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In the present study wheat Ltp 3FI gene was overexpressed in E. coli using
pMAL-pZx vector. Expression vector, pMAL-pZx with maltose binding protein
(MBP) as fusion was used as solubility enhancing pnrlner (Kapust and Waugh. 19991.
The recombinant LTP-MBP fusion protein was found in the IPTG-induced E. coli
culture supernatant as soluble fraction. Although the recon~binant LTP fusion protein
was purified to homogeneity using ammonium sulphate fractionation nnd gel
permeation chromatography, the recovery of LTP domain from the fusion protein
after Factor Xa digestion was not achieved. This could be due to a rapid proteolysis of
the released protein probably caused by a bacterial protease activity that co-purified
with the fusion protein. Similar problems were already encountered with other
investigators (Maina et al., 1988).
Antifungal potential of plant chitinases has been well documented. According
to Roberts and Selitrennikoff (1988) chitinases isolated from the grains of wheat,
barley and maize functioned as endochitinases and inhibited hyphal elongation of
fungi. Huynh er al., (1992) reported 28 kDa chitinases from maize seeds with in vitro
antifungal activity against the growth of Trichoderma reesei, Alternuria solani and
Fusarium oxysporum. The purified chitinase from sorghum seeds showed antifungal
activity against
F. monilifonne. Curvularia lunara
and Aspergillus flavus
(Seetharaman et al., 1997). Ye and Ng. (2005) isolated mung bean chitinase with
antifungal activity against
F. oxysporum, Mycosphaerella arachidicola. Pythium
ophanidennarum and Scerotium rolfsii.
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