R phycoerythrin, a light harvesting protein in some marine algae, and can be widely used in medicine, was isolated and purified from a red alga, Palmaria palmata (Lannaeus) Kuntze, using the streamline column (expanded bed adsorption) combined with ion exchange chromatography. Because the crude extract was applied to the column upwardly, the column would not be blocked by polysaccharides usually very abundant in the extract of marine alga, this kind of blockage could hardly be overcome in ordinary chromatographic column. After applying the crude extract containing 0.5 mol/L (NH4)2SO4, (NH4)2SO4 solution of different concentrations (0.2 mol/L, 0.1 mol/L and 0.05 mol/L) was used to elute the column downwardly and the eluates were collected and desalted. The desalted eluates were then applied onto an ion exchange chromatographic column loaded with Qsepharose for further purification of the R phycoerythrin. Through these two steps, the purity ( OD565/OD280) of the R phycoerythrin from P． palmata was up to 3.5, more than 3.2, the commonly accepted criterion for purity, and the yield of the purified R phycoerythrin could reach 0.122 mg/g of frozen P. palmata, much higher than that of phycobiliproteins purified with the previous methods. The result indicated that the cost of R phycoerythrin will drop down with the method reported in this article.
用膨化柱填料的方法从红藻中规模分离纯化
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