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Biochemical characterization of the alpha-amylase inhibitor in mungbeans and its application in inhibiting the growth of Callosobruchus maculatus
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The insect Callosobruchus maculatus causes considerable damage to harvested mungbean seeds every year, which leads to commercial losses. However, recent studies have revealed that mungbean seeds contain á-amylase inhibitors that can inhibit the protein C. maculatus, preventing growth and development of the insect larvae in the seed, thus preventing further damage. For this reason, the use of á-amylase inhibitors to interfere with the pest’s digestion process has become an interesting alternative biocontrolling agent. In this study, we have isolated and purified the á-amylase inhibitor from mungbean seeds (KPS1) using ammonium sulfate precipitation, gel filtration chromatography and reversed phase HPLC. We found that the á-amylase inhibitor, isolated as a monomer, had a molecular weight of 27 kDa. The á-amylase inhibitor was purified 750-fold with a final yield of 0.4 mg of protein per 30 g of mungbean seeds. Its specific activity was determined at 14.5 U (mg of protein)?1 . Interestingly, we found that the isolated á-amylase inhibitor inhibits C. maculatus á-amylase but not human salivary á-amylase. After preincubation of the enzyme with the inhibitor, the mungbean á-amylase inhibitor inhibited C. maculatus á-amylase activity by decreasing Vmax while increasing the Km constant, indicating that the mungbean á-amylase is a mix noncompetitive inhibitor. The in vivo effect of á-amylase inhibitor on the mortality of C. maculatus shows that the á-amylase inhibitor acts on C. maculatus during the development stage, by reducing carbohydrate digestion necessary for growth and development, rather than during the end laying/hatching stage. Our results suggest that mungbean á-amylase inhibitor could be a useful future biocontrolling agent.
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 Record created 2010-04-13, last modified 2019-07-02

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