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|Type:||Artigo de periódico|
|Title:||The effect of transglutaminase-induced polymerization in the presence of cysteine on beta-lactoglobulin antigenicity|
|Abstract:||The effect of polymerization by the enzyme transglutaminase (TG) on the antigenicity of beta-lactoglobulin (beta-Lg) was investigated. Polymerization was carried out using 7% heat treated beta-Lg and 5-50 U TG g(-1), substrate or 7% untreated beta-Lg in the presence of 0.05-0.4 mol L(-1) cysteine (Cys) and 25 U TG g(-1) substrate. The electrophoretic profile of polymerized samples showed bands corresponding to high molecular mass. For antigenicity evaluation, sera from BALB/c mice sensitized with native beta-Lg, beta-Lg polymerized by 25 U TG g(-1) (beta-Lg HT TG) or polymerized in 0.25 mol L(-1) Cys (beta-Lg Cys TG) were used. Animals sensitized with beta-Lg Cys TG showed lower levels of IgG1 and IgE than those immunized with native beta-Lg or beta-Lg HT TG. These results suggested that polymerization in the presence of Cys modified or hid epitopes, reducing the potential antigenicity of beta-Lg, whereas heat treatment followed by polymerization did not lead to a reduction in antigenicity. (C) 2010 Elsevier Ltd. All rights reserved.|
|Editor:||Elsevier Sci Ltd|
|Appears in Collections:||Artigos e Materiais de Revistas Científicas - Unicamp|
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