1. Universidade Federal do Rio Grande do Norte
2. Centro de Tecnologia
3. DEQ - Departamento de Engenharia Química
4. CT - DEQ - Artigos publicados em periódicos

Título:	Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
Autor(es):	Santos, Everaldo Silvino dos Sousa Junior, Francisco Caninde de Vaz, Michelle Rossana Ferreira Padilha, Carlos Eduardo de Araújo Chibério, Abimaelle Silva Martins, Daniella Regina Arantes Macedo, Gorete Ribeiro de
Palavras-chave:	Expanded bed adsorption;Leishmania infantum chagasi;Recombinant protein purification;Unclarified bacterial homogenate;Visceral leishmaniasis
Data do documento:	1-Abr-2015
Editor:	Elsevier
Referência:	SOUSA JUNIOR, F. C.; VAZ, M. R. F.; PADILHA, C. E.; CHIBERIO, A. S.; MARTINS, D. R. A.; MACEDO, G. R.; SANTOS, E. S.. Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography. Journal of Chromatography. B (Print), p. 1, 2015. Disponivel em https://www.sciencedirect.com/science/article/abs/pii/S1570023215000719?via%3Dihub. Acesso em: 01 abr. 2021. https://doi.org/10.1016/j.jchromb.2015.01.031
Resumo:	Visceral leishmaniasis, a disease caused by Leishmania infantum chagasi, represents a major public health problem in many areas of the world. However, there is currently no vaccine for human use. The aim of this work was to purify the 503 antigen of Leishmania i. chagasi directly from unclarified Escherichia coli feedstock through expanded bed adsorption (EBA) chromatography. Batch experiments were performed to optimize the adsorption and elution conditions of the antigen onto a STREAMLINETM Chelating resin using two central composite rotatable designs (CCRD). The results showed that the optimal binding con- ditions of the 503 antigen were pH 8.0 in the presence of 2.4 M NaCl. For the elution of the target protein, the optimized conditions included the presence of 600.0 mM imidazole. The adsorption isothermal data of the 503 antigen were fitted to the Langmuir adsorption isotherm. The EBA experiment successfully recovered 59.2% of the 503 antigen from the unclarified E. coli homogenate with a purification factor of 6.0
URI:	https://repositorio.ufrn.br/handle/123456789/32482
ISSN:	1570-0232
Aparece nas coleções:	CT - DEQ - Artigos publicados em periódicos

Este item está licenciada sob uma Licença Creative Commons