LLERENA SUSTER Carlos Rafael
Papain Purification Insights: Monitoring by Electrophoretic Approaches and MALDI-TOF Peptide Mass Fingerprint Analyses
CARLOS R. LLERENA SUSTER; WALTER D. OBREGON; SEBASTIAN TREJO; SUSANA R. MORCELLE
TAYLOR & FRANCIS INC
Año: 2011 vol. 44 p. 2124 - 2137
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 MALDITOF/TOF MS analysis. Comparison of the peptide masses analyzed by PMF MALDITOF 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. PMF by MALDI-TOF could be applied as a method to follow papain purification.