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https://locus.ufv.br//handle/123456789/19645
Tipo: | Artigo |
Título: | Binding thermodynamics of synthetic dye Allura Red with bovine serum albumin |
Autor(es): | Lelis, Carini Aparecida Hudson, Eliara Acipreste Ferreira, Guilherme Max Dias Ferreira, Gabriel Max Dias Silva, Luis Henrique Mendes da Silva, Maria do Carmo Hespanhol da Pinto, Maximiliano Soares Pires, Ana Clarissa dos Santos |
Abstract: | The interaction between Allura Red and bovine serum albumin (BSA) was studied in vitro at pH 7.4. The fluorescence quenching was classified as static quenching due to the formation of AR–BSA complex, with binding constant (K) ranging from 3.26 ± 0.09 to 8.08 ± 0.06 104 L.mol−1, at the warfarin binding site of BSA. This complex formation was driven by increasing entropy. Isothermal titration calorimetric measurements also showed an enthalpic contribution. The Allura Red diffusion coefficient determined by the Taylor-Aris technique corroborated these results because it reduced with increasing BSA concentration. Interfacial tension measurements showed that the AR–BSA complex presented surface activity, since interfacial tension of the water-air interface decreased as the colorant concentration increased. This technique also provided a complexation stoichiometry similar to those obtained by fluorimetric experiments. This work contributes to the knowledge of interactions between BSA and azo colorants under physiological conditions. |
Palavras-chave: | Fluorescence Interfacial tension Diffusion coefficient Enthalpy Synthetic food dye |
Editor: | Food Chemistry |
Tipo de Acesso: | Elsevier Ltd. |
URI: | https://doi.org/10.1016/j.foodchem.2016.08.080 http://www.locus.ufv.br/handle/123456789/19645 |
Data do documento: | 15-Fev-2017 |
Aparece nas coleções: | Artigos |
Arquivos associados a este item:
Arquivo | Descrição | Tamanho | Formato | |
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artigo.pdf Until 2100-12-31 | Texto completo | 522,9 kB | Adobe PDF | Visualizar/Abrir ACESSO RESTRITO |
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