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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| 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: |
| Sumario: | 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. |
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