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

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...

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Detalles Bibliográficos
Autores principales: Pérez, Aurora, Carvajal, Carol, Trejo, Sebastián Alejandro, Figuerero Torres, María José, Martin, María Inés, Lorenzo, José Carlos, Natalucci, Claudia Luisa, Hernández, Martha
Formato: Articulo
Lenguaje:Inglés
Publicado: 2010
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/137088
Aporte de:
id I19-R120-10915-137088
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
spellingShingle Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
Pérez, Aurora
Carvajal, Carol
Trejo, Sebastián Alejandro
Figuerero Torres, María José
Martin, María Inés
Lorenzo, José Carlos
Natalucci, Claudia Luisa
Hernández, Martha
Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
topic_facet Ciencias Exactas
Biología
Bromeliaceae
Hohenbergia penduliflora
Chromatography purification
Stems
Thiol proteases
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.
format Articulo
Articulo
author Pérez, Aurora
Carvajal, Carol
Trejo, Sebastián Alejandro
Figuerero Torres, María José
Martin, María Inés
Lorenzo, José Carlos
Natalucci, Claudia Luisa
Hernández, Martha
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_sort Pérez, Aurora
title Penduliflorain I: A Cysteine Protease Isolated from <i>Hohenbergia penduliflora</i> (A.Rich.) Mez (<i>Bromeliaceae</i>)
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>)
publishDate 2010
url http://sedici.unlp.edu.ar/handle/10915/137088
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