Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix

[Display omitted] •Invertebrates tropomyosin (abalone, oyster, shrimp) revealed pepsin resistance.•Vertebrates tropomyosin (chicken, pork, beef) were less stable to digestion.•Raw shrimp myosin light chain (MLC) showed pepsin resistance among invertebrates.•Vertebrate (chicken) MLC was thermally sta...

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Bibliographic Details
Published in:Food chemistry 2023-03, Vol.405, p.134981-134981, Article 134981
Main Authors: Khulal, Urmila, Stojadinovic, Marija, Prodic, Ivana, Rajkovic, Andreja, Cirkovic Velickovic, Tanja
Format: Article
Language:English
Subjects:
abalone
allergenicity
allergens
antibodies
beef
chicken meat
chickens
cooked foods
digestion
food chemistry
Food matrix
gastrointestinal system
heat treatment
In vitro gastrointestinal digestion
Meat allergen pair
Myosin light chain
myosin light chains
oysters
pepsin
polyacrylamide gel electrophoresis
pork
raw chicken meat
seafoods
shrimp
thermal stability
Thermal treatment
Tropomyosin
tropomyosins
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Summary:[Display omitted] •Invertebrates tropomyosin (abalone, oyster, shrimp) revealed pepsin resistance.•Vertebrates tropomyosin (chicken, pork, beef) were less stable to digestion.•Raw shrimp myosin light chain (MLC) showed pepsin resistance among invertebrates.•Vertebrate (chicken) MLC was thermally stable.•A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork. 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.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2022.134981