Bromelain is an enzyme extract derived from the stems of pineapples, although it exists in all parts of the fresh pineapple.[1] The extract has a history of folk medicine use. As an ingredient, it is used in cosmetics, as a topical medication, and as a meat tenderizer.[1]
The term "bromelain" may refer to either of two protease enzymes extracted from the plants of the family Bromeliaceae, or it may refer to a combination of those enzymes along with other compounds produced in an extract.[1] Bromelain enzymes are called fruit bromelain and stem bromelain.[1]
Although tested in a variety of folk medicine and research models for its possible efficacy against diseases, bromelain has only one approved clinical application issued in 2012 by the European Medicines Agency – a topical medication called NexoBrid, used to remove dead tissue in severe skin burns.[2]
Extract components
| Stem bromelain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.32 | ||||||||
| CAS no. | 37189-34-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Fruit bromelain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.33 | ||||||||
| CAS no. | 9001-00-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Bromelain extract is a mixture of protein-digesting (proteolytic) enzymes and several other substances in smaller quantities. The proteolytic enzymes are sulfhydryl proteases; a free sulfhydryl group of a cysteine amino acid side chain is required for function. The two main enzymes are:
History
The first isolation of bromelain was recorded by the Venezuelan chemist Vicente Marcano in 1891 by fermenting the fruit of pineapple.[3] In 1892, Russell Henry Chittenden, assisted by Elliott P. Joslin and Frank Sherman Meara, investigated the matter more completely,[4] and called it 'bromelin'. Later, the term 'bromelain' was introduced and originally applied to any protease from any member of the plant family Bromeliaceae.
Sources
Bromelain is present in all parts of the pineapple plant (genus Ananas),[5] but the stem is the most common commercial source,[5][6] presumably because usable quantities are readily extractable after the fruit has been harvested.[5]
Production
Produced mainly in parts of the world where pineapples are grown, such as Thailand or Malaysia, bromelain is extracted from the peel, stem, leaves or waste of the pineapple plant after processing the fruit for juice or other purposes.[5][6] The starting material is blended and pressed through a filter to obtain a supernatant liquid containing the soluble bromelain enzyme.[6] Further processing includes purification and concentration of the enzyme.[5]
Physical characteristics
Bromelain is a white to tan powder, soluble in water, and is stable at temperatures of 50–60 °C (122–140 °F).[1]
Temperature stability
After an hour at 50 °C (122 °F), 83% of the enzyme remains active, while at 40 °C (104 °F), practically 100% remains active.[7] 8 minutes at 80 °C (176 °F) is sufficient to almost completely inactivate the enzyme.[7] The proteolytic activity of concentrated bromelain solutions remains relatively stable for at least 1 week at room temperature, with minimal inactivation by multiple freeze-thaw cycles or exposure to the digestive enzyme trypsin.[8]
Uses
Meat tenderizing and other uses
Along with papain, bromelain is one of the most popular proteases to use for meat tenderizing.[9] Bromelain is sold in a powdered form, which is combined with a marinade, or directly sprinkled on the uncooked meat.[9]
Cooked or canned pineapple does not have a tenderizing effect, as the enzymes are heat-labile and denatured in the cooking process. Some prepared meat products, such as meatballs and commercially available marinades, include pineapple and/or pineapple-derived ingredients.[5]
Although the quantity of bromelain in a typical serving of pineapple fruit is probably not significant, specific extraction can yield sufficient quantities for domestic and industrial processing, including uses in baking, anti-browning of cut fruit, textiles and cosmetics manufacturing.[5][9]
Potential medical uses
Bromelain has not been scientifically proven to be effective in treating any diseases and has not been approved by the U.S. Food and Drug Administration for the treatment of any disorder.[10] In the United States, the passage of the Dietary Supplement Health and Education Act (DSHEA, 1994) allows the sale of bromelain-containing dietary supplements, even though efficacy has not been confirmed. Ingestion of bromelain may cause an allergic reaction in some people who are sensitive to pineapples.[1][10]
While there have been studies into the medical use of bromelain, "the majority of [them] have methodological issues that make it difficult to draw definite conclusions", as none definitively established efficacy, recommended dosage, long term safety, or adverse interaction with other medications.[10]
A concentrate of proteolytic enzymes enriched in bromelain is approved in Europe for the debridement (removal of dead tissue) of severe burn wounds under the trade name NexoBrid.[2] Systemic enzyme therapy (consisting of combinations of proteolytic enzymes such as bromelain, trypsin, chymotrypsin, and papain) has been investigated in Europe to evaluate the efficacy in breast, colorectal, and plasmacytoma cancer patients.[11] Bromelain may be effective as an adjunct therapy in relieving symptoms of acute rhinosinusitis in patients not treated with antibiotics.[10][12]
See also
References
- 1 2 3 4 5 6 "Bromelain". PubChem, National Library of Medicine, US National Institutes of Health. 14 September 2019. Retrieved 17 September 2019.
- 1 2 "NexoBrid: concentrate of proteolytic enzymes enriched in bromelain". European Medicines Agency. January 7, 2013.
- ↑ "Vicente Marcano (in Spanish) Quote from Google translate: "New theory about the phenomenon of fermentation": "See also the bromeliad (for Annana bromelia L.) pineapple, which is responsible for many phenomena of fermentation of the fruit. This finding, while not making Marcano, was actually made by him, as later confirmed by R. H. Chittenden of Yale University, who argues that "the bromeliad was discovered by a Venezuelan scholar named Vicente Marcano."". Pioneers of Venezuela, PDVSA-Intevep. 1997. Archived from the original on 2007-03-30. Retrieved 2007-03-04.
- ↑ Chittenden RH, Joslin EP, Meara FS (1892). "On the ferments contained in the juice of the pineapple (Ananassa sativa): together with some observations on the composition and proteolytic action of the juice". Transactions of the Connecticut Academy of Arts and Sciences. 8: 281–308.
- 1 2 3 4 5 6 7 Arshad ZI, Amid A, Yusof F, Jaswir I, Ahmad K, Loke SP (September 2014). "Bromelain: an overview of industrial application and purification strategies" (PDF). Applied Microbiology and Biotechnology. 98 (17): 7283–7297. doi:10.1007/s00253-014-5889-y. PMID 24965557. S2CID 824024.
- 1 2 3 Ketnawa S, Chaiwut P, Rawdkuen S (2012). "Pineapple wastes: A potential source for bromelain extraction". Food and Bioproducts Processing. 90 (3): 385–391. doi:10.1016/j.fbp.2011.12.006.
- 1 2 Jutamongkon R, Charoenrein S (2010). "Effect of Temperature on the Stability of Fruit Bromelain from Smooth Cayenne Pineapple" (PDF). Kasetsart Journal: Natural Science. 44: 943–948. Archived from the original (PDF) on 2014-11-29.
- ↑ Hale LP, Greer PK, Trinh CT, James CL (April 2005). "Proteinase activity and stability of natural bromelain preparations". International Immunopharmacology. 5 (4): 783–793. doi:10.1016/j.intimp.2004.12.007. PMID 15710346.
- 1 2 3 Chaurasiya RS, Sakhare PZ, Bhaskar N, Hebbar HU (June 2015). "Efficacy of reverse micellar extracted fruit bromelain in meat tenderization". Journal of Food Science and Technology. 52 (6): 3870–3880. doi:10.1007/s13197-014-1454-z. PMC 4444899. PMID 26028772.
- 1 2 3 4 "Bromelain". National Center for Complementary and Integrative Health, US National Institutes of Health. 24 September 2017. Retrieved 17 December 2018.
- ↑ Beuth J (December 2008). "Proteolytic enzyme therapy in evidence-based complementary oncology: fact or fiction?". Integrative Cancer Therapies. 7 (4): 311–316. doi:10.1177/1534735408327251. PMID 19116226.
- ↑ Guo R, Canter PH, Ernst E (October 2006). "Herbal medicines for the treatment of rhinosinusitis: a systematic review". Otolaryngology–Head and Neck Surgery. 135 (4): 496–506. doi:10.1016/j.otohns.2006.06.1254. PMID 17011407. S2CID 42625009.
External links
- The MEROPS online database for peptidases and their inhibitors:
- Bromelains at the U.S. National Library of Medicine Medical Subject Headings (MeSH)