BROMELAIN ALLERGY
Key Allergens
Bromelain is an enzyme, which is found in pineapples and is often extracted and used in cosmetics, meat rubs and marinades. More recently it is being sold as a health supplement.
The enzyme is found in all parts of the pineapple, but in higher concentrations in the stems. The enzyme is a protease, which means it breaks down another substance, in this instance it breaks down some of the bonds in meat, making it more tender to eat when cooked.
When eating fresh pineapple it is the bromelain enzyme which gives you the tingly/itchy sensation in your mouth and throat. This can be mistaken for an allergic reaction. You can read more on the
Pineapple Page.
Bromelain is actually a defined allergen with the World Health Organization (WHO) - Ana c 2, so is well documented as causing allergic reactions.
The enzyme is a papain, which is the active constituent in latex-related fruits, this is the protein which can cause cross reactivity with
latex.
Bromelain is an allergen in itself, but the fresh pineapple from which it is extracted also contain
profilin proteins. These are more easily damaged with heat and processing than other allergens, so are less likely to be the cause of an allergic reaction to bromelain.
Food Intolerances

Bromelain, like pineapple, is a low FODMAP food.
FODMAP stands for
Fermentable
oligosaccharides,
disaccharides,
monosaccharides
and
polyols. Foods high in FODMAPs can cause symptoms of food intolerance, affecting the gastro intestinal system and this can be mistaken for a true IgE food allergy.
Like pineapple, bromelain is thought to also be high in
salicylates. Salicylates have the potential to cause worsening of asthma, swelling, itching and hives as well as food intolerance symptoms in people who are sensitive to salicylates.
You can read more about
Food Intolerances on the dedicated Food Intolerance Page.
Associated Syndromes
Bromelain is linked to a worsening of asthma symptoms and irritation of dermatitis.
It is also linked to
Latex Food Syndrome. This is where a person who has a latex allergy will get similar symptoms if they eat food with similarly shaped proteins.
Allergy to pineapple and bromelain is sometimes linked to
Celery-Mugwort-Spice Syndrome as the sensitising allergen is a profilin protein. This can cause allergic reactions in people eating lots of seemingly unrelated foods.
Cross Reactivity
Foods linked to Latex Food Syndrome are ones which contain the allergens hevein, chitinase and papains. Papain is most commonly linked with papaya.
Those with a sensitivity to chitinase may have linked allergies to foods which contain high levels of chitinase like avocado, banana, chestnuts, mango, corn (maize), kiwi, papaya, pomegranate, tamarind, cashews, beetroot, chard, spinach and tomatoes. Chitinase allergens can also affect the airways and can be found in coffee, cockroaches and dust mites.
Hevein proteins are found in rubber trees (as a contact allergen) and in turnip (as a food allergen).
Profilin proteins are found in celery, peanut, soyabeans, walnut, lupin, almonds, mustard, hazelnut, kiwi, pineapple, chilli, melon, orange, strawberry, lychee, apple, banana, aubergine (eggplant), peach, pear, tomato, dates, cherry and carrot.
These food lists are not exhaustive, you can see the most up to date food lists on the Cross Reactivity Tool.
Resources
Websites
Web MD - Bromelain
Allergen Encyclopedia - Pineapple
Science Direct - Bromelain
Science Direct - Papain
Articles and Journals
Plant and Arthropod IgE-Binding Papain-like Cysteine Proteases: Multiple Contributions to Allergenicity, 2024
Efficacy and safety of bromelain: A systematic review and meta-analysis, 2023
Bromelain a Potential Bioactive Compound: A Comprehensive Overview from a Pharmacological Perspective, 2021
Occupational allergies to bromelain, 2007
Bromelain, 2006
Sensitization to cross-reactive carbohydrate determinants and the ubiquitous protein profilin: mimickers of allergy, 2004
Asthma caused by bromelain: an occupational allergy, 1998
Let me know if you found any of these interesting or useful.
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