자료유형 | 학위논문 |
---|---|
서명/저자사항 | Protein-Polyphenol Complexation to Reduce Food Protein Allergenicity. |
개인저자 | Plundrich, Nathalie Jennifer. |
단체저자명 | North Carolina State University. Food Science. |
발행사항 | [S.l.]: North Carolina State University., 2018. |
발행사항 | Ann Arbor: ProQuest Dissertations & Theses, 2018. |
형태사항 | 228 p. |
기본자료 저록 | Dissertation Abstracts International 79-12B(E). Dissertation Abstract International |
ISBN | 9780438283954 |
학위논문주기 | Thesis (Ph.D.)--North Carolina State University, 2018. |
일반주기 |
Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
Advisers: Mary Ann Lila |
요약 | Food 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 |
요약 | Plant 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 |
요약 | In 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 |
요약 | One 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 |
요약 | Collectively, 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 |
일반주제명 | Food science. Immunology. |
언어 | 영어 |
바로가기 |
: 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |