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Bromelain
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A jar of meat tenderizer containing bromelain
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| Effective temperature |
40–60°C |
| Optimal temperature |
50–60°C |
| Deactivation temperature |
approximately above 65°C |
| Effective pH |
4.0–8.0 |
| Optimal pH |
4.5–5.5 |
Bromelain is a protein extract derived from the stems of pineapples, although it exists in all parts of the fresh plant and fruit. The extract has a history of folk medicine use. As a culinary ingredient, it may be used as a meat tenderizer.
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.
Although tested in a variety of research models for its possible efficacy against diseases, bromelain has no established research evidence as a nutraceutical or drug.[1] Limited evidence exists for possible effectiveness of a product used to reduce pain from osteoarthritis that combines bromelain with trypsin and rutin.[1]
Contents
- 1 Extract components
- 2 History
- 3 Sources
- 4 Uses
- 4.1 Potential medical uses
- 4.2 Meat tenderizing
- 5 Production
- 6 Temperature stability
- 7 See also
- 8 References
- 9 External links
| Stem bromelain |
| Identifiers |
| EC number |
3.4.22.32 |
| CAS number |
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 |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
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| Fruit bromelain |
| Identifiers |
| EC number |
3.4.22.33 |
| CAS number |
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 |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
Bromelain extract is a mixture of protein-digesting (proteolytic) enzymes or proteases, and several other substances in smaller quantities. The proteolytic enzymes are sulfhydryl proteases, since a free sulfhydryl group of a cysteine side chain is required for function. The two main enzymes are:
- Stem bromelain - EC 3.4.22.32
- Fruit bromelain - EC 3.4.22.33
History
Pineapples have a long tradition as a medicinal plant among the natives of South and Central America. The first isolation of bromelain was recorded by the Venezuelan chemist Vicente Marcano in 1891 by fermenting the fruit of pineapple.[2] In 1892, Russell Henry Chittenden, assisted by Elliott P. Joslin and Frank Sherman Meara, investigated the matter more completely,[3] 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 (Ananas sp.),[citation needed] but the stem is the most common commercial source,[citation needed] presumably because large quantities are readily available after the fruit has been harvested.
Uses
Potential medical uses
Main article: Bromelain (pharmacology)
See also: Proteases (medical and related uses)
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.[4]
Bromelain has not been scientifically proven to be effective in any other diseases and it has not been licensed by the Food and Drug Administration for the treatment of any disorder.[1]
Available in some countries as a product under the name Ananase, bromelain began its reputation for various uses in folk medicine.
As a potential anti-inflammatory agent, it may be useful for treating arthritis,[5] but has neither been confirmed in human studies for this use, nor is it approved with a health claim for such an effect by the Food and Drug Administration or European Food Safety Authority.[1]
While there have been studies which positively correlated the use of bromelain with reduction of symptom severity in osteoarthritis,[6][7] "[t]he majority of the studies 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.[1][8]
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 of proteolytic enzymes in the treatment of breast, colorectal, and plasmacytoma cancer patients.[9]
Bromelain supplements, when taken with other medications (amoxicillin, antibiotics, anticoagulant/antiplatelet drugs), may increase the risk associated with heart rate, blood clotting, and bleeding after surgery.[1]
Meat tenderizing
Along with papain, bromelain is one of the most popular proteases to use for meat tenderizing. Bromelain is sold in a powdered form, which is combined with a marinade, or directly sprinkled on the uncooked meat.
Cooked or canned pineapple does not have a tenderizing effect, as the enzymes are heat-labile and destroyed in the cooking process. Some prepared meat products, such as meatballs and commercially available marinades, include pineapple and/or pineapple-derived ingredients.[citation needed]
Production
Bromelain is produced in Thailand, Taiwan, and other tropical parts of the world where pineapples are grown. It is prepared from the stem of the pineapple plant after harvesting the fruit for other purposes. The stem is peeled, crushed, and pressed to obtain the juice containing the soluble bromelain enzyme. Further processing includes purification and concentration of the enzyme.
Temperature stability
At the optimum temperature, the enzyme acts the fastest, but (at least the fruit variant) is destroyed within few minutes. After an hour at 50 °C (122 °F), 83% of the enzyme remains, while at 40 °C (104 °F), practically 100% remains.[10] As a result of this, the optimum temperature for maximum cumulated activity over time is 35-45 °C. At room temperature, the enzyme can survive at least a week even under multiple freeze-thaw cycles.[11]
See also
References
- ^ a b c d e f "Bromelain". MedlinePlus, US National Institutes of Health. 2014. Retrieved 14 November 2014.
- ^ "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 Dr. RH Chittenden, of Yale University, who argues that "the bromeliad was discovered by a Venezuelan scholar named Vicente Marcano."". Pioneers of Venezuela, PDVSA-Intevep. 1997.
- ^ Chittenden, R H; Elliott P Joslin; Frank Sherman Meara (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.
- ^ "EPAR summary for the public: NexoBrid". European Medicines Agency. December 2012.
- ^ Brien S, Lewith G, Walker A (2004). "Bromelain as a Treatment for Osteoarthritis: a Review of Clinical Studies". Evidence-based complementary and alternative medicine: eCAM. 1 (3): 251–257. doi:10.1093/ecam/neh035. PMC 538506. PMID 15841258.
- ^ Walker AF, Bundy R, Hicks SM, Middleton RW (2002). "Bromelain reduces mild acute knee pain and improves well-being in a dose-dependent fashion in an open study of otherwise healthy adults". Phytomedicine 9 (8): 681–6. doi:10.1078/094471102321621269. PMID 12587686.
- ^ Hale LP, Greer PK, Trinh CT, James CL (2005). "Proteinase activity and stability of natural bromelain preparations". Int Immunopharmacol 5 (4): 783–93. doi:10.1016/j.intimp.2004.12.007. PMID 15710346.
- ^ Brien S, Lewith G, Walker A, Hicks SM, Middleton D (2004). "Bromelain as a Treatment for Osteoarthritis: a Review of Clinical Studies". Evid Based Complement Alternat Med 1 (3): 251–7. doi:10.1093/ecam/neh035. PMC 538506. PMID 15841258.
- ^ Beuth J (2008). "Proteolytic enzyme therapy in evidence-based complementary oncology: fact of fiction?". Integr Cancer Ther 7 (4): 311–316. doi:10.1177/1534735408327251. PMID 19116226.
- ^ Jutamongkon R, Charoenrein S (2010). "Effect of Temperature on the Stability of Fruit Bromelain from Smooth Cayenne Pineapple". Kasetsart J. (Nat. Sci.) 44: 943–8.
- ^ Hale, Laura P.; Greer, Paula K.; Trinh, Chau T.; James, Cindy L. (2005). "Proteinase activity and stability of natural bromelain preparations". International Immunopharmacology 5 (4): 783–93. doi:10.1016/j.intimp.2004.12.007. PMID 15710346.
External links
- The MEROPS online database for peptidases and their inhibitors: Stem Bromelain:C01.005, Fruit Bromelain:C01.028
- Bromelains at the US National Library of Medicine Medical Subject Headings (MeSH)
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Proteases: cysteine proteases (EC 3.4.22)
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| Caspase |
- Caspase 1
- Caspase 2
- Caspase 3
- Caspase 4
- Caspase 5
- Caspase 6
- Caspase 7
- Caspase 8
- Caspase 9
- Caspase 10
- Caspase 12
- Caspase 13
- Caspase 14
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| Fruit-derived |
- Papain
- Ficain
- Bromelain
- Actinidain
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| Calpain |
- CAPN1
- CAPN2
- CAPN3
- CAPN5
- CAPN6
- CAPN7
- CAPN8
- CAPN9
- CAPN10
- CAPN11
- CAPN12
- CAPN13
- CAPN14
- CAPNS1
- CAPNS2
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| Cathepsin |
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| Other |
- Clostripain
- Cancer procoagulant
- Separase
- Autophagin
- Cruzipain
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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