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Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
Khulal, U.; Stojadinovic, M.; Prodic, I.; Rajkovic, A.; Cirkovic Velickovic, T. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. Food Chemistry 405: 134981. https://dx.doi.org/10.1016/j.foodchem.2022.134981
In: Food Chemistry. Elsevier: London. ISSN 0308-8146; e-ISSN 1873-7072, meer
Peer reviewed article  

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  • Khulal, U., meer
  • Stojadinovic, M.
  • Prodic, I.
  • Rajkovic, A., meer
  • Cirkovic Velickovic, T., meer

Abstract
    The 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.

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