Purification and autolysis of the ficin isoforms from fig (Ficus carica cv. Sabz) latex.

PubMed ID: 23312458

Author(s): Zare H, Moosavi-Movahedi AA, Salami M, Mirzaei M, Saboury AA, Sheibani N. Purification and autolysis of the ficin isoforms from fig (Ficus carica cv. Sabz) latex. Phytochemistry. 2013 Mar;87:16-22. doi: 10.1016/j.phytochem.2012.12.006. Epub 2013 Jan 10. PMID 23312458

Journal: Phytochemistry, Volume 87, Mar 2013

Ficin (EC 3.4.22.3), a cysteine endoproteolytic protease in fig trees’ latex, has multiple isoforms. Until now, no data on autolysis of individual ficins (ficin isoforms) are available. Following purification, ficins’ autolysis was determined by HPLC chromatogram changes and ultrafiltrations at different temperatures and storage times. These results showed that the number of HPLC peaks in latex proteins purification of Ficus carica cv. Sabz varied from previous fig varieties or cultivars. Proteolytic activity of ficins was inhibited by specific cysteine protease inhibitors, confirming the participation of the cysteine residue in the active site. The zeta potential of the first two eluted peaks (I and II) was negative, while that of other peaks were positive. All ficins were susceptible to autolysis when stored at high temperatures. In contrast, only the last two ficins (B, C) were prone to autolysis at cold temperature after long storage period. The rate of degradation of the ficins was significantly increased with the increased storage time. The ficin (A) related to peak (III) had the highest and the lowest surface hydrophobic patches and ratio of autolytic to proteolytic activity, respectively.