Abstract
AbstractConcanavalin A, one of most studied lectins for the purification of glycoproteins and sugars, is selected as a model protein. In this study, a Concanavalin A imprinted poly(hydroxyethyl methacrylate) supermacroporous cryogel was prepared for the purification of Concanavalin from jack bean extract. N‐Methacryloyl‐l‐histidine methyl ester with nickel(II) ions was used as the metal ion coordination complex. Concanavalin A imprinted cryogels were characterized by swelling degree, surface area, Fourier transform infrared spectroscopy, scanning electron microscopy and micro computed tomography measurements. Concanavalin A rebinding and desorption on Concanavalin A imprinted and non‐imprinted cryogels were measured using a continuous system. Selective binding studies were carried out in the presence of Concanavalin B and bovine serum albumin. The selectivity studies were confirmed by fast protein liquid chromatography studies using jack bean extract from Canavalia ensiformis.
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