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Updated: Apr 3, 2026

Functional Characterization of Carboxylesterases in Insecticide Resistant House Flies, Musca Domestica
Published on: August 23, 2018
Bacillus subtilis Spore-Displayed Aminopeptidase from Pseudomonas aeruginosa Efficiently Degrades Pyrethroid
Wen-Long Liu1, Xiao-Li Yuan1, Zong-Hong Wen1
1School of Chemistry and Chemical Engineering, Guangxi University, Nanning 530004 Guangxi, P.R. China.
Abstract:
Pyrethroid insecticides are extensively applied owing to their potent insecticidal activity and low mammalian toxicity, yet their hydrophobicity results in persistent environmental residues. Here, we engineered a Bacillus subtilis spore surface display system to anchor Pseudomonas aeruginosa aminopeptidase (PaAps) on the spore coat and evaluated its potential for pyrethroid degradation. Surface-anchored PaAps efficiently degraded various pyrethroids, with β-cypermethrin showing the highest removal. The enzyme exhibited remarkable thermal stability and pH tolerance, with optimal activity at 60 °C and pH 8.0, along with enhanced long-term storage stability. Soil microcosm studies revealed that PaAps not only accelerated β-cypermethrin degradation but also influenced the indigenous microbial community to enhance bioremediation. This study demonstrates a robust and environmentally sustainable biocatalytic strategy for pyrethroid detoxification, with promising applications in environmental remediation and food safety.
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The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...