Phosphorothioate Insecticides Research Articles

A robust electrochemical sensor based on AgNWs@MoS2 for highly sensitive detection of thiabendazole residues in food samples

Thiabendazole (TBZ), a highly toxic phosphorothioate insecticide commonly used in postharvest fruit management, has the potential to cause detrimental effects on human health as an endocrine disruptor. In this study, an electrochemical sensor was developed to detect TBZ by modifying MoS2 on silver nanowires (Ag NWs@MoS2) and integrating them onto a glassy carbon surface. Cyclic voltammetry revealed that TBZ underwent an irreversible, diffusion-controlled process on Ag NWs@MoS2, leading to a two-fold increase in peak current compared to unmodified MoS2. Square wave voltammetry facilitated TBZ detection, and the sensor exhibited a linear range of 0.05–10 μM with a high coefficient of determination (R2 = 0.9958) and a limit of detection (LOD) of 1.75 nM (signal-to-noise ratio = 3). The sensor's applicability for food safety monitoring was verified through TBZ analysis in pear and apple samples, achieving recoveries of 95.5–103.6% with RSDs in the range of 1.98–3.25%.

The impact of solvents on the toxicity of the banned parathion insecticide

The aerial crop dusting and spraying of fields with the phosphorothioate insecticide parathion in the late 1900s, significantly improved crop yields but resulted in high levels of occupational toxicity in handlers and agricultural workers, as well as cases of intentional self-harm poisoning, culminating in its banning in many western countries by early 2000s. However because of the low solubility and volatility of parathion, most available products were formulated using organic solvents e.g. xylene, to increase the efficacy of the aerosols and dusts. In the present study, the toxicity of parathion was assessed when formulated in an aqueous solvents (ethanol/PBS (1:9)), and delivered to macaques as an aerosol. Doses of 780 μg/kg and 1.56 mg/kg were delivered one day apart, using a modified nebulizer calculated to result in lung deposition of ∼480 μg/kg with a similar or larger amount being swallowed; these doses being similar to the estimated lethal oral dose 286ug/kg - 1.43 mg/kg of formulated parathion in humans. Surprisingly, this dose (a combined amount of ∼14 mg) caused only low AChE inhibition and moderate BChE inhibition with no clinical symptoms, indicating that the use of organic solvents may have previously played a critical role in the severity of parathion toxicity following inhalation exposure. In addition, unlike constitutively toxic OPs, which are highly toxic when inhaled, these results are consistent with the idea that phosphorothioate insecticides appear to be more intoxicating following oral than inhalation exposure. However, this still remains uncertain because the presence of organic solvents in the ingested parathion studies was not always known.

Facile synthesis of petal-like VS2 anchored onto graphene nanosheets for the rapid sensing of toxic pesticide in polluted water

Fenitrothion (FT) is a toxic phosphorothioate insecticide that can easily contaminate aquatic environments, leading to a detrimental effect on the aquatic species and harmful endocrine disrupter effects on human health. Therefore, it is vital to develop a reliable methodology for the accurate and precise real-time sensing of carcinogenic FT in water samples at trace concentration to ensure environmental safety. We aim to fabricate the low-cost VS2-attached reduced graphene oxide (RGO) sheets via a simple hydrothermal approach. It was further applied for the rapid and accurate sensing of toxic FT. The VS2/RGO-composite delivers a more favorable microenvironment for the rapid electrocatalytic sensing performance towards toxic FT reduction than the VS2 and RGO modified electrodes. The electron transfer rate constant (ks) and the saturating absorption capacity (Γ) value of FT was evaluated to be 1.52 s−1 and 2.18 × 10−10 mol cm−2, respectively. The constructed sensor exhibits a wide linear relationship after amperometry between the cathodic current densities and the concentrations of FT in the range of 5–90 nM and high sensitivity (5.569 μA nM−1 cm−2); moreover, the detection limit was 0.07 nM (S/N = 3). The fabricated sensor has excellent anti-interference ability and reproducibility for the direct sensing of FT in river water, seawater, and lake water samples with acceptable recoveries. It is a promising sensing device for in-situ quantification of FT in agricultural products and ecological systems.

Draft Genome Sequence of Pseudomonas stutzeri ODKF13, Isolated from Farmland Soil in Alvin, Texas.

Pseudomonas stutzeri ODKF13 is a bacterial microorganism isolated from farmland soil in Alvin, Texas. This strain is notable for its naphthalene degradation and nitrogen fixation pathways and for its characterization as an organophosphate degrader of phosphotriester and phosphorothioate insecticides.

Characterization and comparison of putative Stenotrophomonas maltophilia methyl parathion hydrolases

ABSTRACTThree Stenotrophomonas maltophilia isolates, KKWT11, CBF10-1, TTF10, were collected from organophosphate (OP)-contaminated soil in the Houston metropolitan area. A conserved metallo-β-lactamase (MBL) enzyme purported to function as a methyl parathion hydrolase was identified and found to be distantly homologous to the characterized Pseudomonas sp. WBC-3 methyl parathion hydrolase and shared no significant homology with other organophosphate hydrolases. Following expression of MBL enzymes cloned from S. maltophilia strains KKWT11, CBF10-1, and TTF10, respectively, an enzymatic preference for paraoxon was observed, with concentrations of 70, 40, and 30 µM of p-nitrophenol (PNP) formed after 48 h. Comparatively limited hydrolysis against the phosphorothioate methyl parathion was recorded with concentrations of PNP ranging from 9.5 to 3.5 µM after 48 h. A coexpressive construct harboring a modified organophosphorus hydrolase enzyme and the CBF10-1 MBL enzyme yielded only a slight improvement in degradation of methyl parathion, resulting in 75 µM of PNP formed compared with 69 µM formed by the organophosphorus hydrolase (OPH) control over 48 h. These results suggest that S. maltophilia MBL enzymes are currently insufficient for broad-spectrum hydrolysis of phosphorothioate insecticides. Future studies will thus seek to elucidate their catalytic efficiency against other notable phosphotriester oxons, including chlorpyrifos oxon, and malaoxon.

Photocatalytic degradation of diazinon by illuminated WO3 nanopowder

In this study, photocatalytic degradation of diazinon as a model phosphorothioate insecticide by tungsten oxide nanopowder under UV irradiation was investigated. Effect of operational parameters including WO3 dosage, pH, initial diazinon concentration, and organic compounds (humic acid, oxalic acid, phenol, ethylenediaminetetraacetic acid (EDTA)) on the photocatalytic degradation of diazinon was studied. Degradation efficiency of diazinon by WO3/UV process was more effective than WO3-alone and UV-alone. As the nanocatalyst dosage increased, the photocatalytic degradation of the diazinon decreased. Removal efficiency was decreased by increasing pH and initial diazinon concentration. The reaction rate constant (kobs) was decreased from 0.1233 to 0.0001/min, and the value of electrical energy per order (EEo) was increased from 38.93 to 48,000 (kWh/m3) with increasing initial diazinon concentration from 5 to 50 mg/L, respectively. The photocatalytic degradation of diazinon was increased in the presence of oxalic acid and EDTA, while different trend was observed in the presence of phenol and humic acid. Proper photocatalytic activity was observed even after five successive cycles. Finally, UV/WO3 is identified as a promising technique for the removal of diazinon with high efficiency in a short reaction time.

Fate of few pesticide-metabolizing enzymes in the marine cyanobacterium Phormidium valderianum BDU 20041 in perspective with chlorpyrifos exposure

The marine cyanobacterium Phormidium valderianum BDU 20041 is able to dwell and grow in the presence of chlorpyrifos ( O, O-diethyl- O-[3,5,6-trichloro-2-pyridyl] phosphorothioate), a phosphorothioate insecticide, at a concentration of 45 ppm. Chlorpyrifos exposure resulted in stunted growth of P. valderianum, and a 48-h exposure revealed increase in activity of pesticide-metabolizing enzymes, such as polyphenol oxidase, catalase, superoxide dismutase, esterase, and glutathione S-transferase. Among the three classes of esterases P. valderianum BDU 20041 was found to use esterases A in the metabolization of chlorpyrifos. Increased activity of catalase and superoxide dismutase clearly depicted the provoked state of oxidative stress, concurrently this circuitously proving the triggered mode of reactive oxygen species mediated degradation of chlorpyrifos.

Brain Acetylcholinesterase Activity as a Potential Biomarker for the Rapid Assessment of Chlorpyrifos Toxicity in a Euryhaline Fish,Oreochromis mossambicus

Acute studies of chlorpyrifos, O,O-diethyl-O-(3,5,6-trichloro-2-pyridyl) phosphorothioate insecticide on fish, Oreochromis (Tilapia) mossambicus, were carried out to assess the toxicity in relation to the marker enzyme, acetylcholinesterase (AChE, EC 3.1.1.7) activity in a semi-static system. Chlorpyrifos can be rated as highly toxic to O. mossambicus, with median lethal concentrations (LC50) of 43.52, 35.89, 30.6 and, 25.78 μg L−1 for 24, 48, 72, and 96 h respectively. The time required for 50% inhibition (IT50) of acetylcholinesterase (AChE) activities were measured in the brain of O. mossambicus, exposed to different median lethal concentrations indicated a decrease in time as the concentration increased. After exposure, survival fish were transferred to clean (chemical free) water and studied. AChE recovery were recorded in regular intervals of 3, 7, 14 and 21 days as a biomarker of exposure to this compound. The fish exposed to the LC50 for 24 h (43.52 μg L−1) showed a significant inhibition of AChE ...

Voltammetric study of the hydrolysis product of fenthion at the Nafion®-modified glassy carbon electrode

The differential pulse voltammetric (DPV) method is proposed for the determination of phosphorothioate insecticide (fenthion) based on the oxidation of its hydrolysis product. A single peak at +0.65 V (vs. Ag/AgCl) is observed at the Nafion®-modified glassy carbon electrode in 0.1 M Britton-Robinson buffer solution (pH 4.0) as a supporting electrolyte. The voltammetric behavior of fenthion was investigated over a wide range of pH (2.0–8.0). The effect of the solution and operational parameters on the sensitivity of the DPV peak was carefully examined in order to select the optimum conditions for the determination of fenthion. Under optimum conditions, the oxidation response gives a linear calibration plot over a concentration range of 8.41 × 10−7−5.98 × 10−6 M and the detection limit is found to be 7.6 × 10−7 M. The effects of some diverse metal ions, anions, and some other organic molecules on the determination of fenthion were studied. The applicability of DPV for the determination of fenthion insecticide in a commercial sample as well as in some water samples was demonstrated.

Effect of piperonyl butoxide on diazinon resistance in field strains of the sheep blowfly, Lucilia cuprina (Diptera: Calliphoridae), in New Zealand

AbstractPretreatment of first instar larvae of 28 resistant strains of Lucilia cuprina(Wiedemann) with the inhibitor of microsomal oxidases, piperonyl butoxide, resulted in a biphasic response to the phosphorothioate insecticide diazinon. Analysis of the data revealed a complex response in which both synergist-dependent and independent effects occurred. The responses varied markedly from strain to strain. A laboratory susceptible strain and field strains with resistance factors of less than 20-fold exhibited, in the presence of piperonyl butoxide, an increased LC50 with respect to diazinon whereas those strains with > 20-fold resistance were synergized by the compound. We conclude tentatively that microsomal mixed-function oxidases play a contributory role in the development of resistance and that the variation in synergist effect from strain to strain may be attributed, at least in part, to the two-fold effect of these enzymes on phosphorothioate insecticides such as diazinon.

Flavonoid-induced alterations in cytochrome P450-dependent biotransformation of the organophosphorus insecticide parathion in the mouse

The majority of insecticides currently in use throughout the world belong to the class of the organophosphorus insecticides. Many of these compounds, such as the phosphorothioate insecticides, exert their mammalian toxicity only after undergoing metabolic activation by a variety of cytochrome P450 isoforms to produce their corresponding oxygen analogs (or oxons), which are potent inhibitors of the critical enzyme acetylcholinesterase. Of the many chemicals identified that can modulate cytochrome P450-dependent activities, the flavonoids represent some of the most unusual compounds in that they have been reported to both inhibit and stimulate certain activities. The present study was undertaken to determine if representative flavonoids (at in vitro concentrations of 1–100 μM) can alter the mammalian cytochrome P450-dependent biotransformation and acute toxicity of the phosphorothioate insecticide parathion. The flavonoids 5,6-benzoflavone, flavone, and quercetin had the biphasic effect of stimulating mouse hepatic microsomal parathion oxidation at a concentration of 1 μM, and inhibiting this same activity when increased to 100 μM. In contrast, 7,8-benzoflavone was only inhibitory at all concentrations examined. All the flavonoids examined except quercetin altered the ratio of activation/detoxification of parathion by mouse hepatic microsomes, but had no effect on this same ratio with human CYP1A2. These data suggest that the changes in the activation/detoxification ratio observed with mouse hepatic microsomes resulted from selective inhibition or stimulation of various cytochrome P450 isoforms rather than a flavonoid-induced alteration in the nonenzymatic rearrangement of the putative phosphooxythirane intermediate generated by cytochromes P450 from parathion. Surprisingly, however, none of the four flavonoids in the current study affected the lethality of parathion in vivo, suggesting that the flavonoid-induced alterations in cytochrome P-450-dependent metabolism of parathion documented in vitro were simply not great enough to be of any significance in vivo.

The actions of the H 2-blocker cimetidine on the toxicity and biotransformation of the phosphorothioate insecticide parathion

Parathion, like most organophosphorus insecticides currently in use, must undergo cytochrome P450(P450)-dependent activation in order to exert its acute mammalian toxicity (cholinergic crisis). Since P450 isoforms play such an important role in mediating the toxicity of parathion and related insecticides, factors which significantly alter P450 activities, such as exposure to certain xenobiotics, can also be expected to affect the toxicity of these potentially hazardous insecticides. Cimetidine is a H 2-histamine antagonist that has been shown to inhibit several P450-isoforms. In addition, administration of cimetidine has been reported to result in clinically significant pharmacokinetic interactions with a wide variety of drugs. In the present study coexposure to cimetidine and parathion resulted in a moderate increase in the toxicity of this pesticide. However, coexposure to cimetidine and paraoxon did not alter the toxicity of the organophosphate, indicating that cimetidine likely affected P450-dependent formation of paraoxon from parathion. In vitro incubations of mouse hepatic microsomes demonstrated that, in addition to reducing the velocity of P450-dependent metabolism of parathion, cimetidine increased the proportion of paraoxon formed (activation), and decreased the proportion of p-nitrophenol formed (detoxification). Since parathion is not eliminated significantly by other routes in the mouse, the bulk of parathion in vivo was metabolized by P450 (although more slowly) in the presence of cimetidine, leading to a greater amount of paraoxon produced, and therefore greater toxicity. Incubations with individual P450 isoforms suggested that cimetidine could act by inhibition of P450 isoforms that detoxify parathion to a greater degree than cimetidine-resistant isoforms, and/or cimetidine could alter the proportions of detoxification versus activation of certain individual isoforms.

Gas-phase photolysis of phorate, a phosphorothioate insecticide

Novel methods are described for determining atmospheric photolysis rates for the moderately volatile pesticide, phorate. The gas-phase sunlight photolysis of this substance was determined in three test systems which include: (1) 3-L borosilicate flasks exposed to sunlight and laboratory solar simulation, (2) 100-L Tedlar sunlight exposed air sample bags, and (3) 12,800-L Tedlar sunlight exposed chamber studies using a photochemically stable tracer compound. The kinetic results from all systems indicate rapid gas-phase photolysis under midsummer sunlight conditions with observed half-lives being less than 30 minutes. A pronounced increase in transformation rates with increasing volume to surface area suggests photoreactions occur at more rapid rates in the gas-phase. 14C Radiolabeled phorate irradiations resulted in one conversion product, phorate sulfoxide, and this photoproduct accounted for essentially all of the phorate lost.

The effects of the phosphorothioate insecticide fenitrothion on mammalian cytochrome P450-dependent metabolism of estradiol.

Phosphorothioate insecticides, such as fenitrothion, are suicide substrates of cytochromes P450 (P450). These compounds undergo oxidative desulfuration by P450 resulting in the release and subsequent binding of atomic sulfur to the enzyme. Consequently, the P450-dependent metabolism of certain endogenous substrates could be inhibited by exposure to these insecticides. Formation of 2-hydroxyestradiol (2-OHE2), 4-hydroxyestradiol (4-OHE2), 16 alpha-hydroxyestrone (16 alpha-OHE1), and estriol in mammals occurs by P450-dependent hydroxylation of estradiol at various positions on the steroid nucleus. In the present study, pretreatment of male Swiss Webster mice with increasing doses of fenitrothion resulted in dose-dependent biphasic decreases in 2-OHE2 and 4-OHE2 production in mouse hepatic microsomes compared to control, with substantial decreases even at a dosage as low as 7 mg/kg. Fenitrothion pretreatment also resulted in dose-dependent biphasic increases in 16 alpha-OHE1 and estriol production, along with substantial increases in estrone formation, probably as a result of shunting from the inhibition of 2- and 4-hydroxylation. These data suggest that exposure to fenitrothion might alter estradiol metabolism by inhibition of certain P450 isozymes.

The Effects of the Phosphorothioate Insecticide Fenitrothion on Mammalian Cytochrome P450-Dependent Metabolism of Estradiol

Phosphorothioate insecticides, such as fenitrothion, are suicide substrates of cytochromes P450 (P450). These compounds undergo oxidative desulfuration by P450 resulting in the release and subsequent binding of atomic sulfur to the enzyme. Consequently, the P450-dependent metabolism of certain endogenous substrates could be inhibited by exposure to these insecticides. Formation of 2-hydroxyestradiol (2-OHE2), 4-hydroxyestradiol (4-OHE2), 16α-hydroxyestrone (16α-OHE1), and estriol in mammals occurs by P450-dependent hydroxylation of estradiol at various positions on the steroid nucleus. In the present study, pretreatment of male Swiss Webster mice with increasing doses of fenitrothion resulted in dose-dependent biphasic decreases in 2-OHE2 and 4-OHE2 production in mouse hepatic microsomes compared to control, with substantial decreases even at a dosage as low as 7 mg/kg. Fenitrothion pretreatment also resulted in dose-dependent biphasic increases in 16/-OHE1 and estriol production, along with substantial increases in estrone formation, probably as a result of shunting from the inhibition of 2- and 4-hydroxylation. These data suggest that exposure to fenitrothion might alter estradiol metabolism by inhibition of certain P450 isozymes.

Interaction of ethanol and the organophosphorus insecticide parathion

Phosphorothioate insecticides such as parathion ( O, O-diethyl- O- p-nitrophenyl phosphorothioate) undergo P450-dependent oxidative desulfuration, leading to both activation and detoxification of these compounds. Consequently, alterations in P450-dependent oxidative desulfuration may affect the acute toxicities of these insecticides. In the present study, pretreatment of mice with 15% ethanol in the drinking water for 6 days antagonized the acute toxicity of parathion, but not its toxic metabolite paraoxon ( O, O-diethyl- O- p-nitrophenyl phosphate), suggesting that ethanol affected the oxidative desulfuration of this insecticide. The presence of ethanol within hepatic microsomal incubations did not alter the P450-dependent formation of paraoxon (activation) and p-nitrophenol (detoxification), although p-nitrophenol levels were increased in the presence of ethanol as a result of inhibition of its biotransformation to 4-nitrocatechol by CYP2E1. Ethanol exposure reduced hepatic pyruvate levels, but had no effect on levels of lactate, isocitrate, α-ketoglutarate, and malate. Calculation of cytosolic NAD + NADH and cytosolic NADP + NADPH redox ratios did not reveal any detectable difference in redox state between control and ethanol-treated mice. Since ethanol did not alter directly the P450-dependent activation or detoxification of parathion, and did not decrease NADPH levels, ethanol's antagonism of the acute toxicity of parathion may result from reduced availability of O 2.

The effects of phenobarbital pretreatment on the metabolism and toxicity of paraoxon in the mouse.

The effects of induction of various forms of cytochromes P450 by chemicals like phenobarbital on the hepatic oxidative desulfuration and acute toxicity of the phosphorothioate insecticide parathion have been well-characterized. However, the effects of these chemicals on the metabolism and acute toxicity of the active metabolite paraoxon are less understood. In the present study, daily pretreatment of mice with phenobarbital (intraperitoneally 75 mg/kg) for up to eight days resulted in a transient increase in hepatic microsomal A-esterase activity, with a corresponding transient decrease in serum A-esterase activity (A-esterase was defined as hydrolysis of paraoxon which could be inhibited by EDTA). These alterations could be accounted for by a temporary decrease in the rate of secretion of A-esterase from liver. However, the same pretreatment resulted in a sustained protective effect against the acute toxicity of paraoxon. These data suggest that alterations in A-esterase activity as a result of phenobarbital pretreatment cannot account for the observed antagonism of the acute toxicity of paraoxon. Furthermore, these data demonstrate that the protective effect of phenobarbital pretreatment on phosphorothioate insecticides like parathion cannot be attributed exclusively to alterations in oxidative desulfuration of these compounds.

Toxic Interactions Between Fungicides That Inhibit Ergosterol Biosynthesis and Phosphorothioate Insecticides in the Male Rat and Bobwhite Quail (Colinus virginianus)

The potential for toxic interactions between ergosterol biosynthesis-inhibiting fungicides (EBIFs), used in U.S. agriculture or clinically, and phosphorothioate insecticides was assessed in adult male rats and adult male bobwhite quail (Colinus virginianus) by measuring inhibition of plasma butyryl cholinesterase (BChE) following fungicide and insecticide treatment. Male Sprague-Dawley rats (300 g) were administered corn oil or the following EBIFs: propiconazole (400 mg/kg/day), vinclozolin (400 mg/kg/day), clotrimazole (100 mg/kg/day), or ketoconazole (100 mg/kg/day) for 3 days by oral gavage. Forty-eight hours following the final dose, a single bolus of parathion (0.4 mg/kg in corn oil) or malathion (150 mg/kg in corn oil) or corn oil alone was given po. The rats were terminated 12 hr following parathion or 4 hr following malathion dosing. Significant (p < 0.05) inhibition of BChE was observed with parathion and malathion only following clotrimazole treatment. In contrast, when a similar experiment was performed in bobwhite quail dosed with 12 mg/kg malathion following EBIF treatment, significant BChE inhibition was observed following treatment with vinclozolin or ketoconazole, but not with propiconazole or clotrimazole. Induction of cytochrome P450 in rat and quail liver by EBIFs was accompanied by enhanced oxidative desulfuration of malathion, parathion, and diazinon to toxic oxon products. Increased detoxication via oxidative dearylation/esterolytic clevage also occurred. However, while enhanced acute in vivo insecticide toxicity was observed in both species with a number of EBIF-phosphorothioate combinations, EBIF-induced oxidative activation of phosphorothioates by liver microsomes in vitro was not a good predictor of this effect.

Metabolism and acute toxicity of methyl parathion in pen‐reared and wild northern bobwhites

AbstractPesticide registration guidelines in the United States accept pen‐reared northern bobwhites (Colinus virginianus) for acute toxicity testing and consider them representative of wild terrestrial birds. It is not known how well the various pen‐reared bobwhite strains represent their wild counterpart. The metabolic activation, cholinesterase sensitivity, and toxicity of the or‐ganophosphorus insecticide methyl parathion were compared in pen‐reared and wild bobwhites. Phosphorothioate insecticides such as methyl parathion are activated to their anticholinesterase oxygen analogues (oxons) by microsomal monooxygenases. Methyl paraoxon 150 values for whole‐brain cholinesterase were similar (P &gt; 0.05) for pen‐reared and wild bobwhites (60.0‐65.1 nM). Activation of methyl parathion to methyl paraoxon by liver microsomes was measured indirectly by inhibition of brain cholinesterase. Microsomal specific activities were similar (P &gt; 0.05) for male and female pen‐reared and wild birds (1.15‐1.54 nmol min−1 mg protein−1). There were no differences (P&gt; 0.05) in LD50 values between pen‐reared (9.84 mg/kg) and wild (10.22 mg/kg) bobwhites. Brain cholinesterase was depressed 70 to 85% in nonsurvivors and 23 to 35% in survivors. Results suggest that pen‐reared bobwhites are representative of wild bobwhites. However, comparisons with our previous field research demonstrate that sublethal effects seen in the lab can become lethal under natural conditions. Extrapolations from lab to field must be made cautiously.

Accelerated degradation of methyl parathion, parathion and fenitrothion by suspensions from methyl parathion-and p-nitrophenol-treated soils

Soils (an alluvial and a laterite) contained in pots were treated with methyl parathion, fenitrothion or p-nitrophenol at 15 day intervals under flooded or non-flooded (60% WHC) conditions. Suspensions (non-sterile and sterile) of these treated and untreated soils were tested for their ability to degrade methyl parathion, parathion, fenitrothion and diazinon in a mineral salts medium. Only non-sterile suspensions of methyl parathion- and p-nitrophenol-enriched soils (flooded or non-flooded) distinctly effected accelerated hydrolysis of methyl parathion, parathion and fenitrothion; in contrast, diazinon was not hydrolysed by the suspension of methyl parathion-enriched soils. p-Nitrophenol, formed from methyl parathion or parathion, was eventually metabolized to nitrite by the enrichment cultures while 3-methyl-4-nitrophenol, formed from fenitrothion, resisted further degradation. As in soil enrichment cultures, two bacterial isolates, one each from methyl parathion-enriched alluvial and laterite soils (flooded), effected rapid hydrolysis of methyl parathion, parathion and fenitrothion and then metabolized p-nitrophenol and not 3-methyl-4-nitrophenol, to nitrite. Fenitrothion-retreated soils (flooded or non-flooded) were not conditioned for accelerated hydrolysis of fenitrothion and related phosphorothioate insecticides.