Modeling and simulation of anion exchange chromatography for purification of proteins in complex mixtures

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorBenedini, Leandro J.-
Autor(es): dc.creatorFigueiredo, Douglas-
Autor(es): dc.creatorCabrera-Crespo, Joaquin-
Autor(es): dc.creatorGonçalves, Viviane M.-
Autor(es): dc.creatorSilva, Gabriel G.-
Autor(es): dc.creatorCampani, Gilson-
Autor(es): dc.creatorZangirolami, Teresa C.-
Autor(es): dc.creatorFurlan, Felipe F.-
Data de aceite: dc.date.accessioned2026-02-09T12:34:30Z-
Data de disponibilização: dc.date.available2026-02-09T12:34:30Z-
Data de envio: dc.date.issued2020-04-20-
Data de envio: dc.date.issued2020-04-20-
Data de envio: dc.date.issued2020-01-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/40208-
Fonte completa do material: dc.identifierhttps://www.sciencedirect.com/science/article/abs/pii/S0021967319311148-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1164038-
Descrição: dc.descriptionIon exchange chromatography is extensively used in the purification of biological compounds. Reliable mathematical models describing this chromatographic technique are available and can be used to improve the performance of this separation step. However, the use of synthetic mixtures for model development hampers the application of this approach with real cell extracts processed in downstream operations. This work presents an original approach for handling non-synthetic genuine mixtures of proteins, which was applied in the purification of an untagged recombinant pneumococcal surface protein A (PspA4Pro). First, evaluation was made of the efficiency of steric mass action (SMA) and modified Langmuir isotherms, which were separately used together with the equilibrium dispersive model (EDM). The data used for parameter estimation and model validation were obtained from anion exchange chromatography runs (employing Q-Sepharose FF), applied to real cell extracts produced by different cultivation strategies. Simulations showed that the models were able to describe the complex mixtures of unknown proteins. Next, the EDM and SMA approaches were used to separately describe the profile of PspA4Pro and the pool of protein impurities eluted together. The simulations showed that PspA4Pro tended to elute at the beginning of the peak, enabling the establishment of an alternative elution schedule that provided a 34% increase in the purity achieved using the anion exchange chromatography.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceJournal of Chromatography A-
Palavras-chave: dc.subjectProtein purification-
Palavras-chave: dc.subjectAnion exchange chromatography-
Palavras-chave: dc.subjectMathematical modeling-
Palavras-chave: dc.subjectComplex protein mixture-
Palavras-chave: dc.subjectSteric mass action isotherm-
Palavras-chave: dc.subjectEquilibrium dispersive model-
Título: dc.titleModeling and simulation of anion exchange chromatography for purification of proteins in complex mixtures-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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