Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus
- Autores
- Martos, M. A.; Butiuk, A. P.; Rojas, Natalia Lorena; Hours, Roque Alberto
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The aim of this work was to study the purification and physicochemical properties of an endo-polygalacturonase (PG) produced by Wickerhamomyces anomalus isolated from the citrus fruit peels. The enzyme was purified to homogeneity from the culture filtrate of W. anomalus grown on the yeast nitrogen base medium with glucose as carbon and energy source and citrus pectin as inductor. After anion-exchange chromatography and gel filtration chromatography, PG activity was eluted as a single peak, yielding 21% of the original activity. After dialysis and cation-exchange chromatography, only one fraction with PG activity was obtained, recovering 56% of initial enzyme activity and 1.3-fold increase in specific activity. The molecular weight of the enzyme was estimated as 43 kDa by the SDS-PAGE. The enzyme exhibited maximal activity at pH 4.2 and was stable over a pH range from 3.5 to 6.0 and up to 49°C for 10 h. The Vmax and Km values with polygalacturonic acid as substrate were 0.26 mmol/L. min and 0.173 mg/mL, respectively. Cations such as Cu+2, Fe+3, Mg+2, Mn+2 and Zn+2 did not show any significant effect on PG activity but K+ and Ca+2 reduced it. The purified PG was able to macerate cassava tissues.
Centro de Investigación y Desarrollo en Fermentaciones Industriales - Materia
-
Ciencias Exactas
Characterization
Polygalacturonase
Purification
Wickerhamomyces anomalus - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/85644
Ver los metadatos del registro completo
id |
SEDICI_01999068581fa4fea3f49c11ee806795 |
---|---|
oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/85644 |
network_acronym_str |
SEDICI |
repository_id_str |
1329 |
network_name_str |
SEDICI (UNLP) |
spelling |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalusMartos, M. A.Butiuk, A. P.Rojas, Natalia LorenaHours, Roque AlbertoCiencias ExactasCharacterizationPolygalacturonasePurificationWickerhamomyces anomalusThe aim of this work was to study the purification and physicochemical properties of an endo-polygalacturonase (PG) produced by Wickerhamomyces anomalus isolated from the citrus fruit peels. The enzyme was purified to homogeneity from the culture filtrate of W. anomalus grown on the yeast nitrogen base medium with glucose as carbon and energy source and citrus pectin as inductor. After anion-exchange chromatography and gel filtration chromatography, PG activity was eluted as a single peak, yielding 21% of the original activity. After dialysis and cation-exchange chromatography, only one fraction with PG activity was obtained, recovering 56% of initial enzyme activity and 1.3-fold increase in specific activity. The molecular weight of the enzyme was estimated as 43 kDa by the SDS-PAGE. The enzyme exhibited maximal activity at pH 4.2 and was stable over a pH range from 3.5 to 6.0 and up to 49°C for 10 h. The Vmax and Km values with polygalacturonic acid as substrate were 0.26 mmol/L. min and 0.173 mg/mL, respectively. Cations such as Cu+2, Fe+3, Mg+2, Mn+2 and Zn+2 did not show any significant effect on PG activity but K+ and Ca+2 reduced it. The purified PG was able to macerate cassava tissues.Centro de Investigación y Desarrollo en Fermentaciones Industriales2014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf587-594http://sedici.unlp.edu.ar/handle/10915/85644enginfo:eu-repo/semantics/altIdentifier/issn/1516-8913info:eu-repo/semantics/altIdentifier/doi/10.1590/S1516-8913201402214info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:48:41Zoai:sedici.unlp.edu.ar:10915/85644Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:48:42.073SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
title |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
spellingShingle |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus Martos, M. A. Ciencias Exactas Characterization Polygalacturonase Purification Wickerhamomyces anomalus |
title_short |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
title_full |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
title_fullStr |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
title_full_unstemmed |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
title_sort |
Purification and characterization of a polygalacturonase produced by Wickerhamomyces anomalus |
dc.creator.none.fl_str_mv |
Martos, M. A. Butiuk, A. P. Rojas, Natalia Lorena Hours, Roque Alberto |
author |
Martos, M. A. |
author_facet |
Martos, M. A. Butiuk, A. P. Rojas, Natalia Lorena Hours, Roque Alberto |
author_role |
author |
author2 |
Butiuk, A. P. Rojas, Natalia Lorena Hours, Roque Alberto |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Ciencias Exactas Characterization Polygalacturonase Purification Wickerhamomyces anomalus |
topic |
Ciencias Exactas Characterization Polygalacturonase Purification Wickerhamomyces anomalus |
dc.description.none.fl_txt_mv |
The aim of this work was to study the purification and physicochemical properties of an endo-polygalacturonase (PG) produced by Wickerhamomyces anomalus isolated from the citrus fruit peels. The enzyme was purified to homogeneity from the culture filtrate of W. anomalus grown on the yeast nitrogen base medium with glucose as carbon and energy source and citrus pectin as inductor. After anion-exchange chromatography and gel filtration chromatography, PG activity was eluted as a single peak, yielding 21% of the original activity. After dialysis and cation-exchange chromatography, only one fraction with PG activity was obtained, recovering 56% of initial enzyme activity and 1.3-fold increase in specific activity. The molecular weight of the enzyme was estimated as 43 kDa by the SDS-PAGE. The enzyme exhibited maximal activity at pH 4.2 and was stable over a pH range from 3.5 to 6.0 and up to 49°C for 10 h. The Vmax and Km values with polygalacturonic acid as substrate were 0.26 mmol/L. min and 0.173 mg/mL, respectively. Cations such as Cu+2, Fe+3, Mg+2, Mn+2 and Zn+2 did not show any significant effect on PG activity but K+ and Ca+2 reduced it. The purified PG was able to macerate cassava tissues. Centro de Investigación y Desarrollo en Fermentaciones Industriales |
description |
The aim of this work was to study the purification and physicochemical properties of an endo-polygalacturonase (PG) produced by Wickerhamomyces anomalus isolated from the citrus fruit peels. The enzyme was purified to homogeneity from the culture filtrate of W. anomalus grown on the yeast nitrogen base medium with glucose as carbon and energy source and citrus pectin as inductor. After anion-exchange chromatography and gel filtration chromatography, PG activity was eluted as a single peak, yielding 21% of the original activity. After dialysis and cation-exchange chromatography, only one fraction with PG activity was obtained, recovering 56% of initial enzyme activity and 1.3-fold increase in specific activity. The molecular weight of the enzyme was estimated as 43 kDa by the SDS-PAGE. The enzyme exhibited maximal activity at pH 4.2 and was stable over a pH range from 3.5 to 6.0 and up to 49°C for 10 h. The Vmax and Km values with polygalacturonic acid as substrate were 0.26 mmol/L. min and 0.173 mg/mL, respectively. Cations such as Cu+2, Fe+3, Mg+2, Mn+2 and Zn+2 did not show any significant effect on PG activity but K+ and Ca+2 reduced it. The purified PG was able to macerate cassava tissues. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014 |
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/10915/85644 |
url |
http://sedici.unlp.edu.ar/handle/10915/85644 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/1516-8913 info:eu-repo/semantics/altIdentifier/doi/10.1590/S1516-8913201402214 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 587-594 |
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 |
_version_ |
1842260362938810368 |
score |
13.13397 |