Aktinidain
| Aktinidain | |
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Aktinidain (EC 3.4.22.14, aktinidin, anionska proteaza roda Actinidia, proteinaza A2 Actinidia chinensis) je tip enzima cisteinskih proteaza koji se nalazi u voću, uključujući kivi (rod Actinidia), ananas, mango, banana, smokve i papaju. Ovaj enzim je dio porodice C1 peptidaza proteaza sličnih papainu.[1][2][3][4]
Kao poznati alergen u plodovima kivija,[5] enzim je pod preliminarnim istraživanjem zbog njegovog uticaja na čvrste veza proteina crijevnih epitelnih ćelija.[6][7]
Aktinidain je komercijalno koristan kao sredstvo za omekšavanje mesa [8][9] i u zgrušavanju mlijeka za mliječne proizvode.[10] Temperatura denaturacije aktinidaina je {60oC, niža od one kod sličnih enzima za omekšavanje mesa, bromelaina iz ananasa i papaina iz papaja.[11]
Reference[uredi | uredi izvor]
- ^ Baker EN, Boland MJ, Calder PC, Hardman MJ (novembar 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.
- ^ Kamphuis IG, Drenth J, Baker EN (mart 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.
- ^ Baker EN, Drenth J (1987). "The thiol proteases: structure and mechanism". u Jurnak FA, McPherson A (ured.). Active Sites of Enzymes. Biological Macromolecules and Assemblies. 3. New York: John Wiley and Sons. str. 314–368. ISBN 978-0-471-85142-4.
- ^ Gul S, Mellor GW, Thomas EW, Brocklehurst K (maj 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.
- ^ Maddumage R, Nieuwenhuizen NJ, Bulley SM, Cooney JM, Green SA, Atkinson RG (januar 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.
- ^ Grozdanovic MM, Čavić M, Nešić A, Andjelković U, Akbari P, Smit JJ, Gavrović-Jankulović M (mart 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.
- ^ Cavic M, Grozdanovic MM, Bajic A, Jankovic R, Andjus PR, Gavrovic-Jankulovic M (oktobar 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.
- ^ 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.
- ^ 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.
- ^ Katsaros GI, Tavantzis G, Taoukis PS (januar 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.
- ^ Tarté R (2008). Ingredients in meat products properties, functionality and applications. New York: Springer. ISBN 978-0-387-71327-4.
Vanjski linkovi[uredi | uredi izvor]
- The MEROPS online database for peptidases and their inhibitors: C01.007[mrtav link]
- EC 3.4.22.14
- actinidain na US National Library of Medicine Medical Subject Headings (MeSH)
