{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T03:45:38Z","timestamp":1791431138745,"version":"4.3.3"},"reference-count":41,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2022,12,14]],"date-time":"2022-12-14T00:00:00Z","timestamp":1670976000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Key R&amp;D Program of China","award":["(2021YFD2100702)"],"award-info":[{"award-number":["(2021YFD2100702)"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Foods"],"abstract":"<jats:p>As the main allergens in milk, whey proteins are heat-sensitive proteins and are widespread in dairy products and items in which milk proteins are involved as food additives. The present work sought to investigate the effect of heating sterilization on the allergenicity of \u03b1-lactalbumin (\u03b1-LA) and \u03b2-lactoglobulin (\u03b2-LG), the main composite and allergen in whey protein isolate (WPI), by combining molecular dynamics with experimental techniques for detecting the spatial structure and IgE binding capacity. The structure of WPI was basically destroyed at heat sterilization conditions of 95 \u00b0C for 5 min and 65 \u00b0C for 30 min by SDS-PAGE analysis and spectroscopic analysis. In addition, \u03b1-lactalbumin (\u03b1-LA) may be more sensitive to temperature, resulting in exposure to allergic epitopes and increasing the allergic potential, while the binding capacity of \u03b2-lactoglobulin (\u03b2-LG) to IgE was reduced under 65 \u00b0C for 30 min. By the radius of gyration (Rg) and root-mean-square deviation (RMSD) plots calculated in molecular dynamics simulations, \u03b1-LA was less structurally stable at 368 K, while \u03b2-LG remained stable at higher temperatures, indicating that \u03b1-LA was more thermally sensitive. In addition, we observed that the regions significantly affected by temperatures were associated with the capacity of allergic epitopes (\u03b1-LA 80\u2013101 and \u03b2-LG 82\u201393, 105\u2013121) to bind IgE through root-mean-standard fluctuation (RMSF) plots, which may influence the two major allergens. We inferred that these regions are susceptible to structural changes after sterilization, thus affecting the allergenicity of allergens.<\/jats:p>","DOI":"10.3390\/foods11244050","type":"journal-article","created":{"date-parts":[[2022,12,15]],"date-time":"2022-12-15T02:20:57Z","timestamp":1671070857000},"page":"4050","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Investigation of the Structure and Allergic Potential of Whey Protein by Both Heating Sterilization and Simulation with Molecular Dynamics"],"prefix":"10.3390","volume":"11","author":[{"given":"Zhao","family":"Zhang","sequence":"first","affiliation":[{"name":"School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruida","family":"Ma","sequence":"additional","affiliation":[{"name":"School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunpeng","family":"Xu","sequence":"additional","affiliation":[{"name":"School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lei","family":"Chi","sequence":"additional","affiliation":[{"name":"Dalian Women and Children Medical Center, Dalian 116012, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yue","family":"Li","sequence":"additional","affiliation":[{"name":"Dalian Women and Children Medical Center, Dalian 116012, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9356-753X","authenticated-orcid":false,"given":"Guangqing","family":"Mu","sequence":"additional","affiliation":[{"name":"School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9667-3311","authenticated-orcid":false,"given":"Xuemei","family":"Zhu","sequence":"additional","affiliation":[{"name":"School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,14]]},"reference":[{"key":"ref_1","first-page":"305","article-title":"Nature\u2019s Perfect Food: How Milk Became America\u2019s Drink","volume":"68","author":"Guptill","year":"2003","journal-title":"Rural Sociol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1016\/j.jaci.2008.12.1125","article-title":"Accidental allergic reactions in children allergic to cow\u2019s milk proteins","volume":"123","author":"Pedrosa","year":"2009","journal-title":"J. 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