Artículos de revistas
The effect of transglutaminase-induced polymerization in the presence of cysteine on beta-lactoglobulin antigenicity
Registro en:
International Dairy Journal. Elsevier Sci Ltd, v. 20, n. 6, n. 386, n. 392, 2010.
0958-6946
WOS:000278166400002
10.1016/j.idairyj.2010.01.004
Autor
Villas-Boas, MB
Vieira, KP
Trevizan, G
Zollner, RD
Netto, FM
Institución
Resumen
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) 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. 20 6 386 392 FAEPEX-Unicamp Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)