Abstract
An organic phase containing reversed micelles of Cibacron Blue F-3GA modified lecithin (CB-lecithin) was attached to microporous polypropylene hollow-fiber membranes. This led to the formation of a hollow-fiber column with immobilized dye-affinity reversed micelles within the membrane pores as the stationary phase. This column for chromatographic separation of proteins was called hollow-fiber affinity partitioning chromatography (HFAPC). With a column of 3 mL in net hollow fiber volume, lysozyme and bovine serum albumin (BSA) could be completely separated, and HFAPC experiments with overloaded lysozyme/BSA mixtures yielded a lysozyme fraction with a purity of 93.5% and a high yield. Furthermore, lysozyme was purified by the HFAPC from a crude chicken egg-white solution containing 9.56 mg proteins with a recovery yield of 98.2%. The purity of the lysozyme fraction was increased by 47.4-fold, reaching 85.3% of the total proteins.
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