Actinidain

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actinidain
1aeca.jpg
Biological assembly image of actinidain from Actinidia chinensis . From PDB: 1AEC ​.
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EC no. 3.4.22.14
CAS no. 39279-27-1
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Actinidain (EC 3.4.22.14, actinidin, Actinidia anionic protease, proteinase A2 of Actinidia chinensis) is a type of cysteine protease enzyme found in fruits including kiwifruit (genus Actinidia ), pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases. [1] [2] [3] [4]

Contents

As a known allergen in kiwifruit, [5] the enzyme is under preliminary research for its effect on tight junction proteins of intestinal epithelial cells. [6] [7]

Actinidain is commercially useful as a meat tenderiser [8] [9] and in coagulating milk for dairy products, like yogurt and cheese. [10] The denaturation temperature of actinidain is 60 °C (140 °F), lower than that of similar meat tenderising enzymes bromelain from pineapple and papain from papaya. [11]

History

Actinidain was first identified in 1959 when A.C. Arcus looked into why jellies made with kiwifruit don’t solidify. [12] They went on to show that this phenomenon was caused by a proteolytic enzyme attacking gelatin. [12] This enzyme would go on to be named actinidin as it was identified in a fruit in the genus Actinidia. [12] While similar proteins have been found in other fruits, this cysteine protease is unique to the kiwifruit. [13] [12] A thiol group was identified to be essential for enzyme activity, which is why it was grouped with enzymes like papain and bromelain. [14] [15]

Function

While no clear function has been identified, the enzyme begins to accumulate in the fruit early on and is suspected to be important for fruit development. [16] Actinidain has been found to have a detrimental effect on the larvae of Spodoptera litura , however not enough research has been done into whether the enzyme can be used as a pesticide. [13] It may also be used as a storage protein. [17]

Sequence and structure

Actinidain has an enzyme classification number (EC) of 3.4.22.14. The 3 classifies it as a hydrolase. [18] It is further classified as acting on peptide bonds, also known as a peptidase (3.4). The .22 represents the cysteine endopeptidases and then the .14 is actinidain’s unique identifier within that group. [18] Actinidain is first produced in the kiwi when it is about half its size and then increases in both protease activity and enzyme production until the fruit is fully matured. [13] The enzyme is encoded by a large gene family and is expressed in most tissues of the kiwifruit plant, not just the fruit itself. [13]

Actinidain is similar to papain in size, shape, active site location and conformation, as well as in kinetic studies, which is especially interesting as they only share 48% amino acid similarity. [2] [14] Electron density mapping shows similar α-helices and overall polypeptide folding. [2] [14] While the electron density map indicates 218 amino acids, further sequencing work suggests 220 amino acids with the extra two being found at the C-terminus. [14] [15] The active site includes cysteine and histidine residues that are conserved across several other proteins in the fruit peptidase family. [15] Electron density mapping indicates a double crossover with domain 1 being made up of AA 19-115 and 214-218 and domain II composing of AA 1-18 and 116-213, [14] with both the N-terminal and the C-terminal ends crossing over into both domains. Domain 1 has several α-helices whereas domain 2 is primarily made up of one anti-parallel β-sheet. [14] Actinidain comprises up to 50% of the kiwifruit’s soluble protein content at harvest. [19] Actinidain is active over a wide range of pH, including very acidic conditions, [20] with a pH optimum from 5-7. [21] At least ten different isoforms that all have the same molecular weight and cysteine protease activity as actinidain have been identified but they vary in isoelectric point from acidic (pI 3.9) to basic (pI 9.3). [19]

Human health impacts

Actinidain is able to function at low acidities (pH 1-2) that are found in the human GI tract and therefore is found to assist with protein digestion in the stomach and small intestine. [20] [22] Actinidain enhances the human body’s ability to digest food, particularly when working together with pepsin and pancreatin, by hydrolyzing food proteins more efficiently than human digestive enzymes. [23] Further work is being done into the usefulness of kiwifruit as a digestive aid.

Actinidain is the major allergen in kiwifruit. [19] [20] There does not appear to be any trend when looking at who is allergic to kiwi as it varies within age, geographical differences, and other characteristics clinicians use to track allergens, although the allergy often presents itself as mild symptoms in the mouth. [20] Actinidain provokes both IgG and IgE responses antibody responses, with the IgE binding activity being associated with the severe (anaphylaxis) responses. [19]

Potential applications

Actinidain is used as a high-quality meat tenderizer. [19] When marinating with pork, actinidain was found to tenderize it by affecting the myofibrils and the connective tissue, which are similar to the tissues that are broken down through mechanical tenderization. [24] [25]

Studies have shown that actinidain might be a good alternative milk coagulant, replacing chymosin, a common coagulant used in cheese making. [26]

Related Research Articles

<span class="mw-page-title-main">Kiwifruit</span> Edible berries native to northeast Asia

Kiwifruit or Chinese gooseberry is the edible berry of several species of woody vines in the genus Actinidia. The most common cultivar group of kiwifruit is oval, about the size of a large hen's egg: 5–8 centimetres in length and 4.5–5.5 cm in diameter. It has a thin, fuzzy, fibrous, tart but edible light brown skin and light green or golden flesh with rows of tiny, black, edible seeds. The fruit has a soft texture with a sweet and unique flavour.

<span class="mw-page-title-main">Trypsin</span> Family of digestive enzymes

Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne and was named from the Ancient Greek word for rubbing since it was first isolated by rubbing the pancreas with glycerin.

<span class="mw-page-title-main">Protease</span> Enzyme that cleaves other proteins into smaller peptides

A protease is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in numerous biological pathways, including digestion of ingested proteins, protein catabolism, and cell signaling.

In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.

Bromelain is an enzyme extract derived from the stems of pineapples, although it exists in all parts of the fresh pineapple. 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.

<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">Catalytic triad</span> Set of three coordinated amino acids

A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes. An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence.

<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.

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.

<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">Ficain</span>

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.

<span class="mw-page-title-main">Cathepsin L1</span> Protein-coding gene in the species Homo sapiens

Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism.

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.

<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.

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

<span class="mw-page-title-main">Peptidase 1 (mite)</span>

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>

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).

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.

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

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. ↑ Baker EN, Boland MJ, Calder PC, Hardman MJ (November 1980). "The specificity of actinidin and its relationship to the structure of the enzyme". Biochimica et Biophysica Acta (BBA) - Enzymology. 616 (1): 30–34. doi:10.1016/0005-2744(80)90260-0. PMID   7002215.
  2. 1 2 3 Kamphuis IG, Drenth J, Baker EN (March 1985). "Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain". Journal of Molecular Biology. 182 (2): 317–329. doi:10.1016/0022-2836(85)90348-1. PMID   3889350.
  3. ↑ Baker EN, Drenth J (1987). "The thiol proteases: structure and mechanism". In Jurnak FA, McPherson A (eds.). Active Sites of Enzymes. Biological Macromolecules and Assemblies. Vol. 3. New York: John Wiley and Sons. pp.  314–368. ISBN   978-0-471-85142-4.
  4. ↑ Gul S, Mellor GW, Thomas EW, Brocklehurst K (May 2006). "Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features". The Biochemical Journal. 396 (1): 17–21. doi:10.1042/BJ20051501. PMC   1449998 . PMID   16445383.
  5. ↑ Maddumage R, Nieuwenhuizen NJ, Bulley SM, Cooney JM, Green SA, Atkinson RG (January 2013). "Diversity and relative levels of actinidin, kiwellin, and thaumatin-like allergens in 15 varieties of kiwifruit (Actinidia)". Journal of Agricultural and Food Chemistry. 61 (3): 728–739. doi:10.1021/jf304289f. PMID   23289429.
  6. ↑ Grozdanovic MM, Čavić M, Nešić A, Andjelković U, Akbari P, Smit JJ, Gavrović-Jankulović M (March 2016). "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions". Biochimica et Biophysica Acta (BBA) - General Subjects. 1860 (3): 516–526. doi:10.1016/j.bbagen.2015.12.005. PMID   26701113.
  7. ↑ Cavic M, Grozdanovic MM, Bajic A, Jankovic R, Andjus PR, Gavrovic-Jankulovic M (October 2014). "The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells". Food and Chemical Toxicology. 72: 61–68. doi:10.1016/j.fct.2014.07.012. PMID   25042511.
  8. ↑ Bekhit AA, Hopkins DL, Geesink G, Bekhit AA, Franks P (2014). "Exogenous proteases for meat tenderization". Critical Reviews in Food Science and Nutrition. 54 (8): 1012–1031. doi:10.1080/10408398.2011.623247. PMID   24499119. S2CID   57554.
  9. ↑ Eshamah H, Han I, Naas H, Acton J, Dawson P (April 2014). "Antibacterial effects of natural tenderizing enzymes on different strains of Escherichia coli O157:H7 and Listeria monocytogenes on beef". Meat Science. 96 (4): 1494–1500. doi:10.1016/j.meatsci.2013.12.010. PMID   24447905.
  10. ↑ Katsaros GI, Tavantzis G, Taoukis PS (January 2010). "Production of novel dairy products using actinidin and high pressure as enzyme activity regulator". Innovative Food Science & Emerging Technologies. 11 (1): 47–51. doi:10.1016/j.ifset.2009.08.007.
  11. ↑ Tarté R (2008). Ingredients in meat products properties, functionality and applications. New York: Springer. ISBN   978-0-387-71327-4.
  12. 1 2 3 4 Arcus AC (May 1959). "Proteolytic enzyme of Actinidia chinensis". Biochimica et Biophysica Acta. 33 (1): 242–244. doi:10.1016/0006-3002(59)90522-0. PMID   13651208.
  13. 1 2 3 4 Malone LA, Todd JH, Burgess EP, Philip BA, Christeller JT (June 2005). "Effects of kiwifruit ( Actinidia deliciosa ) cysteine protease on growth and survival of Spodoptera litura larvae (Lepidoptera: Noctuidae) fed with control or transgenic avidin‐expressing tobacco". New Zealand Journal of Crop and Horticultural Science. 33 (2): 99–105. doi: 10.1080/01140671.2005.9514337 . ISSN   0114-0671. S2CID   86179155.
  14. 1 2 3 4 5 6 Baker EN (September 1977). "Structure of actinidin: details of the polypeptide chain conformation and active site from an electron density map at 2-8 A resolution". Journal of Molecular Biology. 115 (3): 263–277. doi:10.1016/0022-2836(77)90154-1. PMID   592367.
  15. 1 2 3 Carne A, Moore CH (July 1978). "The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis". The Biochemical Journal. 173 (1): 73–83. doi:10.1042/bj1730073. PMC   1185751 . PMID   687380.
  16. ↑ Praekelt UM, McKee RA, Smith H (May 1988). "Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinensis". Plant Molecular Biology. 10 (3): 193–202. doi:10.1007/BF00027396. PMID   24277513. S2CID   21213015.
  17. ↑ Chalabi M, Khademi F, Yarani R, Mostafaie A (April 2014). "Proteolytic activities of kiwifruit actinidin (Actinidia deliciosa cv. Hayward) on different fibrous and globular proteins: a comparative study of actinidin with papain". Applied Biochemistry and Biotechnology. 172 (8): 4025–4037. doi:10.1007/s12010-014-0812-7. PMID   24604128. S2CID   44438930.
  18. 1 2 "Information on EC 3.4.22.14 - actinidain". BRENDA Enzyme Database. Retrieved October 3, 2023.
  19. 1 2 3 4 5 Dearman RJ, Beresford L, Foster ES, McClain S, Kimber I (May 2014). "Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin". Journal of Applied Toxicology. 34 (5): 489–497. doi:10.1002/jat.2897. PMID   23754484. S2CID   12609478.
  20. 1 2 3 4 Richardson DP, Ansell J, Drummond LN (December 2018). "The nutritional and health attributes of kiwifruit: a review". European Journal of Nutrition. 57 (8): 2659–2676. doi:10.1007/s00394-018-1627-z. PMC   6267416 . PMID   29470689.
  21. ↑ McDowall MA (June 1970). "Anionic proteinase from Actinidia chinensis. Preparation and properties of the crystalline enzyme". European Journal of Biochemistry. 14 (2): 214–221. doi: 10.1111/j.1432-1033.1970.tb00280.x . PMID   5506167.
  22. ↑ Kaur L, Rutherfurd SM, Moughan PJ, Drummond L, Boland MJ (April 2010). "Actinidin enhances gastric protein digestion as assessed using an in vitro gastric digestion model". Journal of Agricultural and Food Chemistry. 58 (8): 5068–5073. doi:10.1021/jf903332a. PMID   20232890.
  23. ↑ Kaur L, Rutherfurd SM, Moughan PJ, Drummond L, Boland MJ (April 2010). "Actinidin enhances protein digestion in the small intestine as assessed using an in vitro digestion model". Journal of Agricultural and Food Chemistry. 58 (8): 5074–5080. doi:10.1021/jf903835g. PMID   20232891.
  24. ↑ Christensen M, Tørngren MA, Gunvig A, Rozlosnik N, Lametsch R, Karlsson AH, Ertbjerg P (July 2009). "Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue". Journal of the Science of Food and Agriculture. 89 (9): 1607–1614. Bibcode:2009JSFA...89.1607C. doi:10.1002/jsfa.3633. ISSN   0022-5142.
  25. ↑ Anaduaka EG, Chibuogwu CC, Ezugwu AL, Ezeorba TP (2023-04-03). "Nature-derived ingredients as sustainable alternatives for tenderizing meat and meat products: an updated review". Food Biotechnology. 37 (2): 136–165. doi:10.1080/08905436.2023.2201354. ISSN   0890-5436. S2CID   258559035.
  26. ↑ Alirezaei M, Aminlari M, Gheisari HR, Tavana M (2011-03-22). "Actinidin: A Promising Milk Coagulating Enzyme". European Journal of Nutrition & Food Safety: 43–51. ISSN   2347-5641.
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