Last updated on July 20, 2026 · Originally published November 25, 2019
Most approaches to pesticide contamination in cannabis try to remove the offending molecules — filter them out, separate them chromatographically, or avoid them by starting with clean flower. In 2019, a startup based on research from NYU professor Jin Kim Montclare’s laboratory proposed a different approach: rather than physically removing organophosphate pesticides, use an engineered enzyme to break them down into less toxic products that could then be washed away.
The startup, Brooklyn Bioscience, received a National Science Foundation grant to commercialize the technology for organophosphate decontamination, naming cannabis among several potential agricultural markets alongside crops like wine grapes and tea. At the center of the work is a naturally occurring enzyme called phosphotriesterase, or PTE. Enzymes are biological catalysts — proteins that speed up specific chemical reactions — and PTE is notably good at hydrolyzing susceptible bonds found in many organophosphate pesticides.
What Are Organophosphates, and Why Target Them?
Organophosphates have long been a major class of agricultural insecticides, historically adopted in part because many were less environmentally persistent than the older organochlorine pesticides they replaced — though persistence varies considerably among compounds and conditions. They’re also genuinely hazardous: the same mechanism that kills insects — disrupting the nervous system by inhibiting an enzyme called acetylcholinesterase — makes them toxic to humans at sufficient exposure. Their regulatory status varies: ethyl parathion has been removed from US use, chlorpyrifos and diazinon have lost many former applications, and malathion remains registered for agricultural and mosquito-control uses under risk-management requirements. Cannabis presents an added concern, because residues may be inhaled after heating, and some can co-extract with cannabinoids during concentrate production.
Jin Kim Montclare, professor in the Department of Chemical and Biomolecular Engineering
PTE targets susceptible bonds around the phosphorus center of many organophosphate compounds. Using water, it hydrolyzes those bonds and converts susceptible parent pesticides into products that are typically much weaker acetylcholinesterase inhibitors — though those products would still require analytical and toxicological verification. And PTE doesn’t act equally well on every organophosphate: its efficiency depends heavily on the compound’s structure, which is one reason researchers engineer new variants. It’s a mechanism fundamentally different from physical removal — rather than separating the pesticide from the material, it chemically dismantles it.
The Engineering Problem
A naturally occurring enzyme doesn’t automatically make a practical decontamination tool. As Montclare put it in describing the work, “the two problems facing PTE were heat stability and promiscuity” — promiscuity being the enzyme’s ability to break down a variety of organophosphate pesticides rather than just a single one. A version that unravels at moderate temperatures, or that only breaks down one specific compound, would have limited usefulness as a broad field treatment.
The team addressed stability at the enzyme’s structural core. “The key to the first problem lay in the interface between the two parts of the enzyme,” Montclare explained. “We mutated the part of the enzyme at the interface and added a new fluorinated amino acid, which is not found in naturally occurring proteins, to improve its stability.” That approach — incorporating a fluorinated, non-standard amino acid and using computational protein design — produced variants that fold better and hold up longer and at higher temperatures than natural PTE.
Broadening the enzyme’s reach created a different challenge. The researchers altered the chemistry around PTE’s active-site pocket so that a wider range of organophosphate structures could fit, but the resulting variants became more prone to aggregation during production. That shifted part of the engineering effort toward improving the enzyme’s solubility in water.
Computational design was central to making the work tractable. “Computational design allows us to predict how the enzyme will behave with every mutation, thus saving us valuable time and resources,” Montclare noted. With a protein sequence of roughly 400 amino-acid residues, the analysis let the team identify the 10 to 15 most promising sites for mutation rather than testing changes blindly. The proposed Brooklyn Bioscience formulation used the engineered enzyme as a crystalline powder that could be mixed with water and applied as an aqueous crop treatment. That makes it conceptually closer to a decontamination wash than to chromatographic remediation — but it also means the technology shouldn’t be assumed to work directly inside a finished cannabis extract, where the enzyme’s water-based chemistry would have to contend with a hydrophobic oil.
How Close Is This to Reality?
This is promising research, and it’s important to frame it as exactly that rather than a solved problem. Enzymatic detoxification of organophosphates is an active scientific field with decades of work behind it — PTE’s structure was first characterized in the 1990s, and its potential for decontaminating pesticides and even chemical-warfare nerve agents has been studied extensively. Montclare’s own more recent work, in fact, has focused on engineering PTE against V-series nerve agents such as VX and VR rather than on cannabis specifically. Despite those early commercial plans, publicly available evidence does not show that the cannabis application progressed to a validated commercial process.
For cannabis use in particular, several questions would still require validation: how effectively the enzyme works on real flower rather than simplified laboratory substrates; whether waxes and resin limit the enzyme’s contact with the pesticide; whether treatment affects cannabinoids, terpenes, aroma, or microbial stability; whether the enzyme and its reaction products can be removed completely afterward; and whether the process reliably brings every targeted residue below regulatory limits. None of those points has yet been established in published cannabis-specific research.
It also wouldn’t be a universal fix even if validated. PTE acts on organophosphates specifically; it does nothing for the other contaminant classes that show up in cannabis, including the fungicide myclobutanil, which belongs to an entirely different chemical family. Enzymatic detox would be one tool among several rather than a single answer.
For the more established, physical approaches to the same problem — and an honest account of what they can and can’t achieve — see our overview of how pesticides are removed from cannabis extracts.
Originally published 2019. Updated July 2026 to correct the researcher’s name and the Brooklyn Bioscience origin of the work, clarify the enzyme chemistry, and specify what remains unvalidated for cannabis use.
