Ficain

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Ficain
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Crystallographic structure of ficain from Ficus carica, rainbow colored, N-terminus blue, C-terminus red.
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EC no. 3.4.22.3
CAS no. 9001-33-6
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Ficain also known as ficin, debricin, or higueroxyl delabarre (EC 3.4.22.3) is a proteolytic enzyme extracted from the latex sap from the stems, leaves, and unripe fruit of the American wild fig tree Ficus insipida . [1] [2] [3] [4]

Contents

Ficain was originally called ficin, and ficin was originally a mixture of closely related cysteine endopeptidases produced from any species of the genus Ficus , before the terminology was restricted to a specific cysteine endopeptidase enzyme from a specific species.

Cysteine endopeptidases are a group of enzymes that also include the more distantly related papain derived from papaya latex, bromelase (bromelain) extracted from pineapple stem, calpain, caspases, cathepsin B, and chymopapain. [5] Cysteine endopeptidases with similar properties known generically as ficins are present in other members of the genus Ficus, and many species appear to contain multiple types of these enzymes. Somewhat confusingly, the terms ficain and ficin are often treated as synonyms.

Ficain is in the MEROPS clan CA, family C1, subfamily C1A, peptidase C01.006. [5]

Nomenclature

The name ficin was first used by Robbins in 1930 to describe a purified substance with anthelmintic activity isolated from any member of the fig genus. [6] The Enzyme Commission of the International Union of Biochemistry and Molecular Biology (IUBMB) originally assigned EC 3.4.4.12 as ficin in 1961, which was transferred to 3.4.22.3 and renamed to ficain in 1972, making the two term synonymous at the time. [7] Because the proteolytic enzymes from other members of the genus Ficus have not been fully characterized, the IUBMB in 1992 recommended the term ficain be restricted to the specific main proteolytic enzyme found in the ficin powder produced from F. glabrata , [2] a taxon which has since been synonymised with F. insipida. [8] However IUBMB Enzyme Nomenclature database continues to list ficin as a synonym of ficain [7] and the two terms are often used interchangeably.

Applications

Purified ficin is a white powder that was first produced in 1930. It was initially observed how intestinal nematodes dissolved in a ficin solution, which arose interest in the product at the time as an anthelmintic, although it was not widely adopted. [2] Purified ficin is not actually 'pure', it is a mix of different enzymes and can be produced from many different species of Ficus. [2] A commonly used ficin is made from the latex of the common fig and consists of a mixture of several isoforms. [5] [9] Up to ten different proteolytic enzymes were found in one study from that species alone, [2] and it even appears that different cultivars of common fig contain different ratios of these enzymes. [10] The milky sap of the common fig also contains furanocoumarins (psoralen), although oddly enough these are found chiefly in the sap of the leaves and shoots, but not in the sap of the fruits. [11] One factor which may account for this is that psoralen and other furanocoumarins are primarily deterrents against herbivory, acting as photosensitizing agents to induce phytophotodermatitis. Psoralen's absence in fruit sap is consistent with the fact that the fruit of endozoochorous plants represents a relatively rare instance where herbivory is encouraged by the plant.

Although later research found it to be ineffective and potentially unhealthy as an anthelmintic, [2] [3] it later found numerous medical and industrial uses. It is used for cleaning in the production of stitching material for sutures, to prepare animal arteries before transplantation into humans, [3] and for unmasking antigens in serology. [2] It is one of the most commonly used substances for differentiating many blood group antigens: For example, it destroys M, N, S, Duffy a, and Duffy b, and enhances some other antigens including antigens from the Rh, Kidd, Lewis, I, and P1 systems. [5]

It is also used for cleaning the animal intestines used as sausage or cheese-casings. It is used as an additive to make freeze-resistant beer, and has been added to certain formulations of meat tenderizers along with related protease-type enzymes. [3] For example, as a tenderizer it can be added to the meat in the production of bologna sausage, which improves some measurable quality attributes of the final product. [12] It can be used for dissolving the proteins in meat products in order to release potentially present food-borne pathogenic bacteria for safety analysis. Latex from Ficus carica also appears to contain an enzyme which shows marked ability to digest collagen, as opposed to papain. [9] This, however, is not a cysteine protease, but a serine protease. [13]

The crude, unrefined latex of F. insipida is also sold in North and South American as an anthelmintic herbal medicine called 'doctor oje' (ojé in Brazil). [3] [14] The crude latex is toxic, overdoses due to use as a medicine are possible and occur rarely, but it remains a popular drug in certain regions. [14] During the 1940s the substance was known by medical practitioners as leche de higuerón, and it was considered to be the most effective treatment for trichuriasis at the time. [15] Species used in the production of leche de higuerón in the 1920s included F. glaborata and F. laurifolia. [16]

Related Research Articles

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.

<span class="mw-page-title-main">Metalloproteinase</span> Type of enzyme

A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis.

<span class="mw-page-title-main">Papain</span> Widely used enzyme extracted from papayas

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.

<span class="mw-page-title-main">Mountain papaya</span> Species of plant

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).

<span class="mw-page-title-main">Cysteine protease</span> Class of enzymes

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.

<span class="mw-page-title-main">Aspartic protease</span>

Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin.

<span class="mw-page-title-main">Furanocoumarin</span> Class of organic chemical compounds

The furanocoumarins, or furocoumarins, are a class of organic chemical compounds produced by a variety of plants. Most of the plant species found to contain furanocoumarins belong to a handful of plant families. The families Apiaceae and Rutaceae include the largest numbers of plant species that contain furanocoumarins. The families Moraceae and Fabaceae include a few widely distributed plant species that contain furanocoumarins.

<span class="mw-page-title-main">Actinidain</span> Class of enzymes

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.

<i>Ficus insipida</i> Species of fig tree from the Neotropics

Ficus insipida is a common tropical tree in the fig genus of the family Moraceae growing in forest habitats along rivers. It ranges from Mexico to northern South America.

<span class="mw-page-title-main">Chymopapain</span> Enzyme

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.

Cathepsin X is an enzyme. This enzyme catalyses the following chemical reaction

Nepenthesin is an aspartic protease of plant origin that has so far been identified in the pitcher secretions of Nepenthes and in the leaves of Drosera peltata. It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg. While more pH and temperature stable than porcine pepsin A, it is considerably less stable in urea or guanidine hydrochloride. It is the only known protein with such a stability profile.

<span class="mw-page-title-main">Fig</span> Species of flowering plant known as the common fig

The fig is the edible fruit of Ficus carica, a species of small tree in the flowering plant family Moraceae, native to the Mediterranean region, together with western and southern Asia. It has been cultivated since ancient times and is now widely grown throughout the world. Ficus carica is the type species of the genus Ficus, containing over 800 tropical and subtropical plant species.

<span class="mw-page-title-main">Oligopeptidase</span> Enzymes that cleaves peptides but not proteins

An Oligopeptidase is an enzyme that cleaves peptides but not proteins. This property is due to its structure: the active site of this enzyme is located at the end of a narrow cavity which can only be reached by peptides.

Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Glycyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

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

<span class="mw-page-title-main">Peptidase 1 (mite)</span> Class of enzymes found in mites

Peptidase 1 (mite) (EC 3.4.22.65), also known as endopeptidase 1 (mite), is an enzyme found in various species of mites. This enzyme exhibits cysteine protease activity with broad endopeptidase specificity.

<span class="mw-page-title-main">Zingibain</span> Cysteine protease enzyme

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).

<span class="mw-page-title-main">Papain-like protease</span> Protein family of cysteine protease enzymes

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.

References

  1. ↑ "ENZYME 3.4.22.3 ficain". Expasy - Swiss Bioinformatics Resource Portal. Swiss Institute of Bioinformatics. Retrieved 22 May 2021.
  2. 1 2 3 4 5 6 7 Arribére MP, Caffin O, Priolo S (2000). "Proteolytic Enzymes from the Latex of Ficus pumila L. (Moraceae)" (PDF). Acta Farmacéutica Bonaerense. 19 (4): 257–262. Retrieved 22 May 2021.
  3. 1 2 3 4 5 "Ficin". Vitamins & Supplements. WebMD LLC. 2021. Retrieved 22 May 2021.
  4. ↑ Liener IE, Friedenson B (1970). Ficin. Methods Enzymol. Vol. 19. pp. 261–273. doi:10.1016/0076-6879(70)19020-3. ISBN   978-0-12-181881-4.
  5. 1 2 3 4 Brocklehurst K, Willenbrock F, Salih E (1987). "Cysteine proteinases". In Neuberger A, Brocklehurst K (eds.). New Comprehensive Biochemistry: Hydrolytic Enzymes. Amsterdam: Elsevier. pp. 39–158.
  6. ↑ Singleton A, Buttle DJ (January 2013). "Ficain". Handbook of Proteolytic Enzymes. Vol. 2: Metallopeptidases and Cysteine Peptidases. Academic Press. pp. 1877–9. doi:10.1016/B978-0-12-382219-2.00427-0. ISBN   978-0-12-382219-2.
  7. 1 2 "EC 3.4.22.3". IUBMB Enzyme Nomenclature. International Union of Biochemistry and Molecular Biology. Retrieved 22 May 2021.
  8. ↑ "Ficus insipida Willd". Plants of the World Online. Royal Botanic Gardens, Kew. Retrieved 2020-10-09.
  9. 1 2 Vatić S, Mirković N, Milošević JR, Jovčić B, Polović NĐ (December 2020). "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes". International Journal of Food Microbiology. 334 (108851): 108851. doi:10.1016/j.ijfoodmicro.2020.108851. PMID   32911158.
  10. ↑ Zare H, Moosavi-Movahedi AA, Salami M, Mirzaei M, Saboury AA, Sheibani N (March 2013). "Purification and autolysis of the ficin isoforms from fig (Ficus carica cv. Sabz) latex". Phytochemistry. 87: 16–22. Bibcode:2013PChem..87...16Z. doi:10.1016/j.phytochem.2012.12.006. PMC   3755362 . PMID   23312458.
  11. ↑ Zaynoun ST, Aftimos BG, Abi Ali L, Tenekjian KK, Khalidi U, Kurban AK (July 1984). "Ficus carica; isolation and quantification of the photoactive components". Contact Dermatitis. 11 (1): 21–5. doi:10.1111/j.1600-0536.1984.tb00164.x. PMID   6744838. Cited in McGovern and Barkley 2000, section  Phytophotodermatitis.
  12. ↑ Ramezani R, Aminlari M, Fallahi H (July 2006). "Effect of Chemically Modified Soy Proteins and Ficin-tenderized Meat on the Quality Attributes of Sausage". Journal of Food Science. 68 (1): 85–88. doi:10.1111/j.1365-2621.2003.tb14119.x.
  13. ↑ Nishimura K, Higashiya K, Ueshima N, Kojima K, Takita T, Abe T, et al. (April 2021). "Insight into the collagen-degrading activity of a serine protease in the latex of Ficus carica cultivar Masui Dauphine". Bioscience, Biotechnology, and Biochemistry. 85 (5): 1147–1156. doi:10.1093/bbb/zbab025. PMID   33580958.
  14. 1 2 Hansson A, Zelada JC, Noriega HP (April 2005). "Reevaluation of risks with the use of Ficus insipida latex as a traditional anthelmintic remedy in the Amazon". Journal of Ethnopharmacology. 98 (3): 251–7. doi:10.1016/j.jep.2004.12.029. PMID   15814256.
  15. ↑ "Clinical Aspects and Treatment of the More Common Intestinal Parasites of Man (TB-33)". Veterans Administration Technical Bulletin 1946 & 1947. 10: 1–14. 1948.
  16. ↑ The American Journal of Tropical Medicine. Williams and Wilkins. 1921. p. 377.
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