Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography

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...

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Huvudupphovsmän: 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
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spelling ri-123456789-324822021-05-10T19:50:35Z Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography 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 Expanded bed adsorption Leishmania infantum chagasi Recombinant protein purification Unclarified bacterial homogenate Visceral leishmaniasis 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 2021-05-10T19:50:34Z 2021-05-10T19:50:34Z 2015-04-01 article 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 1570-0232 https://repositorio.ufrn.br/handle/123456789/32482 10.1016/j.jchromb.2015.01.031 en Attribution 3.0 Brazil http://creativecommons.org/licenses/by/3.0/br/ application/pdf Elsevier
institution Repositório Institucional
collection RI - UFRN
language English
topic Expanded bed adsorption
Leishmania infantum chagasi
Recombinant protein purification
Unclarified bacterial homogenate
Visceral leishmaniasis
spellingShingle Expanded bed adsorption
Leishmania infantum chagasi
Recombinant protein purification
Unclarified bacterial homogenate
Visceral leishmaniasis
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
Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
description 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
format article
author 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
author_facet 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
author_sort Santos, Everaldo Silvino dos
title Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
title_short Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
title_full Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
title_fullStr Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
title_full_unstemmed Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
title_sort recovery and purification of recombinant 503 antigen of leishmania infantum chagasi using expanded bed adsorption chromatography
publisher Elsevier
publishDate 2021
url https://repositorio.ufrn.br/handle/123456789/32482
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