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Bacterium · Organophosphate hydrolyzer

Brevundimonas diminuta

Source of organophosphate hydrolase, the single most studied pesticide-destroying enzyme in science. The bacterium can grow using a parathion insecticide as its phosphate source.

Identified in Plant JuiceIndependent DNA sequencing · Biome Makers

What published studies document
ContaminantWhat the research documents
Pesticides & herbicidesOrganophosphate hydrolase (OPH) cleaves the triester bond of organophosphate insecticides

From published research on the species, not tests of an Elm Dirt product. Studies often work with one strain, and sequencing identifies species, so results on a site are measured on that site.

On this page (5 sections)
  1. What it is
  2. What the research shows
  3. How it works
  4. Where it fits
  5. Studies

What it is

Brevundimonas diminuta is a small soil and water bacterium, notable here for one enzyme.

Peer-reviewed research shows Brevundimonas diminuta can hydrolyze organophosphate insecticides. It is one of the 291 microbial species identified in Plant Juice by independent lab analysis (Biome Makers).

What the research shows

The key enzyme here is organophosphate hydrolase, which is encoded by the opd gene and breaks the central bond in organophosphate pesticides. The plasmid behind parathion hydrolysis in this organism was identified in 1982 [3], and the gene was cloned and sequenced in 1988 [2]. It is still the benchmark enzyme for destroying organophosphates.

The bacterium gets something out of the reaction. Later work showed the enzyme is a lipoprotein that works with the cell’s phosphate transport system, so the bacterium can grow using an organophosphate insecticide as its phosphate source and in effect feeds on the pesticide [1].

How it works

Organophosphates kill insects by blocking a nerve enzyme, and that same chemistry makes them toxic to people. Organophosphate hydrolase splits the molecule’s central phosphorus-oxygen triester bond with water in a single step, and that one cut removes the toxic action. It works fast and needs neither oxygen nor a feeding substrate, unlike the cometabolic solvent pathways elsewhere in this library.

Breaking the parent molecule is only the first step. Some organophosphate metabolites are toxic and persistent, and one is antimicrobial enough to slow the organisms degrading it [4]. Sampling should include the breakdown products.

Where it fits

This is the organism organophosphate hydrolase was first found in. It suits farm ground, orchards and chemical-handling areas with an organophosphate history; see pesticides and herbicides. On a site, results take months to a year or more and are confirmed by independent lab testing.

Studies

  1. Parthasarathy S, et al. (2016). Organophosphate hydrolase is a lipoprotein and interacts with Pi-specific transport system to facilitate growth of Brevundimonas diminuta using OP insecticide as source of phosphate. Journal of Biological Chemistry 291(14):7774–7785. doi:10.1074/jbc.M116.715110
  2. McDaniel CS, Harper LL, Wild JR (1988). Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase. Journal of Bacteriology 170(5):2306–2311. doi:10.1128/jb.170.5.2306-2311.1988
  3. Serdar CM, Gibson DT, Munnecke DM, Lancaster JH (1982). Plasmid involvement in parathion hydrolysis by Pseudomonas diminuta. Applied and Environmental Microbiology 44(1):246–249. doi:10.1128/aem.44.1.246-249.1982
  4. Armenova N, et al. (2023). Microbial detoxification of residual pesticides in fermented foods: current status and prospects. Foods 12(6):1163. doi:10.3390/foods12061163

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