کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8328925 1540207 2018 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Cross-linked ovalbumin catalyzed by polyphenol oxidase: Preparation, structure and potential allergenicity
ترجمه فارسی عنوان
ابلوبوم متقاطع خورده شده توسط پلی فنول اکسیداز: تهیه، ساختار و آلرژیزاسیون بالقوه
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی
Ovalbumin (OVA) is described as one of the major allergens in hen's egg, and it is the most abundant protein in egg white. Enzyme-mediated covalent cross-linking of food proteins, can influence their structure and allergenicity. The aim of this study was to investigate the potential of polyphenol oxidase from Agaricus bisporus to cross-link OVA (CL-OVA) in the presence or absence of caffeic acid, followed by characterizing the structure and allergenicity of CL-OVA. A single-factor experiment was designed to assess the optimum conditions for cross-linking of OVA by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Under the optimal conditions, structural changes in OVA were analyzed by circular dichroism, ultraviolet and fluorescence spectra. It was shown that CL-OVA became unordered and unfolded, and more tyrosine and tryptophan residues and hydrophobic groups were exposed onto the surface of molecules when compared to the native OVA. Enzyme-linked immunosorbent assay indicated that IgG and IgE binding abilities to OVA significantly reduced after cross-linking. All the findings demonstrated that enzymatic cross-linking in the presence of caffeic acid as a mediator may decrease the antigenicity and potential allergenicity, and the changes of the modified OVA were most likely a consequence of some changes or adjustment in the local conformation of OVA and the epitopes of OVA by cross-linking.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 107, Part B, February 2018, Pages 2057-2064
نویسندگان
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