<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang T</submitter><funding>National Natural Science Foundation of China</funding><pagination>988</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8997858</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(7)</volume><pubmed_abstract>The present study aims to investigate the effects of ultrasound on the non-covalent interaction of β-lactoglobulin (β-LG) and luteolin (LUT) and to investigate the relationship between allergenicity and human intestinal microbiota. After treatment, the conformational structures of β-LG were changed, which reflected by the decrease in α-helix content, intrinsic fluorescence intensity and surface hydrophobicity, whereas the β-sheet content increased. Molecular docking studies revealed the non-covalent interaction of β-LG and LUT by hydrogen bond, van der Walls bond and hydrophobic bond. β-LG-LUT complex treated by ultrasound has a lower IgG/IgE binding ability and inhibits the allergic reaction of KU812 cells, depending on the changes in the conformational epitopes of β-LG. Meanwhile, the β-</pubmed_abstract><journal>Foods (Basel, Switzerland)</journal><pubmed_title>Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks.</pubmed_title><pmcid>PMC8997858</pmcid><funding_grant_id>31960457</funding_grant_id><pubmed_authors>Liu J</pubmed_authors><pubmed_authors>Shao Y</pubmed_authors><pubmed_authors>Wang T</pubmed_authors><pubmed_authors>Chen W</pubmed_authors><pubmed_authors>Tu Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks.</name><description>The present study aims to investigate the effects of ultrasound on the non-covalent interaction of β-lactoglobulin (β-LG) and luteolin (LUT) and to investigate the relationship between allergenicity and human intestinal microbiota. After treatment, the conformational structures of β-LG were changed, which reflected by the decrease in α-helix content, intrinsic fluorescence intensity and surface hydrophobicity, whereas the β-sheet content increased. Molecular docking studies revealed the non-covalent interaction of β-LG and LUT by hydrogen bond, van der Walls bond and hydrophobic bond. β-LG-LUT complex treated by ultrasound has a lower IgG/IgE binding ability and inhibits the allergic reaction of KU812 cells, depending on the changes in the conformational epitopes of β-LG. Meanwhile, the β-</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Mar</publication><modification>2025-04-26T13:05:42.337Z</modification><creation>2025-04-06T14:09:41.147Z</creation></dates><accession>S-EPMC8997858</accession><cross_references><pubmed>35407075</pubmed><doi>10.3390/foods11070988</doi></cross_references></HashMap>