Exploration for anti-insect properties of lectin from seeds of soybean (Glycine max) usingBactrocera cucurbitae as a model

Lectin fromGlycine max L. was extracted and purified by affinity chromatography using asialofetuin-linked porous amino-activated silica beads. The concentration-dependent effect of lectin was studied on freshly laid eggs (0–8 h old) of the melon flyBactrocera cucurbitae (Coquillett); lectin failed to influence egg hatching. However, treating second instar larvae (64–72 h old) with increasing concentrations of lectin significantly reduced the development period, number of pupae and number of emergingB. cucurbitae, and was negatively correlated with the increase in the lectin concentration. The LC₅₀ value, 54μg ml⁻¹, was calculated on the basis of adult emergence. Treatment of the larvae (64–72 h old) with the LC₅₀ concentration resulted in a decrease in pupal weight. The activity of three hydrolase enzymes (esterases, acid and alkaline phosphatases), one oxidoreductase (catalase) and one group transfer enzyme (glutathione S-transferase) was assayed in second instar larvae at the LC₅₀ concentration of lectin after exposure for 24, 48 and 72 h. The activity of esterases increased significantly (P<0.01) at the three exposure intervals, whereas the activities of the three other hydrolyses and the transferases were significantly suppressed (P<0.01). http://www.phytoparasitica.org posting Sept. 13, 2006.