Exploring catalytic degradation of environmental fenamiphos by yeast enolase cross-linked with COOH-functionalized silver nanoparticles

This study investigated the sustainable hydrolysis of the neurotoxic organophosphate insecticide fenamiphos using enolase from Saccharomyces cerevisiae FN6-01. The current detoxification methods for fenamiphos have some limitations. The research explored catalytic degradation using yeast enolase immobilized on COOH-functionalized silver nanoparticles (AgNPs). As enolase hydrolyzes fenamiphos into a less harmful form, Saccharomyces cerevisiae-produced enolase was immobilized on AgNPs through citrate stabilization and COOH functionalization. The synthesized AgNPs were characterized using UV-vis spectrophotometry, FTIR, XRD, and SEM. Enzymatic hydrolysis of fenamiphos was studied under different conditions. Immobilized enolase on AgNPs exhibited better stability and activity than the free enzyme. Hydrolysis efficiency was investigated concerning potassium ferrocyanate concentration and temperature. The immobilized enolase showed excellent thermostability at 30 °C. Statistically significant results (p ≤ 0.05) confirmed the efficacy of immobilized enolase in detoxifying fenamiphos and reducing its adverse effects. This study revealed the mechanism of fenamiphos degradation through base hydrolysis facilitated by enolase while preserving its enzymatic activity. Immobilized yeast enolase demonstrated exceptional performance in fenamiphos hydrolysis, providing a promising approach for environmentally conscious pesticide elimination. The research contributes to sustainable pesticide remediation, offering a scientific basis for enzymatic methods to address environmental challenges associated with pesticide residues.