Abstract

In the current study, a low weight lectin (19.22 kDa) was extracted from Polygonum persicaria by Sepharose 4B-galactose column and its inhibition was determined against digestive α-amylase of Pieris brassicae larvae. Different concentrations of the purified lectin were prepared and incubated with midgut homogenate of larvae to observe its inhibition. Inhibition study revealed IC10, IC30 and IC50 values of 0.013, 0.104 and 0.422 mg/ml against digestive amylolytic activity of larvae. In zymogram analysis, incubation of midgut homogenates with 0.42 mg/ml of the purified lectin showed decrease in sharpness of band A2 and disappearance of band A1. pH profile of inhibition revealed that the purified lectin caused the highest inhibition at pH 10 and 11 corresponding with control experiment. Time dependency of inhibition demonstrated the highest inhibition after 30 min of post-incubation. Stability of the purified lectin was measured by incubating the molecule at 50, 60 and 70 °C. It was observed that the samples incubated at 60 and 70 °C had no inhibition on amylolytic activity. Finally, Linweaver-Burk analysis revealed significant decrease in Vmax versus control showing non-competitive inhibition.

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