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...
Autores principales: | , , , , , , , |
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Formato: | Articulo |
Lenguaje: | Inglés |
Publicado: |
2010
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Materias: | |
Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/137088 |
Aporte de: |
id |
I19-R120-10915-137088 |
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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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Repositorios |
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1764820457827074051 |