Lectins have potential for application in many fields because of their ability to selectively bind glycoconjugates. Jackfruit seeds are a source of various lectins, with several isoforms and isoelectric points. Therefore, ion exchange can be a viable alternative for lectin separation. In this work we developed a single-step purification protocol for lectins from jackfruit seed extract in ion exchange cryogels. Supermacroporous cryogels were functionalized with cationic and anionic exchangers. The matrices produced showed high swelling capacity (12.4 and 14.7 kg kg-1), expansion degree (12.70 to 18.0 L kg-1), and total porosity around 90%. The performance of the ion exchanger cryogels in lectin purification were evaluated. A single elution peak was obtained in all assays. The purification factor (PF) was determined based on the agglutination of human blood ABO types, with a PF of 3.57 in the best condition, using the cryogel functionalized with 2-(Dimethylamino)ethyl methacrylate (DMAEMA) and blood type B agglutination, suggesting the jacalin purification. SDS-PAGE electrophoresis confirmed that the eluted samples showed two strong bands around 13.5 kDa and 16 kDa. The results demonstrate that ion-exchange monolithic cryogels showed potential use for the purification of lectins from jackfruit seeds in a rapid and single-step protocol. Las lectinas tienen potencial para aplicación en diversos campos por su habilidad de enlazar glicoconjugados selectivamente. Las semillas de yaca son una fuente de lectinas, con diferentes isoformas y puntos isoeléctricos. Así, el intercambio iónico es una alternativa para la separación de lectinas. En este trabajo, desarrollamos un protocolo de purificación para extracto de semillas de yaca en criogeles de intercambio iónico (catiónicos y aniónicos). Las matrices producidas demostraron alta capacidad de hinchamiento (12,4 a 14,7 kg kg-1), grado de expansión (12,70 a 18,0 L kg-1) y porosidad total de un 90%. Se evaluó el desempeño de las matrices en la purificación de lectina. Se obtuvo un único pico de elución en todos los ensayos. Se determinó el factor de purificación (FP) con base en la aglutinación de sangre humana de tipos ABO, con un FP de 3,57 bajo las mejores condiciones, usando un criogel funcionalizado con metacrilato de 2-dimetilaminoetilo y aglutinación de sangre tipo B, lo que sugirió la purificación de jacalina. La electroforesis SDS-PAGE confirmó que las muestras eluidas presentaron dos bandas fuertes de 13,5 kDa y 16 kDa. Los resultados demostraron que las matrices presentaron uso potencial para la purificación parcial de lectinas de semillas de yaca.

Growing medical, engineering, biochemical, and biological interest has led to a steady pace of research and development into polymeric monolithic structures with densely interconnected pores for purifying bio compounds. Cryogels, which are generated by freezing a reactive polymerization mixture, are highlighted due to their versatility and low relative cost as macroporous, polymeric, monolithic adsorbents. The conversion of cryogels into affinity adsorbents is one possible alternative to their optimal application. Some of the most often utilized supports for immobilizing particular ligands are monolithic columns manufactured with epoxy radicals on their surfaces. The purification of biomolecules with a high degree of specificity, such as lectins and glycoproteins with an affinity for glycosylated groups, has garnered interest in the use of fixed non-traditional beds functionalized with ligands of particular interest. The interaction is both robust enough to permit the adsorption of glycoproteins and reversible enough to permit the dissociation of molecules in response to changes in the solution’s pH. When compared to other protein A-based approaches, this one has been shown to be more advantageous than its counterparts in terms of specificity, ease of use, and cost-effectiveness. Information on polymeric, macroporous, monolithic adsorbents used in the affinity chromatographic purification of lectins has been published and explored.