Primary purification of two antifungal proteins
from leaves of the fig (Ficus carica L.)
Wei Yan3, Ming Zhao2, Yan Ma2,
Ying-hong Pan1* and Wen-xia Yuan2
of Crop Sciences, Chinese Academy of Agricultural Sciences,
Beijing 100081, People’s Republic of China.
of Pu-erh Tea, Yunnan Agricultural University, Kunming
650201, People’s Republic of China.
of Life Science, Sichuan Normal University, Chengdu 610068,
People’s Republic of China.
Tel: +86-010-82105818. Fax: +86-010-82105817.
TL, Thaumatin-like proteins; RIPs,
ribosome-inactivating proteins; LTPs, lipid-transfer
proteins; EDTA, ethylenediaminetetraacetic acid;
DTT, DL-dithiothreitol; PVPP,
polyvinylpyrrolidone; FPLC, fast protein liquid
chromatography; SDS-PAGE, sodium dodecyl sulfate
polyacrylamide gel electrophoresis; MALDI-TOF MS,
matrix-assisted laser desorption ionization time-of-flight
Low-molecular-weight extracts of fig (Ficus carica
L.) leaves has antifungal and antibacterial activities
against several types of microorganisms. In this work, two
high-molecular-weight fractions with antifungal activity,
termed figinI and figinII were obtained from leaves of fig
using a procedure including ion-exchange chromatography (SP-Sepharose
Fast Flow), hydrophobic-interaction chromatography (Phenyl
Sepharose 6 Fast Flow and RESOURCE ISO) and ion-exchange
chromatography (Mono S). By matrix-assisted laser desorption
ionization time-of-flight mass spectrometry analysis (MALDI-TOF
MS), the molecular mass of figinI was 21531Da and figinII
was 31957Da. This is the first report on isolation of
antifungal proteins from F. carica L., and it shows
their potential for further investigation.
Fig, antifungal protein, chromatography, natural food