Abstract: Magnetosomes synthesized by magnetotactic bacteria were drawn great interest as potential carriers to couple with diverse bioactive macromolecules, anticancer drugs and enzymes due to their unique features such as paramagnetism, nano-scale, narrow size distribution and membrane-bounded. However, it was rarely mentioned on the separation of glycoproteins using magnetosomes. In this paper, the magnetosomes were extracted from Magnetospirillum gryphiswaldense MSR-1, modified with phosphatidylethanolamine (PE), coupled with Bis (sulfoduccinimidyl) suberate sodium salt (BS3), and ligated with lectin, sequentially. Lectin-PE-magnetosome complexes were prepared and used for the separation of glycoproteins. The results showed that the proteins on magnetosomes surface were removed, and modified PE-magnetosomes showed the better dispersion than native magnetosomes. Moreover, 294.64 μg of wheat germ agglutinin (WGA) were coupled to one milligram of PE-magnetosomes, 1.6 times than that coupled to one milligram of magnetosomes. WGA-PE-magnetosomes could specifically separate the ovalbumin (OVA) from the mixture of OVA and Concanavalin A (ConA). In all, it has the great potential application in separation and enrichment of glycoproteins and used in the glycomics.

Key words: magnetosome, lectin, glycoprotein, separation