Characterisation and inhibition studies of Helicoverpa armigera (Hübner) gut α‐amylase

BACKGROUND: The survival of a devastating pest, Helicoverpa armigera, is mainly dependent on the availability of α-amylase. Therefore, characterising H. armigera α-amylase and targeting it with effective inhibitors could aid in reducing its damaging effects. RESULTS: H. armigera gut possessed four isozymes of α-amylase. The molecular weight of the major purified isozyme ranged from 79 to 81 kDa. The purified enzyme was identified to be α-amylase on the basis of products formed from starch. The optimum pH and temperature were 10.0 and 50 °C respectively. The activation energy was 5.7 kcal mol(-1) . The enzyme showed high activity with starch and amylopectin, whereas dextrins were poor substrates. The Michaelis constant Km with starch, amylose and amylopectin was 0.45, 1.23 and 0.11 mg mL(-1) respectively. ZnSO4 , FeSO4 , CuSO4 , citric acid, oxalic acid and salicylic acid were potent inhibitors. ZnSO4 , salicylic acid and pigeonpea α-amylase inhibitor (∼21.0 kDa) acted primarily as competitive inhibitors, FeSO4 and citric acid displayed mainly anticompetitive behaviour, while CuSO4 and oxalic acid behaved mainly as non-competitive inhibitors. CONCLUSIONS: The identification of effective ecofriendly inhibitors could help in managing H. armigera infestation.