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

Ficins autolysis enhanced in order of their elution from the column. As the first and last eluted ficin had the lowest and highest autolysis, respectively. [Display omitted] ► Four ficins were purified from fig (Ficus carica cv. Sabz) latex. ► All ficins were susceptible to autolysis at high tempera...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Phytochemistry (Oxford) 2013-03, Vol.87, p.16-22
Hauptverfasser: Zare, Hamid, Moosavi-Movahedi, Ali Akbar, Salami, Maryam, Mirzaei, Morteza, Saboury, Ali Akbar, Sheibani, Nader
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Ficins autolysis enhanced in order of their elution from the column. As the first and last eluted ficin had the lowest and highest autolysis, respectively. [Display omitted] ► Four ficins were purified from fig (Ficus carica cv. Sabz) latex. ► All ficins were susceptible to autolysis at high temperatures. ► The ficins autolysis rate increased with increasing storage time. ► Ficin (A) had the lowest ratio of autolytic to proteolytic activity. ► Slight ficins hydrophobic patches intensified the autolysis. 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.
ISSN:0031-9422
1873-3700
DOI:10.1016/j.phytochem.2012.12.006