determined by TLC and orcinol-sulphuric acid staining. Its capacity to hydrolyze digalacturonate identified PGase I as an exo-polygalacturonase. SDS-PAGE showed that PGase I is an N-glycosidated monomer. The enzyme has a molecular mass of 42 kDa, optimum pH 4.8 and stability between pH 3.8 and 8.0. A temperature optimum was observed at 50–60 °C, with some enzyme activity retained up to 80 °C. Its activation energy was 5.352 cal mol−1. PGase I showed a higher affinity towards PGA than citric pectin (Km = 0.55 ± 0.02 and 0.72 ± 0.02 mg ml−1, respectively). Consequently, PGase I is an exo-PGase, EC 3.2.1.82.
Fil: Quiroga, Emma Nelly. Universidad Nacional de Tucumán; Argentina
Fil: Sgariglia, Melina Araceli. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Fil: Molina, César F.. Universidad Nacional de Tucumán; Argentina
Fil: Sampietro, Diego Alejandro. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Fil: Soberon, Jose Rodolfo. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Fil: Vattuone, Marta Amelia. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Materia
Characterization
Exo-Polygalacturonase
Purification
Pycnoporus Sanguineus
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:11336/78059
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/78059
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Purification and characterization of an exo-polygalacturonaseQuiroga, Emma NellySgariglia, Melina AraceliMolina, César F.Sampietro, Diego AlejandroSoberon, Jose RodolfoVattuone, Marta AmeliaCharacterizationExo-PolygalacturonasePurificationPycnoporus Sanguineushttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The present work describes the purification and characterization of a novel extracellular polygalacturonase, PGase I, produced by Pycnoporus sanguineus when grown on citrus fruit pectin. This substrate gave enhanced enzyme production as compared to sucrose and lactose. PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product as determined by TLC and orcinol-sulphuric acid staining. Its capacity to hydrolyze digalacturonate identified PGase I as an exo-polygalacturonase. SDS-PAGE showed that PGase I is an N-glycosidated monomer. The enzyme has a molecular mass of 42 kDa, optimum pH 4.8 and stability between pH 3.8 and 8.0. A temperature optimum was observed at 50–60 °C, with some enzyme activity retained up to 80 °C. Its activation energy was 5.352 cal mol−1. PGase I showed a higher affinity towards PGA than citric pectin (Km = 0.55 ± 0.02 and 0.72 ± 0.02 mg ml−1, respectively). Consequently, PGase I is an exo-PGase, EC 3.2.1.82.Fil: Quiroga, Emma Nelly. Universidad Nacional de Tucumán; ArgentinaFil: Sgariglia, Melina Araceli. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; ArgentinaFil: Molina, César F.. Universidad Nacional de Tucumán; ArgentinaFil: Sampietro, Diego Alejandro. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; ArgentinaFil: Soberon, Jose Rodolfo. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; ArgentinaFil: Vattuone, Marta Amelia. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; ArgentinaElsevier2009-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/78059Quiroga, Emma Nelly; Sgariglia, Melina Araceli; Molina, César F.; Sampietro, Diego Alejandro; Soberon, Jose Rodolfo; et al.; Purification and characterization of an exo-polygalacturonase; Elsevier; Mycological Research; 113; 12; 9-2009; 1404-14100953-7562CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0953756209001853info:eu-repo/semantics/altIdentifier/doi/10.1016/j.mycres.2009.09.007info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:13:24Zoai:ri.conicet.gov.ar:11336/78059instacron: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:34982025-10-15 15:13:24.707CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Purification and characterization of an exo-polygalacturonase
title Purification and characterization of an exo-polygalacturonase
spellingShingle Purification and characterization of an exo-polygalacturonase
Quiroga, Emma Nelly
Characterization
Exo-Polygalacturonase
Purification
Pycnoporus Sanguineus
title_short Purification and characterization of an exo-polygalacturonase
title_full Purification and characterization of an exo-polygalacturonase
title_fullStr Purification and characterization of an exo-polygalacturonase
title_full_unstemmed Purification and characterization of an exo-polygalacturonase
title_sort Purification and characterization of an exo-polygalacturonase
dc.creator.none.fl_str_mv Quiroga, Emma Nelly
Sgariglia, Melina Araceli
Molina, César F.
Sampietro, Diego Alejandro
Soberon, Jose Rodolfo
Vattuone, Marta Amelia
author Quiroga, Emma Nelly
author_facet Quiroga, Emma Nelly
Sgariglia, Melina Araceli
Molina, César F.
Sampietro, Diego Alejandro
Soberon, Jose Rodolfo
Vattuone, Marta Amelia
author_role author
author2 Sgariglia, Melina Araceli
Molina, César F.
Sampietro, Diego Alejandro
Soberon, Jose Rodolfo
Vattuone, Marta Amelia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Characterization
Exo-Polygalacturonase
Purification
Pycnoporus Sanguineus
topic Characterization
Exo-Polygalacturonase
Purification
Pycnoporus Sanguineus
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The present work describes the purification and characterization of a novel extracellular polygalacturonase, PGase I, produced by Pycnoporus sanguineus when grown on citrus fruit pectin. This substrate gave enhanced enzyme production as compared to sucrose and lactose. PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product as determined by TLC and orcinol-sulphuric acid staining. Its capacity to hydrolyze digalacturonate identified PGase I as an exo-polygalacturonase. SDS-PAGE showed that PGase I is an N-glycosidated monomer. The enzyme has a molecular mass of 42 kDa, optimum pH 4.8 and stability between pH 3.8 and 8.0. A temperature optimum was observed at 50–60 °C, with some enzyme activity retained up to 80 °C. Its activation energy was 5.352 cal mol−1. PGase I showed a higher affinity towards PGA than citric pectin (Km = 0.55 ± 0.02 and 0.72 ± 0.02 mg ml−1, respectively). Consequently, PGase I is an exo-PGase, EC 3.2.1.82.
Fil: Quiroga, Emma Nelly. Universidad Nacional de Tucumán; Argentina
Fil: Sgariglia, Melina Araceli. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Fil: Molina, César F.. Universidad Nacional de Tucumán; Argentina
Fil: Sampietro, Diego Alejandro. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Fil: Soberon, Jose Rodolfo. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
Fil: Vattuone, Marta Amelia. Universidad Nacional de Tucumán; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán; Argentina
description The present work describes the purification and characterization of a novel extracellular polygalacturonase, PGase I, produced by Pycnoporus sanguineus when grown on citrus fruit pectin. This substrate gave enhanced enzyme production as compared to sucrose and lactose. PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product as determined by TLC and orcinol-sulphuric acid staining. Its capacity to hydrolyze digalacturonate identified PGase I as an exo-polygalacturonase. SDS-PAGE showed that PGase I is an N-glycosidated monomer. The enzyme has a molecular mass of 42 kDa, optimum pH 4.8 and stability between pH 3.8 and 8.0. A temperature optimum was observed at 50–60 °C, with some enzyme activity retained up to 80 °C. Its activation energy was 5.352 cal mol−1. PGase I showed a higher affinity towards PGA than citric pectin (Km = 0.55 ± 0.02 and 0.72 ± 0.02 mg ml−1, respectively). Consequently, PGase I is an exo-PGase, EC 3.2.1.82.
publishDate 2009
dc.date.none.fl_str_mv 2009-09
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/11336/78059
Quiroga, Emma Nelly; Sgariglia, Melina Araceli; Molina, César F.; Sampietro, Diego Alejandro; Soberon, Jose Rodolfo; et al.; Purification and characterization of an exo-polygalacturonase; Elsevier; Mycological Research; 113; 12; 9-2009; 1404-1410
0953-7562
CONICET Digital
CONICET
url http://hdl.handle.net/11336/78059
identifier_str_mv Quiroga, Emma Nelly; Sgariglia, Melina Araceli; Molina, César F.; Sampietro, Diego Alejandro; Soberon, Jose Rodolfo; et al.; Purification and characterization of an exo-polygalacturonase; Elsevier; Mycological Research; 113; 12; 9-2009; 1404-1410
0953-7562
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://www.sciencedirect.com/science/article/pii/S0953756209001853
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.mycres.2009.09.007
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.22299

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