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| caption = Biological assembly image of actinidain from ''[[Actinidia chinensis]]''. From {{PDB|1AEC}}.
| caption = Biological assembly image of actinidain from ''[[Actinidia chinensis]]''. From {{PDB|1AEC}}.
}}
}}
'''Actinidain''' ({{EC number|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 protease]]s.<ref>{{cite journal | vauthors = Baker EN, Boland MJ, Calder PC, Hardman MJ | title = The specificity of actinidin and its relationship to the structure of the enzyme | journal = Biochimica et Biophysica Acta (BBA) - Enzymology | volume = 616 | issue = 1 | pages = 30–4 | date = November 1980 | pmid = 7002215 | doi = 10.1016/0005-2744(80)90260-0 }}</ref><ref>{{cite journal | vauthors = Kamphuis IG, Drenth J, Baker EN | title = 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 = Journal of Molecular Biology | volume = 182 | issue = 2 | pages = 317–29 | date = March 1985 | pmid = 3889350 | doi = 10.1016/0022-2836(85)90348-1 }}</ref><ref>{{cite book |chapter = The thiol proteases: structure and mechanism |title = Active Sites of Enzymes |vauthors = Baker EN, Drenth J |year = 1987 |series = Biological Macromolecules and Assemblies |volume = 3 |pages = [https://archive.org/details/biologicalmacrom0000unse/page/314 314–368] |veditors = Jurnak FA, McPherson A |publisher = John Wiley and Sons |location = New York |isbn = 978-0-471-85142-4 |chapter-url = https://archive.org/details/biologicalmacrom0000unse/page/314 }}</ref><ref>{{cite journal | vauthors = Gul S, Mellor GW, Thomas EW, Brocklehurst K | title = Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features | journal = The Biochemical Journal | volume = 396 | issue = 1 | pages = 17–21 | date = May 2006 | pmid = 16445383 | pmc = 1449998 | doi = 10.1042/BJ20051501 }}</ref>
'''Actinidain''' ({{EC number|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 protease]]s.<ref>{{cite journal | vauthors = Baker EN, Boland MJ, Calder PC, Hardman MJ | title = The specificity of actinidin and its relationship to the structure of the enzyme | journal = Biochimica et Biophysica Acta (BBA) - Enzymology | volume = 616 | issue = 1 | pages = 30–4 | date = November 1980 | pmid = 7002215 | doi = 10.1016/0005-2744(80)90260-0 }}</ref><ref name=":1">{{cite journal | vauthors = Kamphuis IG, Drenth J, Baker EN | title = 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 = Journal of Molecular Biology | volume = 182 | issue = 2 | pages = 317–29 | date = March 1985 | pmid = 3889350 | doi = 10.1016/0022-2836(85)90348-1 }}</ref><ref>{{cite book |chapter = The thiol proteases: structure and mechanism |title = Active Sites of Enzymes |vauthors = Baker EN, Drenth J |year = 1987 |series = Biological Macromolecules and Assemblies |volume = 3 |pages = [https://archive.org/details/biologicalmacrom0000unse/page/314 314–368] |veditors = Jurnak FA, McPherson A |publisher = John Wiley and Sons |location = New York |isbn = 978-0-471-85142-4 |chapter-url = https://archive.org/details/biologicalmacrom0000unse/page/314 }}</ref><ref>{{cite journal | vauthors = Gul S, Mellor GW, Thomas EW, Brocklehurst K | title = Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features | journal = The Biochemical Journal | volume = 396 | issue = 1 | pages = 17–21 | date = May 2006 | pmid = 16445383 | pmc = 1449998 | doi = 10.1042/BJ20051501 }}</ref>


As a known [[allergen]] in kiwifruit,<ref>{{cite journal | vauthors = Maddumage R, Nieuwenhuizen NJ, Bulley SM, Cooney JM, Green SA, Atkinson RG | title = Diversity and relative levels of actinidin, kiwellin, and thaumatin-like allergens in 15 varieties of kiwifruit (Actinidia) | journal = Journal of Agricultural and Food Chemistry | volume = 61 | issue = 3 | pages = 728–39 | date = January 2013 | pmid = 23289429 | doi = 10.1021/jf304289f }}</ref> the enzyme is under preliminary research for its effect on [[tight junction]] proteins of intestinal [[epithelial cell]]s.<ref>{{cite journal | vauthors = Grozdanovic MM, Čavić M, Nešić A, Andjelković U, Akbari P, Smit JJ, Gavrović-Jankulović M | title = Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions | journal = Biochimica et Biophysica Acta (BBA) - General Subjects | volume = 1860 | issue = 3 | pages = 516–26 | date = March 2016 | pmid = 26701113 | doi = 10.1016/j.bbagen.2015.12.005 | url = http://cer.ihtm.bg.ac.rs/handle/123456789/3154 }}</ref><ref>{{cite journal | vauthors = Cavic M, Grozdanovic MM, Bajic A, Jankovic R, Andjus PR, Gavrovic-Jankulovic M | title = The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells | journal = Food and Chemical Toxicology | volume = 72 | pages = 61–8 | date = October 2014 | pmid = 25042511 | doi = 10.1016/j.fct.2014.07.012 }}</ref>
As a known [[allergen]] in kiwifruit,<ref>{{cite journal | vauthors = Maddumage R, Nieuwenhuizen NJ, Bulley SM, Cooney JM, Green SA, Atkinson RG | title = Diversity and relative levels of actinidin, kiwellin, and thaumatin-like allergens in 15 varieties of kiwifruit (Actinidia) | journal = Journal of Agricultural and Food Chemistry | volume = 61 | issue = 3 | pages = 728–39 | date = January 2013 | pmid = 23289429 | doi = 10.1021/jf304289f }}</ref> the enzyme is under preliminary research for its effect on [[tight junction]] proteins of intestinal [[epithelial cell]]s.<ref>{{cite journal | vauthors = Grozdanovic MM, Čavić M, Nešić A, Andjelković U, Akbari P, Smit JJ, Gavrović-Jankulović M | title = Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions | journal = Biochimica et Biophysica Acta (BBA) - General Subjects | volume = 1860 | issue = 3 | pages = 516–26 | date = March 2016 | pmid = 26701113 | doi = 10.1016/j.bbagen.2015.12.005 | url = http://cer.ihtm.bg.ac.rs/handle/123456789/3154 }}</ref><ref>{{cite journal | vauthors = Cavic M, Grozdanovic MM, Bajic A, Jankovic R, Andjus PR, Gavrovic-Jankulovic M | title = The effect of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells | journal = Food and Chemical Toxicology | volume = 72 | pages = 61–8 | date = October 2014 | pmid = 25042511 | doi = 10.1016/j.fct.2014.07.012 }}</ref>


Actinidain is commercially useful as a meat tenderiser<ref>{{cite journal | vauthors = Bekhit AA, Hopkins DL, Geesink G, Bekhit AA, Franks P | title = Exogenous proteases for meat tenderization | journal = Critical Reviews in Food Science and Nutrition | volume = 54 | issue = 8 | pages = 1012–31 | year = 2014 | pmid = 24499119 | doi = 10.1080/10408398.2011.623247 | s2cid = 57554 }}</ref><ref name=":0">{{cite journal | vauthors = Eshamah H, Han I, Naas H, Acton J, Dawson P | title = Antibacterial effects of natural tenderizing enzymes on different strains of Escherichia coli O157:H7 and Listeria monocytogenes on beef | journal = Meat Science | volume = 96 | issue = 4 | pages = 1494–500 | date = April 2014 | pmid = 24447905 | doi = 10.1016/j.meatsci.2013.12.010 }}</ref> and in coagulating milk for dairy products.<ref>{{cite journal | last1 = Katsaros | first1 = George I.| last2 = Tavantzis | first2 = George | last3 = Taoukis | first3 = Petros S. | name-list-style = vanc | date = January 2010 | title = Production of novel dairy products using actinidin and high pressure as enzyme activity regulator | journal = Innovative Food Science & Emerging Technologies | volume = 11 | issue = 1 | pages = 47–51 | doi = 10.1016/j.ifset.2009.08.007 }}</ref> The denaturation temperature of actinidain is {{cvt|60|C|F}}, lower than that of similar meat tenderising enzymes [[bromelain]] from [[pineapple]] and [[papain]] from [[papaya]].<ref>{{cite book | first = Rodrigo | last =Tarté | name-list-style = vanc | title = Ingredients in meat products properties, functionality and applications | date = 2008 | publisher = Springer | location = New York | isbn = 978-0-387-71327-4 | url = https://books.google.com/books?id=C-wrQaaXxj0C&q=actinidin+denaturation+temperature&pg=PA179}}</ref>
Actinidain is commercially useful as a meat tenderiser<ref>{{cite journal | vauthors = Bekhit AA, Hopkins DL, Geesink G, Bekhit AA, Franks P | title = Exogenous proteases for meat tenderization | journal = Critical Reviews in Food Science and Nutrition | volume = 54 | issue = 8 | pages = 1012–31 | year = 2014 | pmid = 24499119 | doi = 10.1080/10408398.2011.623247 | s2cid = 57554 }}</ref><ref name=":0">{{cite journal | vauthors = Eshamah H, Han I, Naas H, Acton J, Dawson P | title = Antibacterial effects of natural tenderizing enzymes on different strains of Escherichia coli O157:H7 and Listeria monocytogenes on beef | journal = Meat Science | volume = 96 | issue = 4 | pages = 1494–500 | date = April 2014 | pmid = 24447905 | doi = 10.1016/j.meatsci.2013.12.010 }}</ref> and in coagulating milk for dairy products, like yogurt and cheese.<ref>{{cite journal | last1 = Katsaros | first1 = George I.| last2 = Tavantzis | first2 = George | last3 = Taoukis | first3 = Petros S. | name-list-style = vanc | date = January 2010 | title = Production of novel dairy products using actinidin and high pressure as enzyme activity regulator | journal = Innovative Food Science & Emerging Technologies | volume = 11 | issue = 1 | pages = 47–51 | doi = 10.1016/j.ifset.2009.08.007 }}</ref> The denaturation temperature of actinidain is {{cvt|60|C|F}}, lower than that of similar meat tenderising enzymes [[bromelain]] from [[pineapple]] and [[papain]] from [[papaya]].<ref>{{cite book | first = Rodrigo | last =Tarté | name-list-style = vanc | title = Ingredients in meat products properties, functionality and applications | date = 2008 | publisher = Springer | location = New York | isbn = 978-0-387-71327-4 | url = https://books.google.com/books?id=C-wrQaaXxj0C&q=actinidin+denaturation+temperature&pg=PA179}}</ref>

=== History ===
Actinidain was first identified in 1959 when A.C. Arcus looked into why jellies made with kiwifruit don’t solidify.<ref name=":2">{{Cite journal |last=Arcus |first=A.C. |date=1959-05 |title=Proteolytic enzyme of Actinidia chinensis |url=https://linkinghub.elsevier.com/retrieve/pii/0006300259905220 |journal=Biochimica et Biophysica Acta (BBA) |language=en |volume=33 |issue=1 |pages=242–244 |doi=10.1016/0006-3002(59)90522-0}}</ref> They went on to show that this phenomenon was caused by a proteolytic enzyme attacking gelatin.<ref name=":2" /> This enzyme would go on to be named ''actinidin'' as it was identified in a fruit in the genus ''[[Actinidia]].''<ref name=":2" /> While similar proteins have been found in other fruits, this cysteine protease is unique to the kiwifruit.<ref name=":3">{{Cite journal |last=Malone |first=L. A. |last2=Todd |first2=J. H. |last3=Burgess |first3=E. P. J. |last4=Philip |first4=B. A. |last5=Christeller |first5=J. T. |date=2005-06 |title=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 |url=http://www.tandfonline.com/doi/abs/10.1080/01140671.2005.9514337 |journal=New Zealand Journal of Crop and Horticultural Science |language=en |volume=33 |issue=2 |pages=99–105 |doi=10.1080/01140671.2005.9514337 |issn=0114-0671}}</ref><ref name=":2" /> A [[thiol]] group was identified to be essential for enzyme activity, which is why it was grouped with enzymes like papain and bromelain.<ref name=":4">{{Cite journal |last=Baker |first=E.N. |date=1977-09 |title=Structure of actinidin: Details of the polypeptide chain conformation and active site from an electron density map at 2·8 Å resolution |url=https://linkinghub.elsevier.com/retrieve/pii/0022283677901541 |journal=Journal of Molecular Biology |language=en |volume=115 |issue=3 |pages=263–277 |doi=10.1016/0022-2836(77)90154-1}}</ref><ref name=":5">{{Cite journal |last=Carne |first=A |last2=Moore |first2=CH |date=1978-07-01 |title=The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis |url=https://europepmc.org/article/MED/687380 |journal=The Biochemical Journal |volume=173 |issue=1 |pages=73-83 |doi=10.1042/bj1730073 |via=Europe PMC}}</ref>

=== 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.<ref>{{Cite journal |last=Praekelt |first=Uta M. |last2=McKee |first2=Raymond A. |last3=Smith |first3=Harry |date=1988 |title=Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinensis |url=http://link.springer.com/10.1007/BF00027396 |journal=Plant Molecular Biology |language=en |volume=10 |issue=3 |pages=193–202 |doi=10.1007/BF00027396 |issn=0167-4412}}</ref> 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.<ref name=":3" /> It may also be used as a storage protein.<ref>{{Cite journal |last=Chalabi |first=Maryam |last2=Khademi |first2=Fatemeh |last3=Yarani |first3=Reza |last4=Mostafaie |first4=Ali |date=2014-04 |title=Proteolytic Activities of Kiwifruit Actinidin (Actinidia deliciosa cv. Hayward) on Different Fibrous and Globular Proteins: A Comparative Study of Actinidin with Papain |url=http://link.springer.com/10.1007/s12010-014-0812-7 |journal=Applied Biochemistry and Biotechnology |language=en |volume=172 |issue=8 |pages=4025–4037 |doi=10.1007/s12010-014-0812-7 |issn=0273-2289}}</ref>

=== Sequence and Structure ===
Actinidain has an enzyme classification number (EC) of 3.4.22.14. The 3 classifies it as a hydrolase.<ref name=":6">{{Cite web |title=Information on EC 3.4.22.14 - actinidain - BRENDA Enzyme Database |url=https://www.brenda-enzymes.org/enzyme.php?ecno=3.4.22.14 |url-status=live |access-date=10/03/2023 |website=BRENDA enzymes}}</ref> 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.<ref name=":6" /> 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.<ref name=":3" /> The enzyme is encoded by a large gene family and is expressed in most tissues of the kiwifruit plant, not just the fruit itself.<ref name=":3" />

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.<ref name=":1" /><ref name=":4" /> Electron density mapping shows similar α-helices and overall polypeptide folding.<ref name=":1" /><ref name=":4" /> 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.<ref name=":4" /><ref name=":5" /> The active site includes cysteine and histidine residues that are conserved across several other proteins in the fruit peptidase family.<ref name=":5" /> 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,<ref name=":4" /> 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.<ref name=":4" /> Actinidain comprises up to 50% of the kiwifruit’s soluble protein content at harvest.<ref name=":7">{{Cite journal |last=Dearman |first=Rebecca J. |last2=Beresford |first2=Lorna |last3=Foster |first3=Emily S. |last4=McClain |first4=Scott |last5=Kimber |first5=Ian |date=2014-05 |title=Characterization of the allergenic potential of proteins: an assessment of the kiwifruit allergen actinidin |url=https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/jat.2897 |journal=Journal of Applied Toxicology |language=en |volume=34 |issue=5 |pages=489–497 |doi=10.1002/jat.2897 |issn=0260-437X}}</ref> Actinidain is active over a wide range of pH, including very acidic conditions,<ref name=":8">{{Cite journal |last=Richardson |first=David P. |last2=Ansell |first2=Juliet |last3=Drummond |first3=Lynley N. |date=2018-12 |title=The nutritional and health attributes of kiwifruit: a review |url=http://link.springer.com/10.1007/s00394-018-1627-z |journal=European Journal of Nutrition |language=en |volume=57 |issue=8 |pages=2659–2676 |doi=10.1007/s00394-018-1627-z |issn=1436-6207 |pmc=PMC6267416 |pmid=29470689}}</ref> with a pH optimum from 5-7.<ref>{{Cite journal |last=McDowall |first=Max A. |date=1970-06 |title=Anionic Proteinase from Actinidia chinensis. Preparation and Properties of the Crystalline Enzyme |url=https://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1970.tb00280.x |journal=European Journal of Biochemistry |language=en |volume=14 |issue=2 |pages=214–221 |doi=10.1111/j.1432-1033.1970.tb00280.x |issn=0014-2956}}</ref> 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).<ref name=":7" />

=== 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.<ref name=":8" /><ref>{{Cite journal |last=Kaur |first=Lovedeep |last2=Rutherfurd |first2=Shane M. |last3=Moughan |first3=Paul J. |last4=Drummond |first4=Lynley |last5=Boland |first5=Mike J. |date=2010-04-28 |title=Actinidin Enhances Gastric Protein Digestion As Assessed Using an in Vitro Gastric Digestion Model |url=https://pubs.acs.org/doi/10.1021/jf903332a |journal=Journal of Agricultural and Food Chemistry |language=en |volume=58 |issue=8 |pages=5068–5073 |doi=10.1021/jf903332a |issn=0021-8561}}</ref> 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.<ref>{{Cite journal |last=Kaur |first=Lovedeep |last2=Rutherfurd |first2=Shane M. |last3=Moughan |first3=Paul J. |last4=Drummond |first4=Lynley |last5=Boland |first5=Mike J. |date=2010-04-28 |title=Actinidin Enhances Protein Digestion in the Small Intestine As Assessed Using an in Vitro Digestion Model |url=https://pubs.acs.org/doi/10.1021/jf903835g |journal=Journal of Agricultural and Food Chemistry |language=en |volume=58 |issue=8 |pages=5074–5080 |doi=10.1021/jf903835g |issn=0021-8561}}</ref> Further work is being done into the usefulness of kiwifruit as a digestive aid.

Actinidain is the major allergen in kiwifruit.<ref name=":7" /><ref name=":8" /> 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.<ref name=":8" /> Actinidain provokes both IgG and IgE responses antibody responses, with the IgE binding activity being associated with the severe (anaphylaxis) responses.<ref name=":7" />

=== Potential Applications ===
Actinidain is used as a high-quality meat tenderizer.<ref name=":7" /> 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.<ref>{{Cite journal |last=Christensen |first=Mette |last2=Tørngren |first2=Mari Ann |last3=Gunvig |first3=Annemarie |last4=Rozlosnik |first4=Noemi |last5=Lametsch |first5=René |last6=Karlsson |first6=Anders H |last7=Ertbjerg |first7=Per |date=2009-07 |title=Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue |url=https://onlinelibrary.wiley.com/doi/10.1002/jsfa.3633 |journal=Journal of the Science of Food and Agriculture |language=en |volume=89 |issue=9 |pages=1607–1614 |doi=10.1002/jsfa.3633 |issn=0022-5142}}</ref><ref>{{Cite journal |last=Anaduaka |first=Emeka Godwin |last2=Chibuogwu |first2=Christian Chiazor |last3=Ezugwu |first3=Arinze Linus |last4=Ezeorba |first4=Timothy Prince Chidike |date=2023-04-03 |title=Nature-derived ingredients as sustainable alternatives for tenderizing meat and meat products: an updated review |url=https://www.tandfonline.com/doi/full/10.1080/08905436.2023.2201354 |journal=Food Biotechnology |language=en |volume=37 |issue=2 |pages=136–165 |doi=10.1080/08905436.2023.2201354 |issn=0890-5436}}</ref>

Studies have shown that actinidain might be a good alternative milk coagulant, replacing chymosin, a common coagulant used in cheese making.<ref>{{Cite journal |last=Alirezaei |first=Masoud |last2=Aminlari |first2=Mahmood |last3=Gheisari |first3=Hamid Reza |last4=Tavana |first4=Maryam |date=2011-03-22 |title=Actinidin: A Promising Milk Coagulating Enzyme |url=https://journalejnfs.com/index.php/EJNFS/article/view/245 |journal=European Journal of Nutrition & Food Safety |language=en |pages=43–51 |issn=2347-5641}}</ref>


== References ==
== References ==

Revision as of 00:51, 24 October 2023

Not to be confused with actinidine or actinide.
actinidain
Biological assembly image of actinidain from Actinidia chinensis. From PDB: 1AEC​.
Identifiers
EC no.3.4.22.14
CAS no.39279-27-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
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NCBIproteins

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]

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]

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): 30–4. doi:10.1016/0005-2744(80)90260-0. PMID 7002215.
  2. ^ a b c 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): 317–29. 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): 728–39. 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): 516–26. 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: 61–8. 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): 1012–31. 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): 1494–500. 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. ^ a b c d Arcus, A.C. (1959-05). "Proteolytic enzyme of Actinidia chinensis". Biochimica et Biophysica Acta (BBA). 33 (1): 242–244. doi:10.1016/0006-3002(59)90522-0. {{cite journal}}: Check date values in: |date= (help)
  13. ^ a b c d Malone, L. A.; Todd, J. H.; Burgess, E. P. J.; Philip, B. A.; Christeller, J. T. (2005-06). "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. {{cite journal}}: Check date values in: |date= (help)
  14. ^ a b c d e f Baker, E.N. (1977-09). "Structure of actinidin: Details of the polypeptide chain conformation and active site from an electron density map at 2·8 Å resolution". Journal of Molecular Biology. 115 (3): 263–277. doi:10.1016/0022-2836(77)90154-1. {{cite journal}}: Check date values in: |date= (help)
  15. ^ a b c Carne, A; Moore, CH (1978-07-01). "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 – via Europe PMC.
  16. ^ Praekelt, Uta M.; McKee, Raymond A.; Smith, Harry (1988). "Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinensis". Plant Molecular Biology. 10 (3): 193–202. doi:10.1007/BF00027396. ISSN 0167-4412.
  17. ^ Chalabi, Maryam; Khademi, Fatemeh; Yarani, Reza; Mostafaie, Ali (2014-04). "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. ISSN 0273-2289. {{cite journal}}: Check date values in: |date= (help)
  18. ^ a b "Information on EC 3.4.22.14 - actinidain - BRENDA Enzyme Database". BRENDA enzymes. Retrieved 10/03/2023. {{cite web}}: Check date values in: |access-date= (help)CS1 maint: url-status (link)
  19. ^ a b c d e Dearman, Rebecca J.; Beresford, Lorna; Foster, Emily S.; McClain, Scott; Kimber, Ian (2014-05). "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. ISSN 0260-437X. {{cite journal}}: Check date values in: |date= (help)
  20. ^ a b c d Richardson, David P.; Ansell, Juliet; Drummond, Lynley N. (2018-12). "The nutritional and health attributes of kiwifruit: a review". European Journal of Nutrition. 57 (8): 2659–2676. doi:10.1007/s00394-018-1627-z. ISSN 1436-6207. PMC 6267416. PMID 29470689. {{cite journal}}: Check date values in: |date= (help)CS1 maint: PMC format (link)
  21. ^ McDowall, Max A. (1970-06). "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. ISSN 0014-2956. {{cite journal}}: Check date values in: |date= (help)
  22. ^ Kaur, Lovedeep; Rutherfurd, Shane M.; Moughan, Paul J.; Drummond, Lynley; Boland, Mike J. (2010-04-28). "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. ISSN 0021-8561.
  23. ^ Kaur, Lovedeep; Rutherfurd, Shane M.; Moughan, Paul J.; Drummond, Lynley; Boland, Mike J. (2010-04-28). "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. ISSN 0021-8561.
  24. ^ Christensen, Mette; Tørngren, Mari Ann; Gunvig, Annemarie; Rozlosnik, Noemi; Lametsch, René; Karlsson, Anders H; Ertbjerg, Per (2009-07). "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. doi:10.1002/jsfa.3633. ISSN 0022-5142. {{cite journal}}: Check date values in: |date= (help)
  25. ^ Anaduaka, Emeka Godwin; Chibuogwu, Christian Chiazor; Ezugwu, Arinze Linus; Ezeorba, Timothy Prince Chidike (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.
  26. ^ Alirezaei, Masoud; Aminlari, Mahmood; Gheisari, Hamid Reza; Tavana, Maryam (2011-03-22). "Actinidin: A Promising Milk Coagulating Enzyme". European Journal of Nutrition & Food Safety: 43–51. ISSN 2347-5641.

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