Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)

Autores
Pérez, Aurora; Carvajal, Carol; Trejo, Sebastián Alejandro; Figuerero Torres, María José; Martin, María Inés; Lorenzo, José Carlos; Natalucci, Claudia Luisa; Hernández, Martha
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Penduliflorain I, a new plant endopeptidase, was isolated and characterized from Hohenbergia penduliflora. Crude extract was obtained from stems. A partially purified enzyme preparation was obtained by ethanol precipitation. This preparation showed maximum activity between pH 7.5 and 8.5, was stable at ionic strength (20% decrease in proteolytic activity could be detected after 2 h in 0.4 M sodium chloride solution), and exhibited high thermal stability (inactivation required heating for 20 min at 75 °C). Inhibition and activation assays indicated the cysteine nature of the enzymatic preparation. Penduliflorain I was purified by anion exchange chromatography (Q-Sepharose HP) by FPLC system. Homogeneity was confirmed by mass spectroscopy. Molecular mass of the enzyme was 23 412.847 Da (MALDI-TOF–MS). Kinetic parameters were determined for PFLNA (Kₘ = 0.3227 mM and kcat = 4.27 s⁻¹). The N-terminal sequence (AVPQSIDWRDYGAVTTDKNQ) of isolated protease showed considerable similarity to other cysteine proteases obtained from stems or fruits of different Bromeliaceae species.
Centro de Investigación de Proteínas Vegetales
Materia
Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
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:10915/137088
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/137088
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)Pérez, AuroraCarvajal, CarolTrejo, Sebastián AlejandroFiguerero Torres, María JoséMartin, María InésLorenzo, José CarlosNatalucci, Claudia LuisaHernández, MarthaCiencias ExactasBiologíaBromeliaceaeHohenbergia pendulifloraChromatography purificationStemsThiol proteasesPenduliflorain I, a new plant endopeptidase, was isolated and characterized from <i>Hohenbergia penduliflora</i>. Crude extract was obtained from stems. A partially purified enzyme preparation was obtained by ethanol precipitation. This preparation showed maximum activity between pH 7.5 and 8.5, was stable at ionic strength (20% decrease in proteolytic activity could be detected after 2 h in 0.4 M sodium chloride solution), and exhibited high thermal stability (inactivation required heating for 20 min at 75 °C). Inhibition and activation assays indicated the cysteine nature of the enzymatic preparation. Penduliflorain I was purified by anion exchange chromatography (Q-Sepharose HP) by FPLC system. Homogeneity was confirmed by mass spectroscopy. Molecular mass of the enzyme was 23 412.847 Da (MALDI-TOF–MS). Kinetic parameters were determined for PFLNA (Kₘ = 0.3227 mM and k<sub>cat</sub> = 4.27 s⁻¹). The N-terminal sequence (AVPQSIDWRDYGAVTTDKNQ) of isolated protease showed considerable similarity to other cysteine proteases obtained from stems or fruits of different <i>Bromeliaceae</i> species.Centro de Investigación de Proteínas Vegetales2010-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf225-233http://sedici.unlp.edu.ar/handle/10915/137088enginfo:eu-repo/semantics/altIdentifier/issn/1572-3887info:eu-repo/semantics/altIdentifier/issn/1573-4943info:eu-repo/semantics/altIdentifier/doi/10.1007/s10930-010-9243-7info:eu-repo/semantics/altIdentifier/pmid/20521163info: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:UNLP2025-10-15T11:23:53Zoai:sedici.unlp.edu.ar:10915/137088Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:23:53.947SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
title Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
spellingShingle Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
Pérez, Aurora
Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
title_short Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
title_full Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
title_fullStr Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
title_full_unstemmed Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
title_sort Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
dc.creator.none.fl_str_mv Pérez, Aurora
Carvajal, Carol
Trejo, Sebastián Alejandro
Figuerero Torres, María José
Martin, María Inés
Lorenzo, José Carlos
Natalucci, Claudia Luisa
Hernández, Martha
author Pérez, Aurora
author_facet Pérez, Aurora
Carvajal, Carol
Trejo, Sebastián Alejandro
Figuerero Torres, María José
Martin, María Inés
Lorenzo, José Carlos
Natalucci, Claudia Luisa
Hernández, Martha
author_role author
author2 Carvajal, Carol
Trejo, Sebastián Alejandro
Figuerero Torres, María José
Martin, María Inés
Lorenzo, José Carlos
Natalucci, Claudia Luisa
Hernández, Martha
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
topic Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
dc.description.none.fl_txt_mv Penduliflorain I, a new plant endopeptidase, was isolated and characterized from <i>Hohenbergia penduliflora</i>. Crude extract was obtained from stems. A partially purified enzyme preparation was obtained by ethanol precipitation. This preparation showed maximum activity between pH 7.5 and 8.5, was stable at ionic strength (20% decrease in proteolytic activity could be detected after 2 h in 0.4 M sodium chloride solution), and exhibited high thermal stability (inactivation required heating for 20 min at 75 °C). Inhibition and activation assays indicated the cysteine nature of the enzymatic preparation. Penduliflorain I was purified by anion exchange chromatography (Q-Sepharose HP) by FPLC system. Homogeneity was confirmed by mass spectroscopy. Molecular mass of the enzyme was 23 412.847 Da (MALDI-TOF–MS). Kinetic parameters were determined for PFLNA (Kₘ = 0.3227 mM and k<sub>cat</sub> = 4.27 s⁻¹). The N-terminal sequence (AVPQSIDWRDYGAVTTDKNQ) of isolated protease showed considerable similarity to other cysteine proteases obtained from stems or fruits of different <i>Bromeliaceae</i> species.
Centro de Investigación de Proteínas Vegetales
description Penduliflorain I, a new plant endopeptidase, was isolated and characterized from <i>Hohenbergia penduliflora</i>. Crude extract was obtained from stems. A partially purified enzyme preparation was obtained by ethanol precipitation. This preparation showed maximum activity between pH 7.5 and 8.5, was stable at ionic strength (20% decrease in proteolytic activity could be detected after 2 h in 0.4 M sodium chloride solution), and exhibited high thermal stability (inactivation required heating for 20 min at 75 °C). Inhibition and activation assays indicated the cysteine nature of the enzymatic preparation. Penduliflorain I was purified by anion exchange chromatography (Q-Sepharose HP) by FPLC system. Homogeneity was confirmed by mass spectroscopy. Molecular mass of the enzyme was 23 412.847 Da (MALDI-TOF–MS). Kinetic parameters were determined for PFLNA (Kₘ = 0.3227 mM and k<sub>cat</sub> = 4.27 s⁻¹). The N-terminal sequence (AVPQSIDWRDYGAVTTDKNQ) of isolated protease showed considerable similarity to other cysteine proteases obtained from stems or fruits of different <i>Bromeliaceae</i> species.
publishDate 2010
dc.date.none.fl_str_mv 2010-05
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/10915/137088
url http://sedici.unlp.edu.ar/handle/10915/137088
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1572-3887
info:eu-repo/semantics/altIdentifier/issn/1573-4943
info:eu-repo/semantics/altIdentifier/doi/10.1007/s10930-010-9243-7
info:eu-repo/semantics/altIdentifier/pmid/20521163
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
225-233
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 13.22299

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