Fusarium avenaceum is the predominant fungal pathogen responsible for root rot in Angelica crops and poses a serious threat to their commercial quality and yield in China. This fungus produces enniatin B (ENN B), a toxin that could be a pathogenicity and virulence factor in plant–pathogen interactions. Yet whether ENN B exacerbates host infection and the onset of root rot in Angelica spp. caused by F. avenaceum is surprisingly understudied. Pathogenicity assays revealed that ENN B co-inoculation with F. avenaceum significantly increased the root rot disease index in Angelica sinensis from 83.33% (pathogen alone) to 92.86% (p < 0.05). Toxin degradation experiments showed that the bacteria Paenibacillus polymyxa and Bacillus tequilensis were capable of degrading 60.69% and 70.02% of ENN B, respectively. Response surface optimization (24.5 °C, 22.01 mg/L ENN B, 0.99% inoculum) enhanced degradation by B. tequilensis to 81.94%, a 11.74% improvement. Three ester compounds were identified by LC-HRMS as potential degradation products of ENN B. In planta trials demonstrated that the disease index was 50.01% for the group co-inoculated with ENN B degradation products and F. avenaceum, a 42.85% reduction compared to the group co-inoculated with ENN B and F. avenaceum. This study provides a new microbial strategy for controlling root rot in Angelica crops from a mycotoxin degradation perspective, which can be applied to promote sustainable agricultural production.

Acetamiprid (ACE) and thiacloprid (THIA) are the dominant cyano-substituted neonicotinoids detected in fruit juices and bottled water, which raises food-safety concerns and regulatory scrutiny. Conventional purification with activated carbon or advanced oxidation shows limited selectivity and has a high energy demand. Covalent organic frameworks (COFs) offer tunable chemistry for targeted adsorption, yet no strategy exists to engineer COF sites that preferentially recognize the cyano group of ACE/THIA. Here, we synthesized a magnetic core-shell adsorbent, Fe₃O₄@COF(TBTD-BD)-Au, by growing cyano-affinitive Au nanoparticles on a Cl-decorated COF shell surrounding a Fe₃O₄ core. Under optimized conditions (pH 6.0, 25 °C), the Fe₃O₄@COF(TBTD-BD)-Au achieved maximum adsorption capacities of 157 mg g⁻¹ (ACE) and 156 mg g⁻¹ (THIA). Uptake followed pseudo-second-order kinetics and the Freundlich isotherm; thermodynamic analysis confirmed an endothermic, spontaneous process. Competitive tests showed >80% removal of ACE and THIA in the presence of four co-occurring neonicotinoids, and the adsorbent retained 91.5% of its initial capacity after six adsorption–desorption cycles. Synergistic Au-cyano coordination, Cl-mediated hydrogen bonding, and π–π stacking confinement confer high selectivity and capacity. This ligand-guided, post-functionalized COF provides promising potential in the field of food sample treatment for contaminant removal.

Amine dehydrogenases (AmDHs) are efficient biocatalysts for asymmetric chiral amine synthesis. This study reports the mining and systematic characterization of three thermophilic amino acid dehydrogenases (AADHs): TmAADH, TaAADH, and MtAADH. Phylogenetically, these enzymes occupy an intermediate position between leucine and phenylalanine dehydrogenases, suggesting hybrid active-site architectures. They shared an optimal pH of 9.0 for reductive amination but differed in oxidative deamination (pH 10.5–11.0) and thermal profiles (optima 35–45 °C; stability hierarchy TmAADH > TaAADH > MtAADH). While all preferred the reductive direction (25–340-fold activity enhancement), they exhibited complementary substrate specificities: MtAADH favored branched aliphatic keto acids, TaAADH short-chain substrates, and TmAADH aromatic α-keto acids. Rational engineering of conserved carboxyl-binding sites (MtAmDH(K67S/N261L), TaAmDH(K68S/N261L) and TmAmDH (K69S/N264L)) successfully converted these AADHs into AmDHs, conferring de novo catalytic activity toward prochiral hydroxy ketones with excellent enantioselectivity (>90% ee, S-configuration). These robust biocatalysts offer promising enzymatic tools for industrial chiral amine production.