Bromelain is an enzyme 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 folk medicine and research models for its possible efficacy against diseases, the only approved clinical application for bromelain was issued in 2012 by the European Medicines Agency for a topical medication called NexoBrid used to remove dead tissue in severe skin burns. [1] There is no other established application for bromelain as a nutraceutical or drug.
Stem bromelain | |||||||||
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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 | ||||||||
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Fruit bromelain | |||||||||
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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 | ||||||||
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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:
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.
Bromelain is present in all parts of the pineapple plant (Ananas sp.), [4] but the stem is the most common commercial source, [4] [5] presumably because usable quantities are readily extractable after the fruit has been harvested. [4]
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. [4] [5] The starting material is blended and pressed through a filter to obtain a supernatant liquid containing the soluble bromelain enzyme. [5] Further processing includes purification and concentration of the enzyme. [4]
After an hour at 50 °C (122 °F), 83% of the enzyme remains, while at 40 °C (104 °F), practically 100% remains. [6] The proteolytic activity of concentrated bromelain solutions remains relatively stable for at least 1 week at room temperature, and multiple freeze-thaw cycles or exposure to the digestive enzyme trypsin have little effect on it. [7]
Along with papain, bromelain is one of the most popular proteases to use for meat tenderizing. [8] Bromelain is sold in a powdered form, which is combined with a marinade, or directly sprinkled on the uncooked meat. [8]
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. [4]
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. [4] [8]
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 . [1]
Bromelain has not been scientifically proven to be effective in treating any other diseases and it has not been approved by the U.S. Food and Drug Administration for the treatment of any disorder. 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.
While there have been studies which positively correlated the use of bromelain with reduction of symptom severity in osteoarthritis, [9] [10] "[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. [11] [12]
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. [13]
Bromelain may be effective as an adjunct therapy in relieving symptoms of acute rhinosinusitis in patients not treated with antibiotics. [12] [14]
Bromelain is also claimed as a tooth plaque removal enhancer in toothpastes. [15]
The pineapple is a tropical plant with an edible fruit; it is the most economically significant plant in the family Bromeliaceae.
The papaya, papaw, or pawpaw is the plant species Carica papaya, one of the 21 accepted species in the genus Carica of the family Caricaceae, and also the name of its fruit. It was first domesticated in Mesoamerica, within modern-day southern Mexico and Central America. It is grown in several countries in regions with a tropical climate. In 2022, India produced 38% of the world's supply of papayas.
In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.
Transglutaminases are enzymes that in nature primarily catalyze the formation of an isopeptide bond between γ-carboxamide groups ( -(C=O)NH2 ) of glutamine residue side chains and the ε-amino groups ( -NH2 ) of lysine residue side chains with subsequent release of ammonia ( NH3 ). Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intramolecular (within the same molecule) reaction can happen. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). The reaction is
Papain, also known as papaya proteinase I, is a cysteine protease enzyme present in papaya and mountain papaya. It is the namesake member of the papain-like protease family.
The mountain papaya also known as mountain pawpaw, papayuelo, chamburo, or simply "papaya" is a species of the genus Vasconcellea, native to the Andes of northwestern South America from Colombia south to central Chile, typically growing at altitudes of 1,500–3,000 metres (4,900–9,800 ft).
Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.
Collagenases are enzymes that break the peptide bonds in collagen. They assist in destroying extracellular structures in the pathogenesis of bacteria such as Clostridium. They are considered a virulence factor, facilitating the spread of gas gangrene. They normally target the connective tissue in muscle cells and other body organs.
Fruit bromelain is an enzyme. This enzyme catalyses the following chemical reaction
Ficain also known as ficin, debricin, or higueroxyl delabarre is a proteolytic enzyme extracted from the latex sap from the stems, leaves, and unripe fruit of the American wild fig tree Ficus insipida.
Actinidain is a type of cysteine protease enzyme found in fruits including kiwifruit, pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases.
Proteases are in use, or have been proposed or tried, for a number of purposes related to medicine or surgery. Some preparations involving protease have undergone successful clinical trials and have regulatory authorization; and some further ones have shown apparently useful effects in experimental medical studies. Proteases have also been used by proponents of alternative therapies, or identified in materials of traditional or folk medicine. A serine protease of human origin, activated protein C, was produced in recombinant form and marketed as Drotrecogin alfa and licensed for intensive-care treatment of severe sepsis. It was voluntarily withdrawn by the manufacturer in 2011 after being shown to be ineffective.
Chymopapain is a proteolytic enzyme isolated from the latex of papaya. It is a cysteine protease which belongs to the papain-like protease (PLCP) group. Because of its proteolytic activity, it is the main molecule in the process of chemonucleolysis, used in some procedures like the treatment of herniated lower lumbar discs in the spine by a nonsurgical method.
Cucumisin is an enzyme. This enzyme catalyzes hydrolysis of a wide range of proteins. It has been identified as an allergen in humans.
Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Ananain is an enzyme. This enzyme catalyses the following chemical reaction
Zingibain, zingipain, or ginger protease is a cysteine protease enzyme found in ginger rhizomes. It catalyses the preferential cleavage of peptides with a proline residue at the P2 position. It has two distinct forms, ginger protease I (GP-I) and ginger protease II (GP-II).
Bromelain, a concentrate of proteolytic enzymes from the pineapple plant, is used in medicine. It is approved in the European Union for the debridement of severe burn wounds under the brand name Nexobrid. It was developed by MediWound.
Tenderness is a quality of meat gauging how easily it is chewed or cut. Tenderness is a desirable quality, as tender meat is softer, easier to chew, and generally more palatable than harder meat. Consequently, tender cuts of meat typically command higher prices. The tenderness depends on a number of factors including the meat grain, the amount of connective tissue, and the amount of fat. Tenderness can be increased by a number of processing techniques, generally referred to as tenderizing or tenderization.
Papain-like proteases are a large protein family of cysteine protease enzymes that share structural and enzymatic properties with the group's namesake member, papain. They are found in all domains of life. In animals, the group is often known as cysteine cathepsins or, in older literature, lysosomal peptidases. In the MEROPS protease enzyme classification system, papain-like proteases form Clan CA. Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile.