Actinidain

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Not to be confused with actinidine or actinide.
actinidain
Actinidain 1AEC.png
Biological assembly image of actinidain from Actinidia chinensis. From PDB: 1AEC​.
Identifiers
EC number 3.4.22.14
CAS number 39279-27-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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 and papaya. This enzyme is part of the papain-like peptidase C1 family.[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 tenderizer[8][9] and in coagulating milk for dairy products.[10]

References[edit]

  1. ^ Baker, E.N.; Boland, M.J.; Calder, P.C.; Hardman, M.J. (1980). "The specificity of actinidin and its relationship to the structure of the enzyme". Biochim. Biophys. Acta. 616 (1): 30–34. doi:10.1016/0005-2744(80)90260-0. PMID 7002215. 
  2. ^ Kamphuis, I.G.; Drenth, J.; Baker, E.N. (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". J. Mol. Biol. 182 (2): 317–329. doi:10.1016/0022-2836(85)90348-1. PMID 3889350. 
  3. ^ Baker, E.N.; Drenth, J. (1987). "The thiol proteases: structure and mechanism". In Jurnak, F.A.; McPherson, A. Active Sites of Enzymes. Biological Macromolecules and Assemblies. 3. New York: John Wiley and Sons. pp. 314–368. ISBN 0-471-85142-6. 
  4. ^ Gul, S; Mellor, G. W.; Thomas, E. W.; Brocklehurst, K (2006). "Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features". Biochemical Journal. 396 (1): 17–21. doi:10.1042/BJ20051501. PMC 1449998Freely accessible. PMID 16445383. 
  5. ^ Maddumage, R; Nieuwenhuizen, N. J.; Bulley, S. M.; Cooney, J. M.; Green, S. A.; Atkinson, R. G. (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, Milica M.; Čavić, Milena; Nešić, Andrijana; Andjelković, Uroš; Akbari, Peyman; Smit, Joost J.; Gavrović-Jankulović, Marija (2016-03-01). "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. 
  7. ^ Cavic, Milena; Grozdanovic, Milica M.; Bajic, Aleksandar; Jankovic, Radmila; Andjus, Pavle R.; Gavrovic-Jankulovic, Marija (2014-10-01). "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. 
  8. ^ Bekhit, A. A.; Hopkins, D. L.; Geesink, G; Bekhit, A. A.; 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. 
  9. ^ Eshamah, Hanan; Han, Inyee; Naas, Hesham; Acton, James; Dawson, Paul (2014-04-01). "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. 
  10. ^ Katsaros, George I.; Tavantzis, George; Taoukis, Petros S. (2010-01-01). "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. 

External links[edit]