Purificação de proteínas por cromatografia: o estado da arte
Data
2023-11-30
Autores
Ferraro, Victor Thiago 
Costa, Cláudio Armando Lopes
Orientadores
Bresolin, Iara Rocha Antunes Pereira
Tipo
Trabalho de conclusão de curso
Título da Revista
ISSN da Revista
Título de Volume
Resumo
Neste trabalho de caráter descritivo foi abordado o estado da arte para purificação de proteínas,
por cromatografia. As proteínas são macromoléculas biológicas que desempenham um papel
vital no crescimento celular, desenvolvimento, hereditariedade, movimento, reprodução e
outras atividades da vida, tendo um papel importante no ramo farmacêutico devido ao seu
enorme poder catalítico e de especificidade. Essa pesquisa teve como objetivo analisar
diferentes técnicas cromatográficas para a purificação de proteínas, assim como as suas
propriedades e aplicações. De acordo com o estudo bibliográfico desenvolvido foi possível
mostrar como as proteínas interagem em relação as diversas técnicas cromatográficas
empregues. Para o embasamento teórico desse trabalho utilizou se pesquisas de diversos autores
e recentes. Os métodos utilizados nessa pesquisa foram uma linha de tempo relacionada as
pesquisas publicadas e uma busca avançada em artigos, pesquisas de teses, livros em bases de
dados como web of science e no google acadêmico. Por fim na pesquisa foi utilizada um estudo
de caso onde abordou-se de forma clara sobre a purificação da enzima β-galactosidase,
utilizando a cromatografia de troca iônica em um leito fixo. Os resultados mostraram que a
força iônica exerceu maior influência na purificação de dobras . A fração β-gal em eluição
usando 0,1-0,4 M de NaCl apresentou rendimento de 51,65 ± 0,17% e FP de 2,00 ± 0,43. Estes
resultados apontam para a recuperação de uma β-gal estável.
In this descriptive work, the state of the art for protein purification by chromatography was addressed. Proteins are biological macromolecules that play a vital role in cell growth, development, heredity, movement, reproduction and other life activities, playing an important role in the pharmaceutical field due to their enormous catalytic power and specificity. This research aimed to analyze different chromatographic techniques for protein purification, as well as their properties and applications. According to the bibliographic study developed, it was possible to show how proteins interact in relation to the different chromatographic techniques used. For the theoretical basis of this work, research from several recent authors was used. The methods used in this research were a timeline related to published research and an advanced search in articles, thesis research, books in databases such as web of science and Google Scholar. Finally, a case study was used in the research, which clearly addressed the purification of the β-galactosidase enzyme, using ion exchange chromatography in a fixed bed. The results showed that ionic strength exerted the greatest influence on fold purification. The β-gal fraction eluting using 0.1-0.4 M NaCl showed a yield of 51.65 ± 0.17% and FP of 2.00 ± 0.43.These results point to the recovery of a β -gal stable.
In this descriptive work, the state of the art for protein purification by chromatography was addressed. Proteins are biological macromolecules that play a vital role in cell growth, development, heredity, movement, reproduction and other life activities, playing an important role in the pharmaceutical field due to their enormous catalytic power and specificity. This research aimed to analyze different chromatographic techniques for protein purification, as well as their properties and applications. According to the bibliographic study developed, it was possible to show how proteins interact in relation to the different chromatographic techniques used. For the theoretical basis of this work, research from several recent authors was used. The methods used in this research were a timeline related to published research and an advanced search in articles, thesis research, books in databases such as web of science and Google Scholar. Finally, a case study was used in the research, which clearly addressed the purification of the β-galactosidase enzyme, using ion exchange chromatography in a fixed bed. The results showed that ionic strength exerted the greatest influence on fold purification. The β-gal fraction eluting using 0.1-0.4 M NaCl showed a yield of 51.65 ± 0.17% and FP of 2.00 ± 0.43.These results point to the recovery of a β -gal stable.