Papain purification insights: Monitoring by electrophoretic approaches and MALDI-TOF peptide mass fingerprint analyses

Carlos R. Llerena-Suster, W. David Obregón, Sebastián A. Trejo, Susana R. Morcelle

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1 Citation (Scopus)

Abstract

Papain was purified from dried Carica papaya latex by fractioned salt precipitation in presence of sodium tetrathionate to preserve enzymatic activity. Purification was followed by different electrophoretic methods. Identification of the purified product was afforded by submitting the peptides obtained by tryptic digestion of papain to matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF/TOF MS) analysis. Comparison of the peptide masses analyzed by peptide mass fingerprinting (PMF) MALDI-TOF and those obtained by theoretical tryptic digestion, revealed the presence of some peptides belonging the other three endopeptidases contained in papaya latex (very similar to papain in molecular weight and pI) in the purified fraction of papain. The PMF by MALDI-TOF could be applied as a method to follow papain purification. © Taylor & Francis Group, LLC.
Original languageEnglish
Pages (from-to)2124-2137
JournalAnalytical Letters
Volume44
Issue number12
DOIs
Publication statusPublished - 1 Aug 2011

Keywords

  • Caricain
  • Chymopapain
  • Glycyl endopeptidase
  • MALDI-TOF peptide mass fingerprint
  • Papain

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