ArticleFood chemistry: X2021
The conformational structural change of β-lactoglobulin via acrolein treatment reduced the allergenicity.
Article in Food chemistry: X, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Influence of phloretin on acrolein-induced protein modification and physicochemical changes in a dairy protein model.Food chemistry: X · 2024Article
- Novel Approaches for Inhibiting the Indoor Allergen Der f 2 Excreted from House Dust Mites by Todomatsu Oil Produced from Woodland Residues.International journal of environmental research and public health · 2022Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-lactoglobulin (BLG) is a major allergen of milk. Since lipid peroxidation such as acrolein commonly exists during milk processing, it is necessary to evaluate its influence on BLG structure and potential allergenicity. The structure of acrolein-treated BLG was detected using SDS-PAGE, fluorescence, ultraviolet spectrum (UV), circular dichroism (CD) and LC-MS-MS, and the potential allergenicity was assessed by
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Registered trials
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