Desenvolvimento e caracterização de trocador catiônico supermacroporoso para a purificação de macromoléculas

• Autor(a) principal: Fontan, Rafael da Costa Ilhéu
• Data de Publicação: 2013
• Tipo de documento: Tese
• Idioma: por
• Título da fonte: LOCUS Repositório Institucional da UFV
• Texto Completo: http://locus.ufv.br/handle/123456789/472
• topic: Adsorção; Criogel; Coluna monolítica; Troca iônica; Lisozima; Adsorption; Cryogel; Monolithic column; Ion exchange; Lysozyme; CNPQ::CIENCIAS AGRARIAS::CIENCIA E TECNOLOGIA DE ALIMENTOS::TECNOLOGIA DE ALIMENTOS

Researchers around the world are interested in the potential use of biomolecules, in special macromolecules, increasing the application of different techniques to purify its. New methodologies and materials are being developed, such as polymeric cryogels, considered the new generation of chromatographic matrices. Cryogels permit the production of high porosity monolithic columns with large pores that allow the passage even of whole cells, which is highly desirable for the macromolecules purification from viscous and non-clarified feedstock solutions. Despite the growing interest in cryogels, studies involving equilibrium conditions and the dynamics of fluid displacement and mass transfer in monolithic beds are still insufficient to adequately characterize this class of adsorbents. Thus, a new ion exchanger monolithic cryogel for the purification of lysozyme from chicken egg was produced and characterized at various aspects, as the physical structure and adsorption equilibrium relationships, including the effect of temperature and ionicstrength of the mobile phase, allowing a better understanding of the adsorptive mechanism of lysozyme on the ion exchanger. The monolithic bed was also characterized as the capillary hydrodynamic and a model was proposed to describe the breakthrough curves, allowing greater understanding of dispersive, diffusive and mass transfer effects. Finally, monolithic bed produced was successfully employed in the purification of lysozyme directly from egg white in a single chromatographic step, being possible its use with a minimum preparation of the feed solution.