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dc.creatorBenedini, Leandro J.-
dc.creatorFigueiredo, Douglas-
dc.creatorCabrera-Crespo, Joaquin-
dc.creatorGonçalves, Viviane M.-
dc.creatorSilva, Gabriel G.-
dc.creatorCampani, Gilson-
dc.creatorZangirolami, Teresa C.-
dc.creatorFurlan, Felipe F.-
dc.date.accessioned2020-04-20T19:50:12Z-
dc.date.available2020-04-20T19:50:12Z-
dc.date.issued2020-02-
dc.identifier.citationBENEDINI, L. J. et al. Modeling and simulation of anion exchange chromatography for purification of proteins in complex mixtures. Journal of Chromatography A, [S.l.], v. 1613, Feb. 2020.pt_BR
dc.identifier.urihttps://www.sciencedirect.com/science/article/abs/pii/S0021967319311148pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/40208-
dc.description.abstractIon 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.pt_BR
dc.languageen_USpt_BR
dc.publisherElsevierpt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceJournal of Chromatography Apt_BR
dc.subjectProtein purificationpt_BR
dc.subjectAnion exchange chromatographypt_BR
dc.subjectMathematical modelingpt_BR
dc.subjectComplex protein mixturept_BR
dc.subjectSteric mass action isothermpt_BR
dc.subjectEquilibrium dispersive modelpt_BR
dc.titleModeling and simulation of anion exchange chromatography for purification of proteins in complex mixturespt_BR
dc.typeArtigopt_BR
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