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Protein-Polyphenol Complexation to Reduce Food Protein Allergenicity

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개인저자Plundrich, Nathalie Jennifer.
단체저자명North Carolina State University. Food Science.
서명/저자사항Protein-Polyphenol Complexation to Reduce Food Protein Allergenicity.
발행사항[S.l.] : North Carolina State University., 2018
발행사항Ann Arbor : ProQuest Dissertations & Theses, 2018
형태사항228 p.
소장본 주기School code: 0155.
ISBN9780438283954
일반주기 Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
Advisers: Mary Ann Lila
요약Food allergy is a worldwide health concern. Peanuts are among the "big eight" foods that can cause food allergy, and has been cited as one of the most serious and prevalent. Peanut allergy is an immunoglobulin (Ig) E-mediated hypersensitivity di
요약Plant polyphenols are known for their natural ability to bind proteins. In previous studies, we have described a new approach to bind fruit juice- and herbal extract-derived polyphenols to peanut proteins (in the form of peanut flour), and demon
요약In the first study, we created peanut protein-polyphenol aggregate particles containing different concentrations of polyphenols derived from cranberry (Vaccinium macrocarpon Ait.) and lowbush blueberry ( Vaccinium angustifolium Ait.) pomaces. Im
요약One of the main peanut allergens bound by blueberry and cranberry polyphenols was Ara h 2. While our previous investigations have shown the potential of using polyphenol binding as a way to mediate allergenicity, the activities of individual pol
요약Collectively, these findings suggest that different classes of polyphenols can both non-covalently and covalently bind to peanut allergens and consequently inhibit epitope binding by epitope-specific IgE, presenting a potential strategy for alle
일반주제명Food science.
Immunology.
언어영어
기본자료 저록Dissertation Abstracts International79-12B(E).
Dissertation Abstract International
대출바로가기http://www.riss.kr/pdu/ddodLink.do?id=T15001291

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