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dc.creatorKhulal, Urmila
dc.creatorStojadinović, Marija M.
dc.creatorProdić, Ivana
dc.creatorRajković, Andrea
dc.creatorĆirković-Veličković, Tanja
dc.date.accessioned2023-10-09T12:40:48Z
dc.date.available2023-11-21
dc.date.issued2023
dc.identifier.issn0308-8146
dc.identifier.urihttp://intor.torlakinstitut.com/handle/123456789/767
dc.description.abstractThe digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.sr
dc.language.isoensr
dc.publisherElseviersr
dc.relationGhent University Global Campus (GUGC), Incheon, Republic of Koreasr
dc.relationBelgian Special Research Fund BOF StG No. 01 N01718sr
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/810752/EU//sr
dc.relationSerbian Academy of Sciences and Arts (grant number F-26)sr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200168/RS//sr
dc.relation.isreferencedbyhttps://doi.org/10.1016/j.foodchem.2022.134981
dc.relation.isreferencedbyhttps://intor.torlakinstitut.com/handle/123456789/766
dc.rightsembargoedAccesssr
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceFood Chemistrysr
dc.subjectfood matrixsr
dc.subjectin vitro gastrointestinal digestionsr
dc.subjectmeat allergen pairsr
dc.subjectmyosin light chainsr
dc.subjectthermal treatmentsr
dc.subjecttropomyosinsr
dc.titleComparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrixsr
dc.typearticlesr
dc.rights.licenseBY-NC-NDsr
dc.citation.rankaM21~
dc.citation.spage134981
dc.citation.volume405
dc.description.otherThis is the peer-reviewed version of the article: [(1) Khulal, U.; Stojadinović, M. M.; Prodić, I.; Rajković, A.; Ćirković-Veličković, T. Comparative Digestion of Thermally Treated Vertebrates and Invertebrates Allergen Pairs in Real Food Matrix. Food Chemistry 2023, 405, 134981. https://doi.org/10.1016/j.foodchem.2022.134981].
dc.description.otherPublished version: [https://intor.torlakinstitut.com/handle/123456789/766]
dc.identifier.fulltexthttp://intor.torlakinstitut.com/bitstream/id/1727/Comparative_digestion_of_acc_2023.pdf
dc.identifier.rcubhttps://hdl.handle.net/21.15107/rcub_intor_767
dc.type.versionacceptedVersionsr


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