Substrate specificities and multiple forms of esterases in the brown planthopper, Nilaparvata lugens (Stal)

Abstract

Substrate specificities have been examined in body homogenates of the brown planthopper, Nilaparvata lugens (Stal), using α-naphthyl acetate, β-naphthyl acetate, trans-permethrin, cis-permethrin, malathion, and fenvalerate as substrates. Eight esterases were resolved from body homogenates of the brown planthopper with p I values in the range of 4.3–5.3 and designated as E1–E8. All E1–E8 hydrolyzed α-naphthyl acetate, β-naphthyl acetate, cis-permethrin, trans-permethrin, and malathion at different rates. Fenvalerate was the most stable substrate to hydrolysis and was hydrolyzed by E1–E8 except E3.