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- W3214076565 endingPage "101454" @default.
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- W3214076565 abstract "Peanut allergy is among the most widespread and life-threatening food allergies. Roasting was conducted to improve the sensorial quality of peanut and to change the structure and allergenicity of allergens. The potential allergenicity of digested defatted peanut powder did not significantly differ between raw and roasted peanuts. The raw/roasted peanut proteins were digested by trypsin and then analyzed with isobaric tags for relative and absolute quantitation (iTRAQ) to discover the changes in peptide quantity. Among the 44 detected peptides, the abundance of 29 peptides significantly increased by up to 36.78 times after roasting. Among those 29 peptides, seventeen peptides overlapped with linear IgE-binding epitopes, which were either destroyed or exposed after roasting. Combined with the spatial structure model, the iTRAQ result indicated the breaking of disulfide bonds and depolymerization of proteins during roasting. Roasting changed the conformational structure of protein, which increased allergen digestibility but did not guarantee a decrease in the potential allergenicity of peanut." @default.
- W3214076565 created "2021-11-22" @default.
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- W3214076565 date "2021-12-01" @default.
- W3214076565 modified "2023-10-15" @default.
- W3214076565 title "The effect of roasting on peanut allergens’ digestibility, allergenicity, and structure" @default.
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- W3214076565 doi "https://doi.org/10.1016/j.fbio.2021.101454" @default.
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