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Purification of oligouronides by immobilized L-histidine pseudoaffinity chromatography

C. Delattre, A.S. Kamalanathan, P. Michaud, M.A. Vijayalakshmi

Journal of Chromatography B, 861 (2008) 181–185

Selective purification of alpha-(1,4)-oligogalacturonides was investigated using several pseudobioaffinity chromatography matrix with aminoacid
L-histidine as pseudobiospecific ligand: (1) sepharose 4B-bisoxyran-histidine, (2) sepharose 4B-epoxy-histidine, (3) silica-oxyran-histidine and
(4) CIM-disk-EDA-histidine. These anionic oligosaccharides prepared by enzymatic and chemical cleavage of polygalacturonic acid were used
as models sugar in order to optimize the adsorption and elution parameters for a selective purification of bioactive oligouronides. Monolithic
CIM-disk chromatography is one of the fastest liquid chromatographic method using for separation and purification of biomolecules thanks to high
mass transfer rate. In this way, this new monolithic CIM-disk system with l-histidine immobilized: immobilized histidine affinity chromatography
(IHAC) constitutes a good tool allowing the fast and selective purification of bioactive oligouronides.

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