Graphitized carbon black (GCB) in the traditional QuEChERS (quick, easy, cheap, effective, rugged, and safe) method was used to remove the interfering substance chlorophyll in vegetable and fruit samples for pesticide residues determination. However, it not only adsorbs pigments, but also adsorbs some planar and aromatic pesticides. In order to solve the shortcoming, a core-shell magnetic molecularly imprinted polymer (Fe₃O₄@MIP) that can specifically recognize and adsorb chlorophyll was synthesized, and an advanced QuEChERS method with the Fe₃O₄@MIP as a purification material was developed. This advanced method presents detection that is highly sensitive, specific, and reproducible for planar and aromatic pesticides. The limits of detection (LOD) ranged from 0.001–0.002 mg kg⁻¹, and the limit of quantification (LOQ) was 0.005 mg kg⁻¹. The recovery for the planar and aromatic pesticides was within 70–110% with the associated relative standard deviations < 15% in leek samples by the advanced QuEChERS method. However, in the traditional QuEChERS method with GCB, the recovery of most planar and aromatic pesticides was <60%. It may also be useful for the determination of other pesticides in vegetable samples with quick and easy sample purification.

Slugs are significant agricultural pests and act as vectors for zoonotic parasites. However, current molluscicide options are limited and associated with substantial environmental risks. This study investigates the role of aldehyde dehydrogenase (ALDH) in the biosynthesis of farnesoic acid (FA), a key intermediate in the sesquiterpenoid hormone pathway, in two slug species: Philomycus bilineatus and Laevicaulis alte. Transcriptomic analysis revealed that both species possess conserved sesquiterpenoid biosynthetic pathways, yet they exhibit distinct levels of ALDH gene expression and differences in FA content. RNA interference (RNAi)-mediated gene silencing was employed to validate the potential of these candidate genes as targets for molluscicide development. Structural modeling of ALDH proteins using AlphaFold2 demonstrated notable divergence in the architecture of their active sites, suggesting species-specific enzymatic properties. Citral, a known inhibitor of ALDH, significantly reduced FA production in vivo and exhibited contact toxicity against both slug species. The lethal concentration 50 (LC₅₀) values were determined to be 378.2 g/L for P. bilineatus and 85.2 g/L for L. alte, respectively. Molecular docking analyses indicated that citral binds within the conserved substrate-binding tunnel of ALDH, potentially inhibiting the oxidation of farnesal. These findings establish ALDH as a critical enzymatic target for disrupting endogenous hormone biosynthesis in slugs and support the development of novel, eco-friendly molluscicides targeting the sesquiterpenoid pathway.