Abstract
Immobilized lectins are a powerful biotechnological tool for separation and isolation of glycoconjugates. In the present study, polyvinyl alcohol (PVA) and glutaraldehyde (GA) were used as a support for Concanavalin A (Con A) covalent immobilization and for entrapment of Parkia pendula seed gum (PpeG). Con A immobilization yielded approximately 30% and 0.6 M glucose solution was the minimum concentration able to elute fetuin from column. PVA-GA-PpeG column was efficiently recognized by pure P. pendula lectin (PpeL). These findings indicate that PVA-GA interpenetrated network showed to be an efficient support for lectin covalent immobilization and as affinity chromatography matrix after trapping of PpeG.
Highlights
Immobilization of native proteins, retaining their biological activity, onto solid support is often a crucial step for a variety of biochemical and biotechnological assays (Eş, Vieira, & Amaral, 2015)
When Concanavalin A (Con A) was immobilized under stirring with Polyvinyl alcohol (PVA)-GA, yield immobilization decreased to approximately 18%
PVA-GA-Con A support was used as affinity chromatography column for fetuin and the purification efficiency obtained was 11%
Summary
Immobilization of native proteins, retaining their biological activity, onto solid support is often a crucial step for a variety of biochemical and biotechnological assays (Eş, Vieira, & Amaral, 2015). In this sense, lectins can be employed immobilized onto these supports for affinity purification of glycoconjugates by selective capture of glycan or glycoconjugates (Brooks, 2009). Lectins are ubiquitous and can bind reversibly, non-covalently to carbohydrates and agglutinate cells and/or precipitate glycoconjugates. They are widely used experimentally in glycobiochemistry and cell biology, e.g., in separation of various biological compounds and cells (Ghazarian, Idoni, & Oppenheimer, 2011). Concanavalin A (Con A) is a glucose-binding legume lectin long-studied and has been used for fractionation and structural analysis of oligosaccharides and glycoproteins (Li, Yu, Xu, & Bao, 2011, Shastri et al, 2015, Huang et al, 2016)
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