Substrate Report for: Malathion

BACKGROUND: In insects, carboxylesterases (CarEs) are enzymes involved in the detoxification of insecticides. However, the molecular mechanism of CarE-mediated insecticide metabolism in Bradysia odoriphaga, a serious agricultural pest, remains unclear. The aim of this study is to investigate the detoxification process of malathion, bifenthrin, and imidacloprid by B. odoriphaga carboxylesterase (Boest1). RESULTS: An alpha class CarE gene Boest1 was cloned from B. odoriphaga. The results of real-time quantitative PCR showed that Boest1 is up-regulated with age during the larval stage, and the level of transcription of Boest1 is higher in the midgut and Malpighian tubule than in other tissues. The expression level of Boest1 was significantly increased after exposure to malathion and bifenthrin. Recombinant BoEST1 expressed in vitro showed high catalytic activity toward alpha-naphthyl acetate, which was substantially inhibited by malathion and triphenyl phosphate. The in vitro metabolism assays showed that BoEST1 demonstrates hydrolytic capacity toward malathion and bifenthrin but not imidacloprid. The binding free energy analysis indicates that BoEST1 has a higher affinity for malathion and bifenthrin than imidacloprid. CONCLUSION: These results suggest that BoEST1 plays a role in the breakdown of insecticides and may be involved in the development of resistance in the Chinese chive pest B. odoriphaga; our findings also provide data for better pest management and perspectives for new pesticides development. This article is protected by copyright. All rights reserved.

Malathion was incubated in water extracts of vegetables at various temperatures and pH, and the amount of malathion present over time was analyzed by a gas chromatograph with a flame photometric detector. Malathion was degraded to a nondetectable level in a 1% asparagus extract incubated at pH 7.4 and 37 degrees C for 4 h. Carrot extract showed the second highest rate of malathion degradation (76%), followed by kale extract (23.7%), spinach extract (9.7%), and broccoli extract (1.5%) under the same conditions. The highest degradation rates of malathion were observed at 37 degrees C, when three different temperatures were tested (5, 25, and 37 degrees C) at pH 7.4. Rate constants were 0.134 min(-)(1) from a 1% asparagus solution and 0.095 min(-)(1) from a 0.5% asparagus solution. The highest degradation rate of malathion was achieved at pH 9 among the pHs tested (pH 4, 7.4, and 9) in a 0.5% asparagus solution. The 0.5% asparagus solution degraded dicarboxylic acid esters by almost 100% for dimethyl succinate and diethyl adipate, by 64% for diethyl acetyl succinate, and 30% for diethyl benzyl malonate when incubated at pH 9 for 20 min. The results support the hypothesis that the enzyme that degrades malathion in the asparagus solutions is a carboxylesterase.