Cutting an onion breaks open its cells and lets an enzyme reach a sulfur compound it is normally kept apart from2, 14. A second enzyme then turns the product into a volatile irritant called syn-propanethial S-oxide1, 2. When it reaches your eyes, it is thought to stimulate nerve endings in the cornea, and your body answers with tears to wash it away7, 8, 10.
A chemical trap that springs when you cut
Inside an intact onion, the ingredients for tears are stored apart. A sulfur compound sits in the cell's cytoplasm, while the enzyme alliinase is usually described as tucked away in a separate compartment, the vacuole14. Slicing ruptures the cells, and the two meet7, 14. Alliinase splits the sulfur compound, called isoalliin, into a short-lived, highly reactive molecule: 1-propenylsulfenic acid2, 3, 14.
A second enzyme, lachrymatory factor synthase (LFS), rearranges that acid into syn-propanethial S-oxide, the 'lachrymatory factor' or tear factor1, 2. For a long time, chemists assumed this step happened on its own1, 2. In 2002, Japanese researchers showed that the onion uses a dedicated enzyme for it1, 2. Sulfenic acid that LFS does not convert instead forms thiosulfinates, compounds linked to the sharp smell of freshly cut onion3, 6, 7. In other words, the tear factor is not stored: it is made on demand, the moment the knife breaks the cells1, 2, 14.
From cutting board to eyeball
The tear factor is volatile, so it escapes into the air2, 9. Instruments above freshly cut onions detected it right away, and it faded within roughly 10 to 30 minutes6.
High-speed filming suggests the air is not the only route. Cornell engineers found that a knife pressing on an onion builds up pressure in the tissue until the thin skin of a layer bursts, spraying fine droplets at up to about 40 meters per second10, 11. Blunter blades produced up to about 40 times more droplets, and faster cuts about four times more10. The researchers suggest that these hovering droplets may carry the irritant toward the eyes, an idea first proposed in 194710.
Once the irritant reaches the eye, it is thought to stimulate free nerve endings in the cornea that belong to the trigeminal nerve7, 8. The brain reads the signal as burning and reflexively tells the tear glands to flush the eye7, 8.
Why would an onion do this?
Scientists see the whole sulfur system as a defense, part of the plant's chemical warfare against microbes and animals: harmless while stored, irritating the moment something bites in2, 14. Garlic mostly stores a slightly different sulfur compound and lacks LFS, so its sulfenic acids turn into thiosulfinates such as allicin instead of the tear factor1, 3, 12.
In 2008, researchers used genetic engineering to silence the LFS gene in onions. Enzyme activity dropped by up to about 1,500-fold, and the cut onions released far less tear factor and more thiosulfinate-derived sulfur compounds4. A Japanese team later produced a tearless onion without genetic engineering by inducing random mutations with an ion beam. In those plants, the first enzyme, alliinase, was barely made at all, while LFS worked normally5.
What we're not sure about
Which receptor is involved? Sulfur compounds from garlic such as allicin activate the pain-sensing channels TRPA1 and TRPV1 on sensory nerves, and crushed-onion extract also switches on TRPV112, 13. We could not find a study that tested syn-propanethial S-oxide itself on these channels, so its exact molecular target remains open12, 13.
The sulfuric acid story: some explainers say the tear factor reacts with the eye's moisture to form sulfuric acid8, 9. Others describe nerve endings detecting the compound directly7, 10, and in water it is reported to break down into propanal6. We found no direct measurement of sulfuric acid in the eye, so this claim is unproven.
The defense idea is plausible, but much of the evidence is indirect: a 2024 study proposing a two-layer onion defense relied on gene-activity and chemistry data, not tests with pests14.
Sources
- Imai S, Tsuge N, Tomotake M, Nagatome Y, Sawada H, Nagata T, Kumagai H (2002): Plant biochemistry: An onion enzyme that makes the eyes water. Nature 419:685
- Silvaroli JA, Pleshinger MJ, Banerjee S, Kiser PD, Golczak M (2017): Enzyme That Makes You Cry - Crystal Structure of Lachrymatory Factor Synthase from Allium cepa. ACS Chemical Biology 12:2296-2304
- Arakawa T, Sato Y, Takabe J, Masamura N, Kato M, Aoyagi M, Kamoi T, Tsuge N, Imai S, Fushinobu S (2017): Structure of Allium lachrymatory factor synthase elucidates catalysis on sulfenic acid substrate. bioRxiv (preprint)
- Eady CC, Kamoi T, Kato M, Porter NG, Davis S, Shaw M, Kamoi A, Imai S (2008): Silencing onion lachrymatory factor synthase causes a significant change in the sulfur secondary metabolite profile. Plant Physiology 147:2096-2106
- Kato M, Masamura N, Shono J, Okamoto D, Abe T, Imai S (2016): Production and characterization of tearless and non-pungent onion. Scientific Reports 6:23779
- Lokke MM, Edelenbos M, Larsen E, Feilberg A (2012): Investigation of Volatiles Emitted from Freshly Cut Onions (Allium cepa L.) by Real Time Proton-Transfer Reaction-Mass Spectrometry (PTR-MS). Sensors 12:16060-16076
- Scott T, University of Delaware (1999): What is the chemical process that causes my eyes to tear when I peel an onion? Scientific American
- Gibbins I, Flinders University (2012): Monday's medical myth: chewing gum stops onion tears. The Conversation
- Burnham PM (2007): Propanethial S-oxide - The Lachrymatory Factor in Onions. Molecule of the Month, University of Bristol School of Chemistry
- Wu Z, Hooshanginejad A, Wang W, Hui C-Y, Jung S (2025): Droplet outbursts from onion cutting. PNAS 122(42):e2512779122
- Ramanujan K (2025): 'Mist opportunity' reveals how onions make cooks cry. Cornell Chronicle, Cornell University
- Bautista DM, Movahed P, Hinman A, Axelsson HE, Sterner O, Hogestatt ED, Julius D, Jordt SE, Zygmunt PM (2005): Pungent products from garlic activate the sensory ion channel TRPA1. PNAS 102:12248-12252
- Salazar H, Llorente I, Jara-Oseguera A, Garcia-Villegas R, Munari M, Gordon SE, Islas LD, Rosenbaum T (2008): A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic. Nature Neuroscience 11:255-261
- Cho H, Park JY, Kim DH, Han J, Natesan K, Choi M-S, Lee S-K, Kim J, Cho K, Ahn BO (2024): Understanding the defense mechanism of Allium plants through the onion isoallicin-omics study. Frontiers in Plant Science 15:1488553
Researched and independently fact-checked on 22 October 2026. Found a mistake? Tell us at querigami@gmail.com and we will correct it here.
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