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dc.creatorGrozdanović, Milica M.
dc.creatorOstojić, Sanja B.
dc.creatorAleksić, Ivana
dc.creatorAnđelković, Uroš
dc.creatorPetersen, Arnd
dc.creatorGavrović-Jankulović, Marija
dc.date.accessioned2018-11-22T00:29:18Z
dc.date.available2018-11-22T00:29:18Z
dc.date.issued2014
dc.identifier.issn0022-5142
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/1859
dc.description.abstractBACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industryen
dc.publisherWiley-Blackwell, Hoboken
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.rightsrestrictedAccess
dc.sourceJournal of the Science of Food and Agriculture
dc.subjectactinidinen
dc.subjectkiwi fruiten
dc.subjectdigestionen
dc.subjectstabilityen
dc.subjectE-64en
dc.titleActive actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterparten
dc.typearticle
dc.rights.licenseARR
dcterms.abstractГроздановиц, Милица М.; Aлексиц, Ивана; Гавровић-Јанкуловић, Марија; Aндјелковиц, Урос; Петерсен, Aрнд; Остојиц, Сања;
dc.citation.volume94
dc.citation.issue14
dc.citation.spage3046
dc.citation.epage3052
dc.identifier.wos000342829800029
dc.identifier.doi10.1002/jsfa.6656
dc.citation.other94(14): 3046-3052
dc.citation.rankM21
dc.identifier.pmid24633720
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-84917691939
dc.identifier.rcubKon_2742


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