Purification and characterization of hieronymain III. Comparison with other proteases previously isolated from Bromelia hieronymi Mez

Mariela A. Bruno, Sebastián A. Trejo, Néstor O. Caffini, Laura M.I. López

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16 Citations (Scopus)

Abstract

A new proteolytic enzyme, named hieronymain III, has been purified by ion-exchange chromatography from unripe fruits of Bromelia hieronymi Mez. The new peptidase belongs to the cysteine catalytic type, as well as hieronymain I and II, the other two peptidases previously isolated from this species. Hieronymain III showed optimum alkaline pH range (8.6-9.3) and the molecular mass (MALDI-TOF) was 23713 Da. The N-terminal sequence (AVPQSIDWRRYGAVTTSRNQG) exhibited a higher percentage identity with hieronymain II (93%) than with hieronymain I (71%). The three peptidases showed notable differences on synthetic substrates degradation: whereas hieronymain III was the only one able to hidrolyze Z-Arg-Arg-p-nitroanilide, hieronymain I and II could degrade Z-Phe-Arg-p-nitroanilide; on the other hand, PFLNA was only split by hieronymain I. Finally, the three proteases showed different preferences on N-α-CBZ-p-nitrophenyl aminoacid ester substrates. From a biotechnological point of view, cleavage specificity differences are significant enough to use these enzymes as potential tools in that area. © 2008 Springer Science+Business Media, LLC.
Original languageEnglish
Pages (from-to)426-433
JournalProtein Journal
Volume27
Issue number7-8
DOIs
Publication statusPublished - 1 Dec 2008

Keywords

  • Bromelia hieronymi
  • Bromeliaceae
  • Cysteine protease
  • Plant peptidases

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