Penduliflorain I: A cysteine protease isolated from Hohenbergia penduliflora (A.Rich.) Mez (Bromeliaceae)

A. Pérez, C. Carvajal, S. Trejo, M. J. Torres, M. I. Martin, J. C. Lorenzo, C. L. Natalucci, M. Hernández

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10 Citations (Scopus)


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 (MALDITOF-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. © Springer Science+Business Media, LLC 2010.
Original languageEnglish
Pages (from-to)225-233
JournalProtein Journal
Issue number4
Publication statusPublished - 1 May 2010


  • Bromeliaceae
  • Chromatography purification
  • Hohenbergia penduliflora
  • Stems
  • Thiol proteases


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