Heterologous expression, biochemical characterization and prospects for insecticide biosensing potential of carboxylesterase Ha006a from Helicoverpa armigera

Enzymes have attracted considerable scientific attention for their crucial role in detoxifying a wide range of harmful compounds. In today's global context, the extensive use of insecticides has emerged as a significant threat to the environment, sparking substantial concern. Insects, including...

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Published in:Pesticide biochemistry and physiology 2024-03, Vol.200, p.105844-105844, Article 105844
Main Authors: Kaur, Harry, Rode, Surabhi, Lonare, Sapna, Demiwal, Pratibha, Narasimhappa, Pavithra, Arun, Etisha, Kumar, Rakesh, Das, Joy, Ramamurthy, Praveen C., Sircar, Debabrata, Sharma, Ashwani Kumar
Format: Article
Language:English
Subjects:
Bioremediation
Biosensor
Carboxylesterase
Helicoverpa armigera
Insecticides
ITC
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Summary:Enzymes have attracted considerable scientific attention for their crucial role in detoxifying a wide range of harmful compounds. In today's global context, the extensive use of insecticides has emerged as a significant threat to the environment, sparking substantial concern. Insects, including economically important pests like Helicoverpa armigera, have developed resistance to conventional pest control methods through enzymes like carboxyl/cholinesterases. This study specifically focuses on a notable carboxyl/cholinesterase enzyme from Helicoverpa armigera (Ha006a), with the goal of harnessing its potential to combat environmental toxins. A total of six insecticides belonging to two different classes displayed varying inhibitory responses towards Ha006a, thereby rendering it effective in detoxifying a broader spectrum of insecticides. The significance of this research lies in discovering the bioremediation property of Ha006a, as it hydrolyzes synthetic pyrethroids (fenvalerate, λ-cyhalothrin and deltamethrin) and sequesters organophosphate (paraoxon ethyl, profenofos, and chlorpyrifos) insecticides. Additionally, the interaction studies between organophosphate insecticides and Ha006a helped in the fabrication of a novel electroanalytical sensor using a modified carbon paste electrode (MCPE). This sensor boasts impressive sensitivity, with detection limits of 0.019 μM, 0.15 μM, and 0.025 μM for paraoxon ethyl, profenofos, and chlorpyrifos, respectively. This study provides a comprehensive biochemical and biophysical characterization of the purified esterase Ha006a, showcasing its potential to remediate different classes of insecticides. [Display omitted] •Insect esterase enzyme (Ha006a) was heterologously expressed and homogenously purified.•Recombinant Ha006a exhibited monomeric conformation with robust catalytic esterase activity.•OP and SP insecticides displayed varying inhibitory responses towards Ha006a.•Ha006a preferentially hydrolyze SP insecticides (deltamethrin, λ-cyhalothrin, and fenvalerate).•A high sensitivity detection OP insecticide was achieved using Ha006a-based biosensor.
ISSN:0048-3575
1095-9939
DOI:10.1016/j.pestbp.2024.105844